NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1207153289|ref|XP_021324032|]
View 

rho-associated protein kinase 2b isoform X2 [Danio rerio]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
51-402 0e+00

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 737.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   51 NKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIM 130
Cdd:cd05596      1 NKNIENFLNRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  131 AFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR 210
Cdd:cd05596     81 AHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  211 NGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYG 290
Cdd:cd05596    161 SGHLKLADFGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  291 KIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNF 370
Cdd:cd05596    241 KIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1207153289  371 dDDIKDDPIGTETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05596    321 -DDIEEDETPEETFPVPKAFVGNHLPFVGFTY 351
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1212-1316 3.78e-49

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269948  Cd Length: 110  Bit Score: 169.84  E-value: 3.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1212 LEGWLSMPAK-NTKRFGWDKKYVVVSSKKILFYDSEQDREQSSPFMILDIDKLFHVRPVTQTDVYRADPREIPRIFQILY 1290
Cdd:cd01242      3 LEGWLSLPNKqNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQILY 82
                           90       100
                   ....*....|....*....|....*...
gi 1207153289 1291 ANEGESKKEE--LPVESLSVTERSLCIP 1316
Cdd:cd01242     83 ANEGESSRPAevTDTLSVSREEKPNTIL 110
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1310-1379 9.26e-42

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410425  Cd Length: 71  Bit Score: 147.49  E-value: 9.26e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1310 ERSLCIPHKGHEFVLTLYHFPSSCEVCPRPLWHVFRPPPALECRRCRVKCHKDHIDRKEEVLAPCRVNYD 1379
Cdd:cd20875      2 EKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
429-1138 7.64e-27

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 119.39  E-value: 7.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKA 508
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 GLETDRKRLLENEVSSLKEQLAELKkknqishlsaEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSL 588
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLE----------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  589 RELQERLAQLENSRLVLEQDKLSLQTslELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTL 668
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 EKEKNKqeidLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN-------QSIEAKSETLKDMEhKLLEERsakqqLENR 741
Cdd:TIGR02168  481 ERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIE-AALGGR-----LQAV 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  742 LMqlEKENSVLDCDYKQAKHELQ-----------------ELRSLKENLTEQVEVLNVRVQQET---------------- 788
Cdd:TIGR02168  551 VV--ENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPklrkalsyllggvlvv 628
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  789 --------QRK---------TLcQGDL----KVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQL 847
Cdd:TIGR02168  629 ddldnaleLAKklrpgyrivTL-DGDLvrpgGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  848 KEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDL 927
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  928 EKEkimkeleikdmIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKL----KHIQQKLEKIKEEEKQMKS 1003
Cdd:TIGR02168  788 EAQ-----------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQIEELSEDIES 856
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1004 LTVSYEKQiQVEKTLKIQAINKLAEVMKKTDGRPHQIN------NTDIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQR-- 1075
Cdd:TIGR02168  857 LAAEIEEL-EELIEELESELEALLNERASLEEALALLRseleelSEELRELESKRSELRRELEELREKLAQLELRLEGle 935
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1076 -EINDMQAMIAEESQVRLEMQMSLDSK-DSDIERLRSQLTSLsihsldTTSISSIGN-DLDSDEAY 1138
Cdd:TIGR02168  936 vRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRL------ENKIKELGPvNLAAIEEY 995
 
Name Accession Description Interval E-value
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
51-402 0e+00

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 737.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   51 NKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIM 130
Cdd:cd05596      1 NKNIENFLNRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  131 AFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR 210
Cdd:cd05596     81 AHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  211 NGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYG 290
Cdd:cd05596    161 SGHLKLADFGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  291 KIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNF 370
Cdd:cd05596    241 KIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1207153289  371 dDDIKDDPIGTETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05596    321 -DDIEEDETPEETFPVPKAFVGNHLPFVGFTY 351
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
78-340 4.91e-87

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.04  E-value: 4.91e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289    78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKrsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   158 MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmvRCDTA 236
Cdd:smart00220   79 CEGGDLFDlLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE--KLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLIC 316
Cdd:smart00220  157 VGTPEYMAPEVLLGKG----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                           250       260
                    ....*....|....*....|....*
gi 1207153289   317 AFLS-SREVRLgrtGVDEIKCHPFF 340
Cdd:smart00220  233 KLLVkDPEKRL---TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
74-392 1.59e-70

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 240.10  E-value: 1.59e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:PTZ00263    16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDStgmvR 232
Cdd:PTZ00263    96 LLEFVVGGELFThLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD----R 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIEMskNAK 312
Cdd:PTZ00263   172 TFTLCGTPEYLAPEVIQSKG----HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGR--LKFPNWFDG--RAR 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  313 DLICAFLSSREV-RLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDD--DIKDDPIGTETFPPP 387
Cdd:PTZ00263   244 DLVKGLLQTDHTkRLGtlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKypDSPVDRLPPLTAAQQ 323

                   ....*
gi 1207153289  388 RAFAG 392
Cdd:PTZ00263   324 AEFAG 328
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1212-1316 3.78e-49

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269948  Cd Length: 110  Bit Score: 169.84  E-value: 3.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1212 LEGWLSMPAK-NTKRFGWDKKYVVVSSKKILFYDSEQDREQSSPFMILDIDKLFHVRPVTQTDVYRADPREIPRIFQILY 1290
Cdd:cd01242      3 LEGWLSLPNKqNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQILY 82
                           90       100
                   ....*....|....*....|....*...
gi 1207153289 1291 ANEGESKKEE--LPVESLSVTERSLCIP 1316
Cdd:cd01242     83 ANEGESSRPAevTDTLSVSREEKPNTIL 110
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
81-293 9.47e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 9.47e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-----FEMVKRsdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaadPEARER-----FRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCD 234
Cdd:COG0515     87 EYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  235 TAVGTPDYISPEVLMsqgGTGYYGReCDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:COG0515    167 TVVGTPGYMAPEQAR---GEPVDPR-SDVYSLGVTLYELLTGRPPFDGDSPAELLRAHL 221
Pkinase pfam00069
Protein kinase domain;
78-340 1.51e-42

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 155.09  E-value: 1.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNI-LREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLgfihrdikpdnmlldrnghlkladfgtcmkmdstgmvrcDTA 236
Cdd:pfam00069   80 VEGGSLFDLLSEKGaFSEREAKFIMKQILEGLESGSSL---------------------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNS-LTFPDDIemSKNAKDLI 315
Cdd:pfam00069  121 VGTPWYMAPEVLGGNP----YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAfPELPSNL--SEEAKDLL 194
                          250       260
                   ....*....|....*....|....*
gi 1207153289  316 CAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:pfam00069  195 KKLLKKDPSK--RLTATQALQHPWF 217
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1310-1379 9.26e-42

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 147.49  E-value: 9.26e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1310 ERSLCIPHKGHEFVLTLYHFPSSCEVCPRPLWHVFRPPPALECRRCRVKCHKDHIDRKEEVLAPCRVNYD 1379
Cdd:cd20875      2 EKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
429-1138 7.64e-27

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 119.39  E-value: 7.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKA 508
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 GLETDRKRLLENEVSSLKEQLAELKkknqishlsaEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSL 588
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLE----------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  589 RELQERLAQLENSRLVLEQDKLSLQTslELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTL 668
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 EKEKNKqeidLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN-------QSIEAKSETLKDMEhKLLEERsakqqLENR 741
Cdd:TIGR02168  481 ERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIE-AALGGR-----LQAV 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  742 LMqlEKENSVLDCDYKQAKHELQ-----------------ELRSLKENLTEQVEVLNVRVQQET---------------- 788
Cdd:TIGR02168  551 VV--ENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPklrkalsyllggvlvv 628
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  789 --------QRK---------TLcQGDL----KVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQL 847
Cdd:TIGR02168  629 ddldnaleLAKklrpgyrivTL-DGDLvrpgGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  848 KEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDL 927
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  928 EKEkimkeleikdmIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKL----KHIQQKLEKIKEEEKQMKS 1003
Cdd:TIGR02168  788 EAQ-----------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQIEELSEDIES 856
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1004 LTVSYEKQiQVEKTLKIQAINKLAEVMKKTDGRPHQIN------NTDIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQR-- 1075
Cdd:TIGR02168  857 LAAEIEEL-EELIEELESELEALLNERASLEEALALLRseleelSEELRELESKRSELRRELEELREKLAQLELRLEGle 935
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1076 -EINDMQAMIAEESQVRLEMQMSLDSK-DSDIERLRSQLTSLsihsldTTSISSIGN-DLDSDEAY 1138
Cdd:TIGR02168  936 vRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRL------ENKIKELGPvNLAAIEEY 995
HR1_ROCK2 cd11638
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
494-560 2.65e-25

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2; ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212028 [Multi-domain]  Cd Length: 67  Bit Score: 100.39  E-value: 2.65e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  494 KVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKL 560
Cdd:cd11638      1 KALLQHKNTEYQRKAEHEADRKRNLENEVNSLKDQLEDLKKKNQNSQISNEKNIQLQRQLDEANALL 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
426-985 1.91e-23

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 108.10  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  426 LNHTESN---------DLEKRLKKLE------EKFKhemQAKEELEN-KCRIANQRLEKLSKDLEEEVNARQEAEDNLRS 489
Cdd:COG1196    181 LEATEENlerledilgELERQLEPLErqaekaERYR---ELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  490 LEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKknQISHLsAEKNIHLERQLEEVSAKLQAELEESER 569
Cdd:COG1196    258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--DIARL-EERRRELEERLEELEEELAELEEELEE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  570 LKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKS 649
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  650 SLSKAEVEKRQLQEDLTTLEKEknkqeidlsfkLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLL 729
Cdd:COG1196    415 RLERLEEELEELEEALAELEEE-----------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  730 EERSAKQQLENRLMQLEKENSVLDCDYKQAKH---------ELQELRSLKENLTEQVE-----VLNVRVQQETQRKTLCQ 795
Cdd:COG1196    484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLlaglrglagAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAI 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  796 GDLKVQRQ---------EINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEM-KDQLEAEQYFTKLYK 865
Cdd:COG1196    564 EYLKAAKAgratflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLA 643
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  866 TQIRELKEESD--------------EKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEK 931
Cdd:COG1196    644 GRLREVTLEGEggsaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  932 IMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLK 985
Cdd:COG1196    724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
146-286 7.82e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.80  E-value: 7.82e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK 224
Cdd:NF033483    77 EDGGIPYIVMEYVDGRTLKDyIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA 156
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  225 MDSTGMVRCDTAVGTPDYISPEvlmsQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLV 286
Cdd:NF033483   157 LSSTTMTQTNSVLGTVHYLSPE----QARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
433-979 6.90e-21

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 99.86  E-value: 6.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELEnkcrianQRLEKLSKDLEEEVNARQE-------AEDNLRSLEKEKVLLKHQRTQSV 505
Cdd:pfam01576   79 ELESRLEEEEERSQQLQNEKKKMQ-------QHIQDLEEQLDEEEAARQKlqlekvtTEAKIKKLEEDILLLEDQNSKLS 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  506 RKagletdrKRLLENEVSSLKEQLAELKKKNQisHLSAEKNIHlERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLE 585
Cdd:pfam01576  152 KE-------RKLLEERISEFTSNLAEEEEKAK--SLSKLKNKH-EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:pfam01576  222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLekeknKQEIDLSFKLKAVQQSL----EQE--------EAEHKTTKARLAD-NNKINQSIEAKSETLKdmehkllEER 732
Cdd:pfam01576  302 EAL-----KTELEDTLDTTAAQQELrskrEQEvtelkkalEEETRSHEAQLQEmRQKHTQALEELTEQLE-------QAK 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  733 SAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVqQETQRktlcqgdlkvQRQEinsLRSSE 812
Cdd:pfam01576  370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARL-SESER----------QRAE---LAEKL 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEaeqyftklyktqirelkEESDEKVKLykdaQQRIEDL 892
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ-----------------EETRQKLNL----STRLRQL 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  893 QEERDSLASQLEvsltkadSEQLARITVEEQYSDLEKEkimkeleikdmIARHRQDLAEKDGTINSLEESNRTLTVDVAN 972
Cdd:pfam01576  495 EDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQ-----------LSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556

                   ....*..
gi 1207153289  973 LASEKEE 979
Cdd:pfam01576  557 LTQQLEE 563
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
433-1029 3.71e-20

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 97.44  E-value: 3.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKekvLLKHQRTQSVRKAGLEt 512
Cdd:PRK03918   190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES---LEGSKRKLEEKIRELE- 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLLENEVSSLKEQLAELKKKNQishlSAEKNIHLER---QLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLR 589
Cdd:PRK03918   266 ERIEELKKEIEELEEKVKELKELKE----KAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  590 ELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNagsetitdLQGRIYGLEGElkHIKSSLSKAEVEKRQLQEDLTTLE 669
Cdd:PRK03918   342 ELKKKLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT 411
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  670 KEKNKQEIDLSFKLKAVQQsLEQEEAEHKTTKARLADNNKINQsIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEN 749
Cdd:PRK03918   412 ARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  750 SvldcdykqAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTlcqGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTL 829
Cdd:PRK03918   490 K--------KESELIKLKELAEQLKELEEKLKKYNLEELEKKA---EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  830 EkqnqELSKEREESEKQLKEMKDQLEAEQYFT-KLYKTQIRELKEESDEKVKLyKDAQQRIEDLQEERDSLASQLEVSLT 908
Cdd:PRK03918   559 A----ELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  909 KADSEQLARITVEEQYSDLEKEKIMKELE-IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHI 987
Cdd:PRK03918   634 ELAETEKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  988 QqklekikEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEV 1029
Cdd:PRK03918   714 E-------KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1320-1374 7.82e-11

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 58.63  E-value: 7.82e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  1320 HEFVLTLYHFPSSCEVCPRPLWHVFRPppALECRRCRVKCHKDHIDRkeeVLAPC 1374
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQ--GLRCSECKVKCHKKCADK---VPKAC 50
 
Name Accession Description Interval E-value
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
51-402 0e+00

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 737.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   51 NKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIM 130
Cdd:cd05596      1 NKNIENFLNRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  131 AFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR 210
Cdd:cd05596     81 AHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  211 NGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYG 290
Cdd:cd05596    161 SGHLKLADFGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  291 KIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNF 370
Cdd:cd05596    241 KIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1207153289  371 dDDIKDDPIGTETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05596    321 -DDIEEDETPEETFPVPKAFVGNHLPFVGFTY 351
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
25-404 0e+00

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 717.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   25 SPLNLESLLDSVTALALDLNHPALRKNKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVY 104
Cdd:cd05621      1 SPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVNKIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  105 AMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEV 184
Cdd:cd05621     81 AMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  185 VLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWW 264
Cdd:cd05621    161 VLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWW 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  265 SVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQ 344
Cdd:cd05621    241 SVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFRNDQ 320
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  345 WTFDTIRDTMAPVVPELSSDIDTSNFdDDIKDDPIGTETFPPPRAFAGNQLPFVGFTYFR 404
Cdd:cd05621    321 WNWDNIRETAAPVVPELSSDIDTSNF-DDIEDDKGDVETFPIPKAFVGNQLPFVGFTYYR 379
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
6-409 0e+00

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 670.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289    6 GKRIESRVRKLETLIKNQKSPLNLESLLDSVTALALDLNHPALRKNKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIG 85
Cdd:cd05622      3 GESFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   86 RGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVT 165
Cdd:cd05622     83 RGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  166 LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYISP 245
Cdd:cd05622    163 LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISP 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  246 EVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVR 325
Cdd:cd05622    243 EVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVR 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  326 LGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFdDDIKDDPIGTETFPPPRAFAGNQLPFVGFTYFRE 405
Cdd:cd05622    323 LGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNF-DDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSN 401

                   ....
gi 1207153289  406 DQLL 409
Cdd:cd05622    402 RRYL 405
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
76-402 2.27e-179

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 537.64  E-value: 2.27e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG----- 229
Cdd:cd05573     81 EYMPGGDLMNLLIKYDVfPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGdresy 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 -----------------------MVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLV 286
Cdd:cd05573    161 lndsvntlfqdnvlarrrphkqrRVRAYSAVGTPDYIAPEVLRGTG----YGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  287 GTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRtgVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDID 366
Cdd:cd05573    237 ETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLCDPEDRLGS--AEEIKAHPFFKGIDW--ENLRESPPPFVPELSSPTD 312
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1207153289  367 TSNFDDDIKDDPI-GTETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05573    313 TSNFDDFEDDLLLsEYLSNGSPLLGKGKQLAFVGFTF 349
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
76-402 3.51e-164

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 496.87  E-value: 3.51e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05597      1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRC 233
Cdd:cd05597     81 DYYCGGDLLTLLSKFEdrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEVLM-SQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDD-IEMSKNA 311
Cdd:cd05597    161 SVAVGTPDYISPEILQaMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPDDeDDVSEEA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  312 KDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNFDDDiKDDPIGTETFPPPR--A 389
Cdd:cd05597    241 KDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDW--DNIRDSTPPYIPEVTSPTDTSNFDVD-DDDLRHTDSLPPPSnaA 317
                          330
                   ....*....|...
gi 1207153289  390 FAGNQLPFVGFTY 402
Cdd:cd05597    318 FSGLHLPFVGFTY 330
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
12-405 1.73e-143

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 445.22  E-value: 1.73e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   12 RVRKLETLI-----KNQKSpLNLESLLDSVTALALDLNHPALRKNKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLIGR 86
Cdd:cd05624      4 RLKKLEQLLldgpqRNESA-LSVETLLDVLVCLYTECSHSPLRRDKYVSEFLEWAKPFTQLVKEMQLHRDDFEIIKVIGR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   87 GAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTL 166
Cdd:cd05624     83 GAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  167 TSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYIS 244
Cdd:cd05624    163 LSKFEdkLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYIS 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  245 PEVLMS-QGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDI-EMSKNAKDLICAFLSSR 322
Cdd:cd05624    243 PEILQAmEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVtDVSEEAKDLIQRLICSR 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  323 EVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNF--DDDIKDDPigtETFPPPR--AFAGNQLPFV 398
Cdd:cd05624    323 ERRLGQNGIEDFKKHAFFEGLNW--ENIRNLEAPYIPDVSSPSDTSNFdvDDDVLRNP---EILPPSShtGFSGLHLPFV 397

                   ....*..
gi 1207153289  399 GFTYFRE 405
Cdd:cd05624    398 GFTYTTE 404
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
76-402 5.60e-143

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 440.59  E-value: 5.60e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05601      1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRC 233
Cdd:cd05601     81 EYHPGGDLLSLLSRYDdiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEVL--MSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNA 311
Cdd:cd05601    161 KMPVGTPDYIAPEVLtsMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVSESA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  312 KDLICAFLSSREVRLGRTGvdeIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPI-GTETFPPPRAF 390
Cdd:cd05601    241 VDLIKGLLTDAKERLGYEG---LCCHPFFSGIDW--NNLRQTVPPFVPTLTSDDDTSNFDEFEPKKTRpSYENFNKSKGF 315
                          330
                   ....*....|..
gi 1207153289  391 AGNQLPFVGFTY 402
Cdd:cd05601    316 SGKDLPFVGFTF 327
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
76-402 6.89e-140

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 432.04  E-value: 6.89e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05599      1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcd 234
Cdd:cd05599     81 EFLPGGDMMTLLMKKDTlTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAY-- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDL 314
Cdd:cd05599    159 STVGTPDYIAPEVFLQKG----YGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  315 ICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNFDD--DIKDDPIGTETFPPPRAFAG 392
Cdd:cd05599    235 IERLLCDAEHRLGANGVEEIKSHPFFKGVDW--DHIRERPAPILPEVKSILDTSNFDEfeEVDLQIPSSPEAGKDSKELK 312
                          330
                   ....*....|.
gi 1207153289  393 NQ-LPFVGFTY 402
Cdd:cd05599    313 SKdWVFIGYTY 323
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
10-402 6.30e-135

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 422.12  E-value: 6.30e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   10 ESRVRKLETLIKNQKSP-----LNLESLLDSVTALALDLNHPALRKNKNIDAFLSRYEKAVCNLKELQVKLDDFDRVKLI 84
Cdd:cd05623      1 EVRLRQLEQLILDGPGQtngqcFSVETLLDILICLYDECSNSPLRREKNILEYLEWAKPFTSKVKQMRLHKEDFEILKVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   85 GRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLV 164
Cdd:cd05623     81 GRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  165 TLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDY 242
Cdd:cd05623    161 TLLSKFEdrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  243 ISPEVLMS-QGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDI-EMSKNAKDLICAFLS 320
Cdd:cd05623    241 ISPEILQAmEDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVtDVSENAKDLIRRLIC 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  321 SREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNFDDDikDDPI-GTETFPPPR--AFAGNQLPF 397
Cdd:cd05623    321 SREHRLGQNGIEDFKNHPFFVGIDW--DNIRNCEAPYIPEVSSPTDTSNFDVD--DDCLkNCETMPPPThtAFSGHHLPF 396

                   ....*
gi 1207153289  398 VGFTY 402
Cdd:cd05623    397 VGFTY 401
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
76-404 7.01e-112

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 356.63  E-value: 7.01e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05598      1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM----KMDSTGM 230
Cdd:cd05598     81 DYIPGGDLMSLLIKKGIfEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRCdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKN 310
Cdd:cd05598    161 LAH-SLVGTPNYIAPEVLLRTG----YTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  311 AKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPELSSDIDTSNFD----DDIKDDPIGTETFPP 386
Cdd:cd05598    236 AKDLILRLCCDAEDRLGRNGADEIKAHPFFAGIDW--EKLRKQKAPYIPTIRHPTDTSNFDpvdpEKLRSSDEEPTTPND 313
                          330
                   ....*....|....*...
gi 1207153289  387 PRAFAGNQLPFVGFTYFR 404
Cdd:cd05598    314 PDNGKHPEHAFYEFTFRR 331
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
84-340 3.59e-111

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 351.05  E-value: 3.59e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGTPDY 242
Cdd:cd05123     81 FSHLSKEgRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA-KELSSDGDRTYTFCGTPEY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  243 ISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIemSKNAKDLICAFLSS- 321
Cdd:cd05123    160 LAPEVLLGKG----YGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKIL--KSPLKFPEYV--SPEAKSLISGLLQKd 231
                          250
                   ....*....|....*....
gi 1207153289  322 REVRLGRTGVDEIKCHPFF 340
Cdd:cd05123    232 PTKRLGSGGAEEIKAHPFF 250
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
76-406 1.60e-110

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 354.54  E-value: 1.60e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05629      1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM----------- 223
Cdd:cd05629     81 EFLPGGDLMTMLIKYDTfSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayy 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  224 -----------KMDSTGMVRCDT------------------------AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGV 268
Cdd:cd05629    161 qkllqgksnknRIDNRNSVAVDSinltmsskdqiatwkknrrlmaysTVGTPDYIAPEIFLQQG----YGQECDWWSLGA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  269 FIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfD 348
Cdd:cd05629    237 IMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLITNAENRLGRGGAHEIKSHPFFRGVDW--D 314
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  349 TIRDTMAPVVPELSSDIDTSNF-DDDIKDDPigTETFPPPRAFAGNQ------LPFVGFTYFRED 406
Cdd:cd05629    315 TIRQIRAPFIPQLKSITDTSYFpTDELEQVP--EAPALKQAAPAQQEesveldLAFIGYTYKRFD 377
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
84-345 2.93e-94

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 305.29  E-value: 2.93e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRS--DSAFFweERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd05579      1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNqvDSVLA--ERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--------------TCMKMD 226
Cdd:cd05579     79 DLYSLLENVGaLDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGlskvglvrrqiklsIQKKSN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIE 306
Cdd:cd05579    159 GAPEKEDRRIVGTPDYLAPEILLGQG----HGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGK--IEWPEDPE 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1207153289  307 MSKNAKDLICAFLSSR-EVRLGRTGVDEIKCHPFFKNDQW 345
Cdd:cd05579    233 VSDEAKDLISKLLTPDpEKRLGAKGIEEIKNHPFFKGIDW 272
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
76-372 4.59e-90

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 294.10  E-value: 4.59e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05580      1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDStgmvRCD 234
Cdd:cd05580     81 EYVPGGELFSLLRRSGrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD----RTY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKDL 314
Cdd:cd05580    157 TLCGTPEYLAPEIILSKG----HGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKIL--EGKIRFPS--FFDPDAKDL 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  315 ICAFLSS-REVRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDD 372
Cdd:cd05580    229 IKRLLVVdLTKRLGnlKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDK 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
78-340 4.91e-87

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.04  E-value: 4.91e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289    78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKrsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   158 MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmvRCDTA 236
Cdd:smart00220   79 CEGGDLFDlLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE--KLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLIC 316
Cdd:smart00220  157 VGTPEYMAPEVLLGKG----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                           250       260
                    ....*....|....*....|....*
gi 1207153289   317 AFLS-SREVRLgrtGVDEIKCHPFF 340
Cdd:smart00220  233 KLLVkDPEKRL---TAEEALQHPFF 254
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
75-408 7.15e-87

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 288.11  E-value: 7.15e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd05627      1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM---KMDSTGM 230
Cdd:cd05627     81 MEFLPGGDMMTLLMKKDtLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTglkKAHRTEF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRCDT-------------------------------AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd05627    161 YRNLThnppsdfsfqnmnskrkaetwkknrrqlaysTVGTPDYIAPEVFMQTG----YNKLCDWWSLGVIMYEMLIGYPP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  280 FYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVP 359
Cdd:cd05627    237 FCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVDW--EHIRERPAAIPI 314
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  360 ELSSDIDTSNFDDDIKDDPIGTETFPPPRAFAGNQLPFVGFTYFREDQL 408
Cdd:cd05627    315 EIKSIDDTSNFDDFPESDILQPAPNTTEPDYKSKDWVFLNYTYKRFEGL 363
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
76-408 1.44e-82

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 276.15  E-value: 1.44e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05628      1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM---KMDSTGMV 231
Cdd:cd05628     81 EFLPGGDMMTLLMKKDtLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTglkKAHRTEFY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 R-------------------------------CDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd05628    161 RnlnhslpsdftfqnmnskrkaetwkrnrrqlAFSTVGTPDYIAPEVFMQTG----YNKLCDWWSLGVIMYEMLIGYPPF 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  281 YSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPE 360
Cdd:cd05628    237 CSETPQETYKKVMNWKETLIFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVDW--EHIRERPAAIPIE 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  361 LSSDIDTSNFDDDIKDD---PIGTETFPPPRAFAGNQLPFVGFTYFREDQL 408
Cdd:cd05628    315 IKSIDDTSNFDEFPDSDilkPSVAVSNHPETDYKNKDWVFINYTYKRFEGL 365
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
69-402 2.26e-81

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 273.06  E-value: 2.26e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   69 KELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDE 148
Cdd:cd05600      4 RRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC----- 222
Cdd:cd05600     84 ENVYLAMEYVPGGDFRTLLNNSGIlSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgtls 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 ------MK-------------------------MDSTGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIY 271
Cdd:cd05600    164 pkkiesMKirleevkntafleltakerrniyraMRKEDQNYANSVVGSPDYMAPEVLRGEG----YDLTVDYWSLGCILF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  272 ELLVGDTPFYSESLVGTYGKIMDHKNSLTFP------DDIEMSKNAKDLICAFLSSREVRLGRTgvDEIKCHPFFKNDQW 345
Cdd:cd05600    240 ECLVGFPPFSGSTPNETWANLYHWKKTLQRPvytdpdLEFNLSDEAWDLITKLITDPQDRLQSP--EQIKNHPFFKNIDW 317
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  346 tfDTIRD-TMAPVVPELSSDIDTSNFDD-----------DIKDDPIGTETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05600    318 --DRLREgSKPPFIPELESEIDTSYFDDfndeadmakykDVHEKQKSLEGSGKNGGDNGNRSLFVGFTF 384
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
77-345 5.32e-79

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 262.34  E-value: 5.32e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd05609      1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC----MKMDST--- 228
Cdd:cd05609     81 YVEGGDCATLLKNIgPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglMSLTTNlye 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMVRCDT-------AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTF 301
Cdd:cd05609    161 GHIEKDTrefldkqVCGTPEYIAPEVILRQG----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI--SDEIEW 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  302 PDDIE-MSKNAKDLICAFLSSREV-RLGRTGVDEIKCHPFFKNDQW 345
Cdd:cd05609    235 PEGDDaLPDDAQDLITRLLQQNPLeRLGTGGAEEVKQHPFFQDLDW 280
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-366 2.02e-78

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 262.17  E-value: 2.02e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05574      1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTL---TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd05574     81 DYCPGGELFRLlqkQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTA----------------------------VGTPDYISPEVLMSQGGTGyygrECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd05574    161 RKSLrkgsrrssvksieketfvaepsarsnsfVGTEEYIAPEVIKGDGHGS----AVDWWTLGILLYEMLYGTTPFKGSN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  285 LVGTYGKIMdhKNSLTFPDDIEMSKNAKDLICAFL---SSRevRLG-RTGVDEIKCHPFFKNDQWtfDTIRDTMAPVVPE 360
Cdd:cd05574    237 RDETFSNIL--KKELTFPESPPVSSEAKDLIRKLLvkdPSK--RLGsKRGASEIKRHPFFRGVNW--ALIRNMTPPIIPR 310

                   ....*.
gi 1207153289  361 LSSDID 366
Cdd:cd05574    311 PDDPID 316
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
78-390 3.82e-78

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 263.80  E-value: 3.82e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05626      3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM----------- 225
Cdd:cd05626     83 IPGGDMMSLLIRMEVfPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthnskyyqk 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 ---------------DSTGMVRC--------------------DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFI 270
Cdd:cd05626    163 gshirqdsmepsdlwDDVSNCRCgdrlktleqratkqhqrclaHSLVGTPNYIAPEVLLRKG----YTQLCDWWSVGVIL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  271 YELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWTFDtI 350
Cdd:cd05626    239 FEMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERLGRNGADDIKAHPFFSEVDFSSD-I 317
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1207153289  351 RDTMAPVVPELSSDIDTSNFDDDIKDDPIGTETFPPPRAF 390
Cdd:cd05626    318 RTQPAPYVPKISHPMDTSNFDPVEEESPWNDASGDSTRTW 357
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
82-403 9.52e-77

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 257.53  E-value: 9.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQS-PWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05570      1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRhPFLTGLHACFQTEDRLYFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVtltsnYDI------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCD 234
Cdd:cd05570     81 GDLM-----FHIqrarrfTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC-KEGIWGGNTTS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPddIEMSKNAKDL 314
Cdd:cd05570    155 TFCGTPDYIAPEILREQD----YGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDE--VLYP--RWLSREAVSI 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  315 ICAFLS-SREVRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDD-IKDDPIGTETFPPPRAf 390
Cdd:cd05570    227 LKGLLTkDPARRLGcgPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEfTSESPRLTPVDSDLLT- 305
                          330
                   ....*....|...
gi 1207153289  391 AGNQLPFVGFTYF 403
Cdd:cd05570    306 NIDQEEFRGFSYI 318
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
76-372 3.02e-74

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 249.24  E-value: 3.02e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14209      1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCd 234
Cdd:cd14209     81 EYVPGGEMFShLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLC- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 tavGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDdiEMSKNAKDL 314
Cdd:cd14209    160 ---GTPEYLAPEIILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPS--HFSSDLKDL 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  315 ICAFLS---SRevRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDD 372
Cdd:cd14209    229 LRNLLQvdlTK--RFGnlKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
78-371 2.11e-72

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 247.27  E-value: 2.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05625      3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC-------------- 222
Cdd:cd05625     83 IPGGDMMSLLIRMGVfPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqs 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 ---MKMDSTGM---------VRC--------------------DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFI 270
Cdd:cd05625    163 gdhLRQDSMDFsnewgdpenCRCgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTG----YTQLCDWWSVGVIL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  271 YELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFKNDQWTFDtI 350
Cdd:cd05625    239 FEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSD-L 317
                          330       340
                   ....*....|....*....|.
gi 1207153289  351 RDTMAPVVPELSSDIDTSNFD 371
Cdd:cd05625    318 RQQSAPYIPKITHPTDTSNFD 338
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-372 9.97e-72

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 241.96  E-value: 9.97e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05612      1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDStgmvRCD 234
Cdd:cd05612     81 EYVPGGELFSyLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRD----RTW 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIEMSknAKDL 314
Cdd:cd05612    157 TLCGTPEYLAPEVIQSKG----HNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGK--LEFPRHLDLY--AKDL 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  315 ICAFLS-SREVRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDD 372
Cdd:cd05612    229 IKKLLVvDRTRRLGnmKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDD 289
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
84-345 4.45e-71

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 239.05  E-value: 4.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmvRCDTAVGTPDY 242
Cdd:cd05572     81 WTiLRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGR--KTWTFCGTPEY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  243 ISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS--ESLVGTYGKIMDHKNSLTFPDDIemSKNAKDLICAFLS 320
Cdd:cd05572    159 VAPEIILNKG----YDFSVDYWSLGILLYELLTGRPPFGGddEDPMKIYNIILKGIDKIEFPKYI--DKNAKNLIKQLLR 232
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  321 -SREVRLG--RTGVDEIKCHPFFKNDQW 345
Cdd:cd05572    233 rNPEERLGylKGGIRDIKKHKWFEGFDW 260
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
74-392 1.59e-70

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 240.10  E-value: 1.59e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:PTZ00263    16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDStgmvR 232
Cdd:PTZ00263    96 LLEFVVGGELFThLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD----R 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIEMskNAK 312
Cdd:PTZ00263   172 TFTLCGTPEYLAPEVIQSKG----HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGR--LKFPNWFDG--RAR 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  313 DLICAFLSSREV-RLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDD--DIKDDPIGTETFPPP 387
Cdd:PTZ00263   244 DLVKGLLQTDHTkRLGtlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKypDSPVDRLPPLTAAQQ 323

                   ....*
gi 1207153289  388 RAFAG 392
Cdd:PTZ00263   324 AEFAG 328
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
81-345 7.64e-68

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 229.67  E-value: 7.64e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAF-SQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd05611      1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIqGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcmkMDSTGMVRCDTA-- 236
Cdd:cd05611     81 GGDCASLIKTLGgLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFG----LSRNGLEKRHNKkf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIE--MSKNAKDL 314
Cdd:cd05611    157 VGTPDYLAPETILGVGDD----KMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNIL--SRRINWPEEVKefCSPEAVDL 230
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  315 ICAFLSSR-EVRLGRTGVDEIKCHPFFKNDQW 345
Cdd:cd05611    231 INRLLCMDpAKRLGANGYQEIKSHPFFKSINW 262
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
76-340 2.01e-67

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 229.02  E-value: 2.01e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05581      1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM---- 230
Cdd:cd05581     81 EYAPNGDLLEyIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSpest 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 ------------VRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNS 298
Cdd:cd05581    161 kgdadsqiaynqARAASFVGTAEYVSPELL----NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIV--KLE 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  299 LTFPDDIemSKNAKDLICAFLsSREV--RLG---RTGVDEIKCHPFF 340
Cdd:cd05581    235 YEFPENF--PPDAKDLIQKLL-VLDPskRLGvneNGGYDELKAHPFF 278
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
82-402 2.14e-67

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 230.75  E-value: 2.14e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQ---QVYAMKQLSKFEMVK-RSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05584      2 KVLGKGGYGKVFQVRKTTGSdkgKIFAMKVLKKASIVRnQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVrCDTA 236
Cdd:cd05584     82 LSGGELFMHLEREGIfMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTV-THTF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKDLIC 316
Cdd:cd05584    161 CGTIEYMAPEILTRSG----HGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKIL--KGKLNLPP--YLTNEARDLLK 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  317 AFLSSREV-RLGRTGVD--EIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDI-KDDPIGTETFPPPRAFAG 392
Cdd:cd05584    233 KLLKRNVSsRLGSGPGDaeEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFtKQTPVDSPDDSTLSESAN 312
                          330
                   ....*....|
gi 1207153289  393 NqlPFVGFTY 402
Cdd:cd05584    313 Q--VFQGFTY 320
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
82-402 1.26e-66

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 228.42  E-value: 1.26e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAF-SQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05592      1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGT 239
Cdd:cd05592     81 GDLMfHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC-KENIYGENKASTFCGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIemSKNAKDLICAFL 319
Cdd:cd05592    160 PDYIAPEILKGQ----KYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT--PHYPRWL--TKEAASCLSLLL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  320 SSR-EVRLGRTGVD--EIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIGTeTFPPPRAFAG-NQL 395
Cdd:cd05592    232 ERNpEKRLGVPECPagDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVL-TPVDKKLLASmDQE 310

                   ....*..
gi 1207153289  396 PFVGFTY 402
Cdd:cd05592    311 QFKGFSF 317
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
83-402 1.93e-66

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 227.45  E-value: 1.93e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd05585      1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGTPD 241
Cdd:cd05585     81 LFHhLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC-KLNMKDDDKTNTFCGTPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  242 YISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIEmsKNAKDLICAFLS- 320
Cdd:cd05585    160 YLAPELLLGHG----YTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKIL--QEPLRFPDGFD--RDAKDLLIGLLNr 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  321 SREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIGTETFPPPRAFAGNQLPFVGF 400
Cdd:cd05585    232 DPTKRLGYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSVVDDSHLSESVQQQFEGW 311

                   ..
gi 1207153289  401 TY 402
Cdd:cd05585    312 SY 313
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
82-402 5.89e-66

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 226.43  E-value: 5.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQS-PWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05575      1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKhPFLVGLHYSFQTKDKLYFVLDYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGT 239
Cdd:cd05575     81 GELFFhLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC-KEGIEPSDTTSTFCGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdHKnSLTFPDDIemSKNAKDLICAFL 319
Cdd:cd05575    160 PEYLAPEVLRKQP----YDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNIL-HK-PLRLRTNV--SPSARDLLEGLL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  320 -SSREVRLG-RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIGTETFPPPRAFAGN---- 393
Cdd:cd05575    232 qKDRTKRLGsGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVSasvq 311
                          330
                   ....*....|.
gi 1207153289  394 --QLPFVGFTY 402
Cdd:cd05575    312 eaDNAFDGFSY 322
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
82-403 6.82e-66

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 226.12  E-value: 6.82e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSP-WIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05587      2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVMEYVNG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVtltsnYDI------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCD 234
Cdd:cd05587     82 GDLM-----YHIqqvgkfKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC-KEGIFGGKTTR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknSLTFPDdiEMSKNAKDL 314
Cdd:cd05587    156 TFCGTPDYIAPEIIAYQ----PYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEH--NVSYPK--SLSKEAVSI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  315 ICAFLS---SREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPigTETFPPPRAFA 391
Cdd:cd05587    228 CKGLLTkhpAKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEP--PVLTPTDKLVI 305
                          330
                   ....*....|....
gi 1207153289  392 GN--QLPFVGFTYF 403
Cdd:cd05587    306 MNidQSEFEGFSFV 319
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
77-341 3.00e-63

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 216.19  E-value: 3.00e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd14007      1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgmvRCDT 235
Cdd:cd14007     81 YAPNGELYKeLKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSN---RRKT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  236 AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIemSKNAKDLI 315
Cdd:cd14007    158 FCGTLDYLPPEMVEGKE----YDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVD--IKFPSSV--SPEAKDLI 229
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  316 CAFLSSREVRlgRTGVDEIKCHPFFK 341
Cdd:cd14007    230 SKLLQKDPSK--RLSLEQVLNHPWIK 253
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
82-402 1.63e-61

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 213.42  E-value: 1.63e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKV---SQQVYAMKQLSKfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd05582      1 KVLGQGSFGKVFLVRKITgpdAGTLYAMKVLKK-ATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAV 237
Cdd:cd05582     80 RGGDLFTrLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS-KESIDHEKKAYSFC 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKDLICA 317
Cdd:cd05582    159 GTVEYMAPEVVNRRG----HTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIL--KAKLGMPQ--FLSPEAQSLLRA 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  318 -FLSSREVRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDI-----KDDPIgtetfPPPRA 389
Cdd:cd05582    231 lFKRNPANRLGagPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFtsrtpKDSPG-----VPPSA 305
                          330
                   ....*....|...
gi 1207153289  390 FAgNQLpFVGFTY 402
Cdd:cd05582    306 NA-HQL-FRGFSF 316
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
77-339 3.83e-60

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 207.33  E-value: 3.83e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd05117      1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLR-REIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd05117     80 LCTGGELfdrIVKKGSFS--EREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDI--EMS 308
Cdd:cd05117    158 LK--TVCGTPYYVAPEVLKGKG----YGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKIL--KGKYSFDSPEwkNVS 229
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  309 KNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd05117    230 EEAKDLIKRLLVVDPKK--RLTAAEALNHPW 258
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
82-386 1.21e-59

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 208.36  E-value: 1.21e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd05571      1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGTP 240
Cdd:cd05571     81 ELFFHLSRERVfSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC-KEEISYGATTKTFCGTP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIemSKNAKDLICAFLS 320
Cdd:cd05571    160 EYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELIL--MEEVRFPSTL--SPEAKSLLAGLLK 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  321 SR-EVRLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIgtETFPP 386
Cdd:cd05571    232 KDpKKRLGggPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESV--ELTPP 298
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
84-340 1.38e-59

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 205.57  E-value: 1.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05578      8 IGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 -VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTgmvRCDTAVGTPD 241
Cdd:cd05578     88 rYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNiATKLTDGT---LATSTSGTKP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  242 YISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKI-MDHKNSLTFPddIEMSKNAKDLICAFLS 320
Cdd:cd05578    165 YMAPEVFMRA----GYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRaKFETASVLYP--AGWSEEAIDLINKLLE 238
                          250       260
                   ....*....|....*....|.
gi 1207153289  321 -SREVRLGrtGVDEIKCHPFF 340
Cdd:cd05578    239 rDPQKRLG--DLSDLKNHPYF 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
82-402 4.91e-59

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 206.68  E-value: 4.91e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05590      1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmVRCDTAV 237
Cdd:cd05590     81 GDLmfhIQKSRRFD--EARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNG-KTTSTFC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKDLICA 317
Cdd:cd05590    158 GTPDYIAPEILQEM----LYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAIL--NDEVVYPT--WLSQDAVDILKA 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  318 FLSSR-EVRLGRT---GVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDD-IKDDPIGT---ETFPPpra 389
Cdd:cd05590    230 FMTKNpTMRLGSLtlgGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDfIKEDPVLTpieESLLP--- 306
                          330
                   ....*....|...
gi 1207153289  390 fAGNQLPFVGFTY 402
Cdd:cd05590    307 -MINQDEFRNFSY 318
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
84-402 7.96e-59

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 206.27  E-value: 7.96e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIM---AFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05586      1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGT 239
Cdd:cd05586     81 GELFwHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS-KADLTDNKTTNTFCGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIeMSKNAKDLICAFL 319
Cdd:cd05586    160 TEYLAPEVLLDEKG---YTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGK--VRFPKDV-LSDEGRSFVKGLL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  320 SSR-EVRLGRT-GVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDD-----IKDDPIGTETFPPPRAFAG 392
Cdd:cd05586    234 NRNpKHRLGAHdDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEftnasLLNANIVPWAQRPGLPGAT 313
                          330
                   ....*....|....*..
gi 1207153289  393 N-------QLPFVGFTY 402
Cdd:cd05586    314 StplspsvQANFRGFTF 330
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
82-404 1.30e-58

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 205.42  E-value: 1.30e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05591      1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDL---VTLTSNYDIPEewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAV 237
Cdd:cd05591     81 GDLmfqIQRARKFDEPR--ARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC-KEGILNGKTTTTFC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdHKNSLtFPddIEMSKNAKDLICA 317
Cdd:cd05591    158 GTPDYIAPEILQELE----YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL-YP--VWLSKEAVSILKA 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  318 FLS-SREVRLG----RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDI-KDDPIGTETfPPPRAFA 391
Cdd:cd05591    230 FMTkNPAKRLGcvasQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFtKEEPVLTPV-DPAVIKQ 308
                          330
                   ....*....|...
gi 1207153289  392 GNQLPFVGFTYFR 404
Cdd:cd05591    309 INQEEFRGFSFVN 321
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
78-405 1.90e-58

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 204.84  E-value: 1.90e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDEKYLYLV 154
Cdd:cd05589      1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSarhPFLVNLFACFQTPEHVCFV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKmdstGM---V 231
Cdd:cd05589     81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE----GMgfgD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhknsltfpDDIE----M 307
Cdd:cd05589    157 RTSTFCGTPEFLAPEVLTDTS----YTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVN--------DEVRyprfL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  308 SKNAKDLICAFL-SSREVRLGRTGVD--EIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDI-KDDPIGTET 383
Cdd:cd05589    225 STEAISIMRRLLrKNPERRLGASERDaeDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFtSEKPVLTPP 304
                          330       340
                   ....*....|....*....|..
gi 1207153289  384 FPPPRAFAGNQLPFVGFTYFRE 405
Cdd:cd05589    305 KEPRPLTEEEQALFKDFDYVAD 326
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
72-373 5.62e-58

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 204.00  E-value: 5.62e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKY 150
Cdd:cd05619      1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDL---VTLTSNYDIPEewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDS 227
Cdd:cd05619     81 LFFVMEYLNGGDLmfhIQSCHKFDLPR--ATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC-KENM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKI-MDHKNSLTFpddie 306
Cdd:cd05619    158 LGDAKTSTFCGTPDYIAPEILLGQK----YNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIrMDNPFYPRW----- 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  307 MSKNAKD-LICAFLSSREVRLGRTGvdEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDD 373
Cdd:cd05619    229 LEKEAKDiLVKLFVREPERRLGVRG--DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKE 294
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
82-387 2.06e-57

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 201.77  E-value: 2.06e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd05595      1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGTP 240
Cdd:cd05595     81 ELFfHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC-KEGITDGATMKTFCGTP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDieMSKNAKDLICAFLS 320
Cdd:cd05595    160 EYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIL--MEEIRFPRT--LSPEAKSLLAGLLK 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  321 SR-EVRLGRTGVD--EIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIgteTFPPP 387
Cdd:cd05595    232 KDpKQRLGGGPSDakEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSI---TITPP 298
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
77-392 4.84e-57

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 201.30  E-value: 4.84e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRhKVS----QQVYAMKQLSKFEMVKRSDSAFFWE-ERDIMA-FSQSPWIVQLCCAFQDEKY 150
Cdd:cd05614      1 NFELLKVLGTGAYGKVFLVR-KVSghdaNKLYAMKVLRKAALVQKAKTVEHTRtERNVLEhVRQSPFLVTLHYAFQTDAK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd05614     80 LHLILDYVSGGELFThLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVRCDTAVGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH--KNSLTFPDDIem 307
Cdd:cd05614    160 KERTYSFCGTIEYMAPEIIRGKSG---HGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRilKCDPPFPSFI-- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  308 SKNAKDLICAFL-SSREVRLGR--TGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKD-DPIGTET 383
Cdd:cd05614    235 GPVARDLLQKLLcKDPKKRLGAgpQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNlEPVYSPA 314
                          330
                   ....*....|..
gi 1207153289  384 FPPP---RAFAG 392
Cdd:cd05614    315 GTPPsgaRVFQG 326
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
75-371 2.98e-56

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 199.34  E-value: 2.98e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd05610      3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG------------- 220
Cdd:cd05610     83 MEYLIGGDVKSLLHIYGyFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGlskvtlnrelnmm 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  221 ---TCMKMDST----------------------------------GMVRCDTA--VGTPDYISPEVLMSQGgtgyYGREC 261
Cdd:cd05610    163 dilTTPSMAKPkndysrtpgqvlslisslgfntptpyrtpksvrrGAARVEGEriLGTPDYLAPELLLGKP----HGPAV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  262 DWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPD-DIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd05610    239 DWWALGVCLFEFLTGIPPFNDETPQQVFQNIL--NRDIPWPEgEEELSVNAQNAIEILLTMDPTK--RAGLKELKQHPLF 314
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1207153289  341 KNDQWtfDTIRDTMAPVVPELSSDIDTSNFD 371
Cdd:cd05610    315 HGVDW--ENLQNQTMPFIPQPDDETDTSYFE 343
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
84-342 3.79e-56

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 196.08  E-value: 3.79e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRhKVS----QQVYAMKQLSKFEMVKRSDSAffwE----ERDIM-AFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd05583      2 LGTGAYGKVFLVR-KVGghdaGKLYAMKVLKKATIVQKAKTA---EhtmtERQVLeAVRQSPFLVTLHYAFQTDAKLHLI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRC 233
Cdd:cd05583     78 LDYVNGGELFThLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEVLmsQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH--KNSLTFPDDieMSKNA 311
Cdd:cd05583    158 YSFCGTIEYMAPEVV--RGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRilKSHPPIPKT--FSAEA 233
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1207153289  312 KDLICAFLSSR-EVRLG--RTGVDEIKCHPFFKN 342
Cdd:cd05583    234 KDFILKLLEKDpKKRLGagPRGAHEIKEHPFFKG 267
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
77-402 5.25e-56

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 197.91  E-value: 5.25e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05616      1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVtltsnYDI------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTG 229
Cdd:cd05616     81 EYVNGGDLM-----YHIqqvgrfKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMC-KENIWD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknSLTFPDdiEMSK 309
Cdd:cd05616    155 GVTTKTFCGTPDYIAPEIIAYQP----YGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEH--NVAYPK--SMSK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  310 NAKdLICAFLSSRE--VRL--GRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPElSSDIDTSNFDDDIKDDPIgtETFP 385
Cdd:cd05616    227 EAV-AICKGLMTKHpgKRLgcGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPK-ACGRNAENFDRFFTRHPP--VLTP 302
                          330
                   ....*....|....*....
gi 1207153289  386 PPRAFAGN--QLPFVGFTY 402
Cdd:cd05616    303 PDQEVIRNidQSEFEGFSF 321
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
82-371 8.27e-55

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 194.01  E-value: 8.27e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05620      1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVtltsnYDIPEEW------AQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCD 234
Cdd:cd05620     81 GDLM-----FHIQDKGrfdlyrATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC-KENVFGDNRAS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemSKNAKDL 314
Cdd:cd05620    155 TFCGTPDYIAPEILQGLK----YTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI--RVDTPHYPRWI--TKESKDI 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  315 ICAFLSSREV-RLGRTGvdEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFD 371
Cdd:cd05620    227 LEKLFERDPTrRLGVVG--NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFD 282
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
81-339 3.55e-54

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 190.04  E-value: 3.55e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-------FEMVKRsdsaffweERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd14003      5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKsklkeeiEEKIKR--------EIEIMKLLNHPNIIKLYEVIETENKIYL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDStgm 230
Cdd:cd14003     77 VMEYASGGELFDyIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGlsNEFRGGS--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 vRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIemSKN 310
Cdd:cd14003    154 -LLKTFCGTPAYAAPEVLL---GRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKIL--KGKYPIPSHL--SPD 225
                          250       260
                   ....*....|....*....|....*....
gi 1207153289  311 AKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14003    226 ARDLIRRMLVVDPSK--RITIEEILNHPW 252
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
77-340 7.48e-54

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 188.95  E-value: 7.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd05122      1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKI-NLESKEKKESIL--NEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmvRCD 234
Cdd:cd05122     78 FCSGGSLKDLLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK--TRN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdHKNSLTFPDDIEMSKNAKDL 314
Cdd:cd05122    156 TFVGTPYWMAPEVIQGK----PYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIA-TNGPPGLRNPKKWSKEFKDF 230
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  315 ICAFLSSREVrlGRTGVDEIKCHPFF 340
Cdd:cd05122    231 LKKCLQKDPE--KRPTAEQLLKHPFI 254
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
81-402 1.55e-53

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 190.94  E-value: 1.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd05604      1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNvKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKmdstGMVRCDTAV- 237
Cdd:cd05604     81 GGELFfHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKE----GISNSDTTTt 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 --GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdHKNSLTFPDdieMSKNAKDLI 315
Cdd:cd05604    157 fcGTPEYLAPEVIRKQP----YDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENIL-HKPLVLRPG---ISLTAWSIL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  316 CAFLS-SREVRLG-RTGVDEIKCHPFFKNDQWTfDTIRDTMAPVV-PELSSDIDTSNFDDDIKDdpigtETFPPPRAFAG 392
Cdd:cd05604    229 EELLEkDRQLRLGaKEDFLEIKNHPFFESINWT-DLVQKKIPPPFnPNVNGPDDISNFDAEFTE-----EMVPYSVCVSS 302
                          330       340
                   ....*....|....*....|.
gi 1207153289  393 NQL-----------PFVGFTY 402
Cdd:cd05604    303 DYSivnasvleaddAFVGFSY 323
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
69-385 4.24e-53

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 190.19  E-value: 4.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   69 KELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQ-QVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQD 147
Cdd:PTZ00426    23 RKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKD 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:PTZ00426   103 ESYLYLVLEFVIGGEFFTfLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 StgmvRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhkNSLTFPDDIE 306
Cdd:PTZ00426   183 T----RTYTLCGTPEYIAPEILLNVG----HGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILE--GIIYFPKFLD 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  307 msKNAKDLICAFLSSREV-RLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKD----DPI 379
Cdd:PTZ00426   253 --NNCKHLMKKLLSHDLTkRYGnlKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQEDltiaDKI 330

                   ....*.
gi 1207153289  380 GTETFP 385
Cdd:PTZ00426   331 TNENDP 336
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
82-402 1.31e-52

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 188.40  E-value: 1.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKrSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd05588      1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKK-ELVN-DDEDIDWVQTEKHVFETAsnhPFLVGLHSCFQTESRLFFVIEFV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM----KMDSTGmvrc 233
Cdd:cd05588     79 NGGDLMfHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeglrPGDTTS---- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 dTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFyseSLVGTYGKIMDHKNSLTFPDDIE------- 306
Cdd:cd05588    155 -TFCGTPNYIAPEILRGED----YGFSVDWWALGVLMFEMLAGRSPF---DIVGSSDNPDQNTEDYLFQVILEkpiripr 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  307 -MSKNAKDLICAFLSSREV-RLG---RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIGT 381
Cdd:cd05588    227 sLSVKAASVLKGFLNKNPAeRLGchpQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQL 306
                          330       340
                   ....*....|....*....|.
gi 1207153289  382 ETFPPPRAFAGNQLPFVGFTY 402
Cdd:cd05588    307 TPDDPDVIEKIDQSEFEGFEY 327
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
74-379 7.75e-52

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 186.38  E-value: 7.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLY 152
Cdd:cd05602      5 KPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNvKHPFLVGLHFSFQTTDKLY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC---MKMDST 228
Cdd:cd05602     85 FVLDYINGGELFYhLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCkenIEPNGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMVRCdtavGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTfPDdieMS 308
Cdd:cd05602    165 TSTFC----GTPEYLAPEVLHKQP----YDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLK-PN---IT 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  309 KNAKDLICAFLSS-REVRLGRTG-VDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPI 379
Cdd:cd05602    233 NSARHLLEGLLQKdRTKRLGAKDdFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPV 305
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
77-359 2.40e-51

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 183.28  E-value: 2.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRhKVSQ----QVYAMKQLSKFEMVKRSDSA-FFWEERDIMA-FSQSPWIVQLCCAFQDEKY 150
Cdd:cd05613      1 NFELLKVLGTGAYGKVFLVR-KVSGhdagKLYAMKVLKKATIVQKAKTAeHTRTERQVLEhIRQSPFLVTLHYAFQTDTK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd05613     80 LHLILDYINGGELFThLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVRCDTAVGTPDYISPEVLmsQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH--KNSLTFPDdiEM 307
Cdd:cd05613    160 NERAYSFCGTIEYMAPEIV--RGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRilKSEPPYPQ--EM 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  308 SKNAKDLI-CAFLSSREVRL--GRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVP 359
Cdd:cd05613    236 SALAKDIIqRLLMKDPKKRLgcGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
75-390 8.05e-51

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 183.74  E-value: 8.05e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd05593     14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRC 233
Cdd:cd05593     94 MEYVNGGELfFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-KEGITDAATM 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKD 313
Cdd:cd05593    173 KTFCGTPEYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSADAKS 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  314 LICAFL---SSREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIgteTFPPPRAF 390
Cdd:cd05593    245 LLSGLLikdPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTI---TITPPEKY 321
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
77-340 1.03e-50

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 180.02  E-value: 1.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd06606      1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEV-ELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCD- 234
Cdd:cd06606     80 YVPGGSLASLLKKFGkLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTk 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYGKIMDHKNSLTFPDDieMSKNAKD 313
Cdd:cd06606    160 SLRGTPYWMAPEVIRGEG----YGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEPPPIPEH--LSEEAKD 233
                          250       260       270
                   ....*....|....*....|....*....|
gi 1207153289  314 licaFLS---SREVRLgRTGVDEIKCHPFF 340
Cdd:cd06606    234 ----FLRkclQRDPKK-RPTADELLQHPFL 258
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
72-402 4.28e-50

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 181.35  E-value: 4.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAF-SQSPWIVQLCCAFQDEKY 150
Cdd:cd05615      6 RVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALqDKPPFLTQLHSCFQTVDR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd05615     86 LYFVMEYVNGGDLMYHIQQVgKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 mVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknSLTFPDdiEMSK 309
Cdd:cd05615    166 -VTTRTFCGTPDYIAPEIIAYQP----YGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEH--NVSYPK--SLSK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  310 NAKDLICAFLS---SREVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDiDTSNFDDDI-KDDPIGTetfP 385
Cdd:cd05615    237 EAVSICKGLMTkhpAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFtRGQPVLT---P 312
                          330
                   ....*....|....*....
gi 1207153289  386 PPRAFAGN--QLPFVGFTY 402
Cdd:cd05615    313 PDQLVIANidQADFEGFSY 331
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
75-415 5.07e-50

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 182.15  E-value: 5.07e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKrSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDEKYL 151
Cdd:cd05618     19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKK-ELVN-DDEDIDWVQTEKHVFEQAsnhPFLVGLHSCFQTESRL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd05618     97 FFVIEYVNGGDLMfHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFyseSLVGTYGKIMDHKNSLTFPDDIE---- 306
Cdd:cd05618    177 T-TSTFCGTPNYIAPEILRGED----YGFSVDWWALGVLMFEMMAGRSPF---DIVGSSDNPDQNTEDYLFQVILEkqir 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  307 ----MSKNAKDLICAFLSSR-EVRLG---RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDP 378
Cdd:cd05618    249 iprsLSVKAASVLKSFLNKDpKERLGchpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEP 328
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1207153289  379 IGTETFPPPRAFAGNQLPFVGFTYFreDQLLTQQNKC 415
Cdd:cd05618    329 VQLTPDDDDIVRKIDQSEFEGFEYI--NPLLMSAEEC 363
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
75-379 2.16e-49

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 179.83  E-value: 2.16e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVkRSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDEKYL 151
Cdd:cd05617     14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKK-ELV-HDDEDIDWVQTEKHVFEQAssnPFLVGLHSCFQTTSRL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd05617     92 FLVIEYVNGGDLMfHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYseslVGTYGKIMDHKNSLtFPDDIE---- 306
Cdd:cd05617    172 T-TSTFCGTPNYIAPEILRGEE----YGFSVDWWALGVLMFEMMAGRSPFD----IITDNPDMNTEDYL-FQVILEkpir 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  307 ----MSKNAKDLICAFLSSR-EVRLG---RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDP 378
Cdd:cd05617    242 iprfLSVKASHVLKGFLNKDpKERLGcqpQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEP 321

                   .
gi 1207153289  379 I 379
Cdd:cd05617    322 V 322
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1212-1316 3.78e-49

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269948  Cd Length: 110  Bit Score: 169.84  E-value: 3.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1212 LEGWLSMPAK-NTKRFGWDKKYVVVSSKKILFYDSEQDREQSSPFMILDIDKLFHVRPVTQTDVYRADPREIPRIFQILY 1290
Cdd:cd01242      3 LEGWLSLPNKqNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQILY 82
                           90       100
                   ....*....|....*....|....*...
gi 1207153289 1291 ANEGESKKEE--LPVESLSVTERSLCIP 1316
Cdd:cd01242     83 ANEGESSRPAevTDTLSVSREEKPNTIL 110
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
82-402 6.28e-49

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 177.47  E-value: 6.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS-QSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05603      1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNlKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC---MKMDSTGMVRCdta 236
Cdd:cd05603     81 GELfFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCkegMEPEETTSTFC--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 vGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdHKnsltfPDDIEMSKN--AKDL 314
Cdd:cd05603    158 -GTPEYLAPEVLRKEP----YDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNIL-HK-----PLHLPGGKTvaACDL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  315 ICAFL-SSREVRLG-RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIGTE---TFPPPRA 389
Cdd:cd05603    227 LQGLLhKDQRRRLGaKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSvgrTPDLTAS 306
                          330
                   ....*....|...
gi 1207153289  390 FAGNQLPFVGFTY 402
Cdd:cd05603    307 SSSSSSAFLGFSY 319
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
76-340 7.69e-49

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 174.66  E-value: 7.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14099      1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTL-TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMvRCD 234
Cdd:cd14099     81 ELCSNGSLMELlKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE-RKK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGGTGYygrECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIEMSKNAKDL 314
Cdd:cd14099    160 TLCGTPNYIAPEVLEKKKGHSF---EVDIWSLGVILYTLLVGKPPFETSDVKETYKRI--KKNEYSFPSHLSISDEAKDL 234
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  315 ICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14099    235 IRSMLQPDPTK--RPSLDEILSHPFF 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
84-273 1.02e-48

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 172.84  E-value: 1.02e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVIPK--EKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPD 241
Cdd:cd00180     79 KDLLKENKgpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPP 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1207153289  242 YISPEVLMSQggtGYYGRECDWWSVGVFIYEL 273
Cdd:cd00180    159 YYAPPELLGG---RYYGPKVDIWSLGVILYEL 187
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
84-340 1.08e-48

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 174.66  E-value: 1.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAF-----------FWEERDIMAFSQSPWIVQLCCAFQDEK--Y 150
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNdrgkiknalddVRREIAIMKKLDHPNIVRLYEVIDDPEsdK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtCMKMDS 227
Cdd:cd14008     81 LYLVLEYCEGGPVMELDSGDRvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG-VSEMFE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRCDTAVGTPDYISPEvLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIem 307
Cdd:cd14008    160 DGNDTLQKTAGTPAFLAPE-LCDGDSKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPEL-- 236
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1207153289  308 SKNAKDLICAFL--SSREvrlgRTGVDEIKCHPFF 340
Cdd:cd14008    237 SPELKDLLRRMLekDPEK----RITLKEIKEHPWV 267
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
81-315 4.47e-48

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 172.77  E-value: 4.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDS-AFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd14014      5 VRLLGRGGMGEVYRARDTLLGRPVAIKVL-RPELAEDEEFrERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVG 238
Cdd:cd14014     84 GGSLADlLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGSVLG 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  239 TPDYISPEVLMSQGGTGyygrECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLI 315
Cdd:cd14014    164 TPAYMAPEQARGGPVDP----RSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAII 236
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
72-404 1.24e-47

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 174.83  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd05594     21 KVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd05594    101 CFVMEYANGGELfFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVRcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSK 309
Cdd:cd05594    181 ATM-KTFCGTPEYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFPR--TLSP 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  310 NAKDLICAFLSSREV-RLGRTGVD--EIKCHPFFKNDQWTFDTIRDTMAPVVPELSSDIDTSNFDDDIKDDPIgteTFPP 386
Cdd:cd05594    252 EAKSLLSGLLKKDPKqRLGGGPDDakEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQMI---TITP 328
                          330       340
                   ....*....|....*....|....*
gi 1207153289  387 P------RAFAGNQLP-FVGFTYFR 404
Cdd:cd05594    329 PdqddsmETVDNERRPhFPQFSYSA 353
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
76-342 1.77e-47

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 171.24  E-value: 1.77e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMK--QLSKFEMVKRSDSAffweERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd06623      1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKkiHVDGDEEFRKQLLR----ELKTLRSCESPYVVKCYGAFYKEGEISI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLT-SNYDIPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMV 231
Cdd:cd06623     77 VLEYMDGGSLADLLkKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT-LD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFySESLVGTYGKIMDHKNS--LTFPDDIEMSK 309
Cdd:cd06623    156 QCNTFVGTVTYMSPERIQGE----SYSYAADIWSLGLTLLECALGKFPF-LPPGQPSFFELMQAICDgpPPSLPAEEFSP 230
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1207153289  310 NAKDLI--CAFLSSREvrlgRTGVDEIKCHPFFKN 342
Cdd:cd06623    231 EFRDFIsaCLQKDPKK----RPSAAELLQHPFIKK 261
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
81-293 9.47e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 9.47e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-----FEMVKRsdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaadPEARER-----FRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCD 234
Cdd:COG0515     87 EYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTG 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  235 TAVGTPDYISPEVLMsqgGTGYYGReCDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:COG0515    167 TVVGTPGYMAPEQAR---GEPVDPR-SDVYSLGVTLYELLTGRPPFDGDSPAELLRAHL 221
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
84-345 2.53e-46

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 168.47  E-value: 2.53e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcMKMDSTGMVRCDTAVGTP 240
Cdd:cd05577     81 KYHIYNVGtrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLG--LAVEFKGGKKIKGRVGTH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF--YSESLVGTYGKIMDHKNSLTFPDDieMSKNAKDLICAF 318
Cdd:cd05577    159 GYMAPEVLQ---KEVAYDFSVDWFALGCMLYEMIAGRSPFrqRKEKVDKEELKRRTLEMAVEYPDS--FSPEARSLCEGL 233
                          250       260       270
                   ....*....|....*....|....*....|
gi 1207153289  319 LSSR-EVRLG--RTGVDEIKCHPFFKNDQW 345
Cdd:cd05577    234 LQKDpERRLGcrGGSADEVKEHPFFRSLNW 263
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
84-338 2.71e-46

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 167.92  E-value: 2.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdsAFF----------------------WEERDIMAFSQSPWIVQL 141
Cdd:cd14118      2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQA--GFFrrppprrkpgalgkpldpldrvYREIAILKKLDHPNVVKL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  142 CCAFQD--EKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADF 219
Cdd:cd14118     80 VEVLDDpnEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  220 GTCMKMDSTGMVRCDTAvGTPDYISPEVLmSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhkNSL 299
Cdd:cd14118    160 GVSNEFEGDDALLSSTA-GTPAFMAPEAL-SESRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKT--DPV 235
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207153289  300 TFPDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHP 338
Cdd:cd14118    236 VFPDDPVVSEQLKDLILRMLDKNPSE--RITLPEIKEHP 272
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
84-339 2.00e-44

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 162.01  E-value: 2.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLE-SEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMDSTGMVrcDTAVGT 239
Cdd:cd14009     80 SQYIRKRGrLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMA--ETLCGS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFL 319
Cdd:cd14009    158 PLYMAPEILQFQ----KYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLL 233
                          250       260
                   ....*....|....*....|
gi 1207153289  320 SSREVRlgRTGVDEIKCHPF 339
Cdd:cd14009    234 RRDPAE--RISFEEFFAHPF 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
77-293 2.03e-44

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 161.86  E-value: 2.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRS-DSAFFweERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd08215      1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKErEEALN--EVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgM 230
Cdd:cd08215     79 EYADGGDLAQKIKKQKkkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLEST-T 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  231 VRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd08215    158 DLAKTVVGTPYYLSPELCENKP----YNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIV 216
Pkinase pfam00069
Protein kinase domain;
78-340 1.51e-42

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 155.09  E-value: 1.51e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNI-LREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLgfihrdikpdnmlldrnghlkladfgtcmkmdstgmvrcDTA 236
Cdd:pfam00069   80 VEGGSLFDLLSEKGaFSEREAKFIMKQILEGLESGSSL---------------------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNS-LTFPDDIemSKNAKDLI 315
Cdd:pfam00069  121 VGTPWYMAPEVLGGNP----YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAfPELPSNL--SEEAKDLL 194
                          250       260
                   ....*....|....*....|....*
gi 1207153289  316 CAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:pfam00069  195 KKLLKKDPSK--RLTATQALQHPWF 217
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1310-1379 9.26e-42

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 147.49  E-value: 9.26e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1310 ERSLCIPHKGHEFVLTLYHFPSSCEVCPRPLWHVFRPPPALECRRCRVKCHKDHIDRKEEVLAPCRVNYD 1379
Cdd:cd20875      2 EKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
82-340 1.30e-41

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 153.95  E-value: 1.30e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14081      7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcMKMDSTGMVRCDTAVGTP 240
Cdd:cd14081     87 ELFDyLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFG--MASLQPEGSLLETSCGSP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemSKNAKDLICAFLS 320
Cdd:cd14081    165 HYACPEVIK---GEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKV--KRGVFHIPHFI--SPDAQDLLRRMLE 237
                          250       260
                   ....*....|....*....|
gi 1207153289  321 SREVRlgRTGVDEIKCHPFF 340
Cdd:cd14081    238 VNPEK--RITIEEIKKHPWF 255
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1314-1381 1.37e-41

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 146.70  E-value: 1.37e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289 1314 CIPHKGHEFVLTLYHFPSSCEVCPRPLWHVFRPPPALECRRCRVKCHKDHIDRKEEVLAPCRVNYDMS 1381
Cdd:cd20874      2 FLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
78-345 8.79e-41

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 152.51  E-value: 8.79e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05605      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcd 234
Cdd:cd05605     82 MNGGDLkfhIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPF--YSESL----VGTYGKIMDHKNSLTFPDDiems 308
Cdd:cd05605    160 GRVGTVGYMAPEVVKNE----RYTFSPDWWGLGCLIYEMIEGQAPFraRKEKVkreeVDRRVKEDQEEYSEKFSEE---- 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  309 knAKDlICAFLSSRE--VRLG--RTGVDEIKCHPFFKNDQW 345
Cdd:cd05605    232 --AKS-ICSQLLQKDpkTRLGcrGEGAEDVKSHPFFKSINF 269
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
76-360 4.64e-40

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 150.42  E-value: 4.64e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05608      1 DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGM 230
Cdd:cd05608     81 TIMNGGDLRYHIYNVDeenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVEL-KDGQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRCDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYseslvgTYGKIMDHK--------NSLTFP 302
Cdd:cd05608    160 TKTKGYAGTPGFMAPELLLGE----EYDYSVDYFTLGVTLYEMIAARGPFR------ARGEKVENKelkqrilnDSVTYS 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  303 DdiEMSKNAKDlICAFLSSREV--RLG-RTG-VDEIKCHPFFKNDQWTFDTIRDTMAPVVPE 360
Cdd:cd05608    230 E--KFSPASKS-ICEALLAKDPekRLGfRDGnCDGLRTHPFFRDINWRKLEAGILPPPFVPD 288
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
76-339 5.66e-40

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 148.94  E-value: 5.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSDS--AFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd14002      1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPK---RGKSEKelRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRc 233
Cdd:cd14002     78 VTEYAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVL- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 dTAV-GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAK 312
Cdd:cd14002    157 -TSIkGTPLYMAPELVQEQP----YDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIV--KDPVKWPS--NMSPEFK 227
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  313 DLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14002    228 SFLQGLLNKDPSK--RLSWPDLLEHPF 252
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
82-339 1.28e-39

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 148.32  E-value: 1.28e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14663      6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRCDTAVGT 239
Cdd:cd14663     86 ELFSkIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGlSALSEQFRQDGLLHTTCGT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDdiEMSKNAKDLICAFL 319
Cdd:cd14663    166 PNYVAPEVLARR---GYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIM--KGEFEYPR--WFSPGAKSLIKRIL 238
                          250       260
                   ....*....|....*....|
gi 1207153289  320 SSREVRlgRTGVDEIKCHPF 339
Cdd:cd14663    239 DPNPST--RITVEQIMASPW 256
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
83-359 1.82e-39

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 148.35  E-value: 1.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAF----SQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd05606      1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgGDCPFIVCMTYAFQTPDKLCFILDLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcmkmdstgmVRCD--- 234
Cdd:cd05606     81 NGGDLhYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLG----------LACDfsk 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 ----TAVGTPDYISPEVLmsQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESlvgTYGKIMDHKNSLT----FPDDie 306
Cdd:cd05606    151 kkphASVGTHGYMAPEVL--QKGVA-YDSSADWFSLGCMLYKLLKGHSPFRQHK---TKDKHEIDRMTLTmnveLPDS-- 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  307 MSKNAKDLICAFLsSREV--RLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVP 359
Cdd:cd05606    223 FSPELKSLLEGLL-QRDVskRLGclGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
72-339 1.92e-38

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 144.71  E-value: 1.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd14116      1 QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDST 228
Cdd:cd14116     81 YLILEYAPLGTVyreLQKLSKFD--EQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 gmvRCDTAVGTPDYISPEvlMSQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemS 308
Cdd:cd14116    159 ---RRTTLCGTLDYLPPE--MIEGRM--HDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRI--SRVEFTFPDFV--T 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  309 KNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14116    228 EGARDLISRLLKHNPSQ--RPMLREVLEHPW 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
77-279 2.45e-38

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 144.78  E-value: 2.45e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd14069      2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENI-KKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR-CD 234
Cdd:cd14069     81 YASGGELFdKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERlLN 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  235 TAVGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd14069    161 KMCGTLPYVAPELL---AKKKYRAEPVDVWSCGIVLFAMLAGELP 202
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
78-342 7.92e-38

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 143.89  E-value: 7.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05607      4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVrcD 234
Cdd:cd05607     84 MNGGDLkyhIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPI--T 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF--YSESLVGTYGKIMDHKNSLTFPDDIeMSKNAK 312
Cdd:cd05607    162 QRAGTNGYMAPEILKEES----YSYPVDWFAMGCSIYEMVAGRTPFrdHKEKVSKEELKRRTLEDEVKFEHQN-FTEEAK 236
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  313 DLICAFLSSR-EVRLG-RTGVDEIKCHPFFKN 342
Cdd:cd05607    237 DICRLFLAKKpENRLGsRTNDDDPRKHEFFKS 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
84-280 9.60e-38

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 142.29  E-value: 9.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKvSQQVyAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd13999      1 IGSGSFGEVYKGKWR-GTDV-AIKKL-KVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIPEEWAQFytaeVVLALDA------IHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd13999     78 YDLLHKKKIPLSWSLR----LKIALDIargmnyLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKM-TGVV 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd13999    153 GTPRWMAPEVLRGEP----YTEKADVYSFGIVLWELLTGEVPF 191
C1_ROCK cd20813
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil ...
1314-1377 4.03e-37

protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil containing protein kinase (ROCK) family; ROCK is a serine/threonine protein kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410363  Cd Length: 65  Bit Score: 133.93  E-value: 4.03e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289 1314 CIPHKGHEFVLTLYHFPSSCEVCPRPLWHVFRPPPALECRRCRVKCHKDHIDRKEEVLAPCRVN 1377
Cdd:cd20813      2 TISHKGHEFVEITFHMPTTCDVCHKPLWHLFKPPPALECKRCRMKIHKDHVDKEEYFIPPCKVN 65
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
77-293 4.18e-37

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 140.99  E-value: 4.18e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQ--LSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd08530      1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEvnLGSLSQKEREDSV---NEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTG 229
Cdd:cd08530     78 MEYAPFGDLSKLISKRKkkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS-KVLKKN 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  230 MVRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd08530    157 LAK--TQIGTPLYAAPEVWKGRP----YDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVC 214
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
82-284 4.51e-37

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 141.38  E-value: 4.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDSAFFWEERDIM-------AFSQsPWIVQLCCAFQDEKYLYLV 154
Cdd:cd14084     12 RTLGSGACGEVKLAYDKSTCKKVAIKIINK-RKFTIGSRREINKPRNIEteieilkKLSH-PCIIKIEDFFDAEDDYYIV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMDSTGM 230
Cdd:cd14084     90 LELMEGGELFDrVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGETSL 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  231 VRcdTAVGTPDYISPEVLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14084    170 MK--TLCGTPTYLAPEVLRSFGTEG-YTRAVDCWSLGVILFICLSGYPPFSEEY 220
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
78-315 4.85e-37

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 140.92  E-value: 4.85e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFE------MVKrsdsaffwEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd14095      2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKckgkehMIE--------NEVAILRRVKHPNIVQLIEEYDTDTEL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG----HLKLADFGTCMKMD 226
Cdd:cd14095     74 YLVMELVKGGDLFdAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 STGMVRCdtavGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS-----ESLvgtYGKIMDHKNSLTF 301
Cdd:cd14095    154 EPLFTVC----GTPTYVAPEILAETG----YGLKVDIWAAGVITYILLCGFPPFRSpdrdqEEL---FDLILAGEFEFLS 222
                          250
                   ....*....|....*.
gi 1207153289  302 P--DDIemSKNAKDLI 315
Cdd:cd14095    223 PywDNI--SDSAKDLI 236
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
78-342 6.07e-37

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 141.28  E-value: 6.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05631      2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIP---EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcd 234
Cdd:cd05631     82 MNGGDLKFHIYNMGNPgfdEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVR-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF--YSESLVGTYGKIMDHKNSLTFPDdiEMSKNAK 312
Cdd:cd05631    160 GRVGTVGYMAPEVINNEK----YTFSPDWWGLGCLIYEMIQGQSPFrkRKERVKREEVDRRVKEDQEEYSE--KFSEDAK 233
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1207153289  313 DlICAFLSSRE--VRLGRT--GVDEIKCHPFFKN 342
Cdd:cd05631    234 S-ICRMLLTKNpkERLGCRgnGAAGVKQHPIFKN 266
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-316 6.69e-37

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 140.58  E-value: 6.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14083      3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDS--LENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML---LDRNGHLKLADFGTCmKMDSTG 229
Cdd:cd14083     81 ELVTGGELfdrIVEKGSYT--EKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLS-KMEDSG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFP--DDIem 307
Cdd:cd14083    158 VM--STACGTPGYVAPEVLAQKP----YGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPywDDI-- 229

                   ....*....
gi 1207153289  308 SKNAKDLIC 316
Cdd:cd14083    230 SDSAKDFIR 238
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
84-339 7.67e-37

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 141.24  E-value: 7.67e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVK----------RSDSAFFWEERDIMAFSQSPW-------------IVQ 140
Cdd:cd14200      8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKqygfprrpppRGSKAAQGEQAKPLAPLERVYqeiailkkldhvnIVK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  141 LCCAFQD--EKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLAD 218
Cdd:cd14200     88 LIEVLDDpaEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIAD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  219 FGTCMKMDSTGMVRCDTAvGTPDYISPEVLmSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdhKNS 298
Cdd:cd14200    168 FGVSNQFEGNDALLSSTA-GTPAFMAPETL-SDSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI---KNK 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  299 -LTFPDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14200    243 pVEFPEEPEISEELKDLILKMLDKNPET--RITVPEIKVHPW 282
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
75-341 7.89e-37

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 140.77  E-value: 7.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd14117      5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDStgmVRC 233
Cdd:cd14117     85 LEYAPRGELYKeLQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPS---LRR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEvlMSQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPddIEMSKNAKD 313
Cdd:cd14117    162 RTMCGTLDYLPPE--MIEGRT--HDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIV--KVDLKFP--PFLSDGSRD 233
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  314 LICAFLssREVRLGRTGVDEIKCHPFFK 341
Cdd:cd14117    234 LISKLL--RYHPSERLPLKGVMEHPWVK 259
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
77-319 1.38e-36

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 139.92  E-value: 1.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK--FEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd14098      1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkVAGNDKNLQLF-QREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG--HLKLADFGTCmKMDSTGMV 231
Cdd:cd14098     80 MEYVEGGDLMDfIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLA-KVIHTGTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 rCDTAVGTPDYISPEVLMS--QGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFP--DDIEM 307
Cdd:cd14098    159 -LVTFCGTMAYLAPEILMSkeQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRI--RKGRYTQPplVDFNI 235
                          250
                   ....*....|..
gi 1207153289  308 SKNAKDLICAFL 319
Cdd:cd14098    236 SEEAIDFILRLL 247
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
76-341 2.84e-36

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 138.63  E-value: 2.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQlskfeMVKRSDSAFFWE---ERDIMAFSQSPWIVQLCCAFQDEKYLY 152
Cdd:cd06605      1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKV-----IRLEIDEALQKQilrELDVLHKCNSPYIVGFYGAFYSEGDIS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLDRNGHLKLADFGTcmkmdSTGM 230
Cdd:cd06605     76 ICMEYMDGGSLdKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGV-----SGQL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VR--CDTAVGTPDYISPEVLmsQGGTgyYGRECDWWSVGVFIYELLVGDTPfYSESLVGTYGKIMD------HKNSLTFP 302
Cdd:cd06605    151 VDslAKTFVGTRSYMAPERI--SGGK--YTVKSDIWSLGLSLVELATGRFP-YPPPNAKPSMMIFEllsyivDEPPPLLP 225
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207153289  303 DDiEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFK 341
Cdd:cd06605    226 SG-KFSPDFQDFVSQCLQKDPTE--RPSYKELMEHPFIK 261
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
76-342 2.96e-36

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 140.49  E-value: 2.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05632      2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDIP---EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd05632     82 TIMNGGDLKFHIYNMGNPgfeEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 cdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYseslvGTYGKIMDHKNSLTFPDDIE-----M 307
Cdd:cd05632    162 --GRVGTVGYMAPEVLNNQ----RYTLSPDYWGLGCLIYEMIEGQSPFR-----GRKEKVKREEVDRRVLETEEvysakF 230
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207153289  308 SKNAKDlICAFLSSREV--RLG--RTGVDEIKCHPFFKN 342
Cdd:cd05632    231 SEEAKS-ICKMLLTKDPkqRLGcqEEGAGEVKRHPFFRN 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
77-292 3.20e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 138.83  E-value: 3.20e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQD--EKYLYLV 154
Cdd:cd08217      1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLV-SEVNILRELKHPNIVRYYDRIVDraNTTLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLG-----FIHRDIKPDNMLLDRNGHLKLADFGTCmK 224
Cdd:cd08217     80 MEYCEGGDLAQLIKKCKkenqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLA-R 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  225 MDSTGMVRCDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKI 292
Cdd:cd08217    159 VLSHDSSFAKTYVGTPYYMSPELLNEQ----SYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKI 222
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
84-319 7.71e-36

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 137.01  E-value: 7.71e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAmkqlSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFA----AKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD--RNGHLKLADFGTCMKMDSTGMVRCDTavGTP 240
Cdd:cd14006     77 LDrLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEELKEIF--GTP 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  241 DYISPEVLMSQGGTGyygrECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFL 319
Cdd:cd14006    155 EFVAPEIVNGEPVSL----ATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLL 229
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
82-281 2.21e-35

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 135.82  E-value: 2.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd06627      6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVM-GEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmVRCDTAVGTP 240
Cdd:cd06627     85 SLASIIKKFgKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVE-KDENSVVGTP 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  241 DYISPEVL-MSQGGTgyygrECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd06627    164 YWMAPEVIeMSGVTT-----ASDIWSVGCTVIELLTGNPPYY 200
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
84-338 2.46e-35

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 135.97  E-value: 2.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEM------VKRsdsaffweERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14078     11 IGSGGFAKVKLATHILTGEKVAIKIMDKKALgddlprVKT--------EIEALKNLSHQHICRLYHVIETDNKIFMVLEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTA 236
Cdd:cd14078     83 CPGGELFDYIVAKDrLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHLETC 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLtfPDdiEMSKNAKDLIC 316
Cdd:cd14078    163 CGSPAYAAPELIQ---GKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEE--PE--WLSPSSKLLLD 235
                          250       260
                   ....*....|....*....|..
gi 1207153289  317 AFLSSREVRlgRTGVDEIKCHP 338
Cdd:cd14078    236 QMLQVDPKK--RITVKELLNHP 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
82-340 2.52e-35

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 135.89  E-value: 2.52e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQL---VRHKVsqQVyAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd14162      6 KTLGHGSYAVVKKaysTKHKC--KV-AIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLVTLT-SNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG---TCMKMDSTGMVRCD 234
Cdd:cd14162     83 ENGDLLDYIrKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGfarGVMKTKDGKPKLSE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVgtygKIMDH-KNSLTFPDDIEMSKNAKD 313
Cdd:cd14162    163 TYCGSYAYASPEILR---GIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLK----VLLKQvQRRVVFPKNPTVSEECKD 235
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  314 LICAFLSSREVRLgrtGVDEIKCHPFF 340
Cdd:cd14162    236 LILRMLSPVKKRI---TIEEIKRDPWF 259
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
77-293 2.79e-35

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 135.62  E-value: 2.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQ--LSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd08529      1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAI---DEARVLSKLNSPYVIKYYDSFVDKGKLNIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMV 231
Cdd:cd08529     78 MEYAENGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVA-KILSDTTN 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  232 RCDTAVGTPDYISPEvlMSQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd08529    157 FAQTIVGTPYYLSPE--LCEDKP--YNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIV 214
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
78-284 2.81e-35

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 135.42  E-value: 2.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfeMVKRSDSAFFWEERdIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06614      2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMR---LRKQNKELIINEIL-IMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIP--EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGMVRCDT 235
Cdd:cd06614     78 MDGGSLTDIITQNPVRmnESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL-TKEKSKRNS 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  236 AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd06614    157 VVGTPYWMAPEVIKRKD----YGPKVDIWSLGIMCIEMAEGEPPYLEEP 201
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
82-339 1.58e-34

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 133.68  E-value: 1.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFS--QSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd06632      6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSklRHPNIVQYYGTEREEDNLYIFLEYVP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcdTAVG 238
Cdd:cd06632     86 GGSIHKLLQRYGaFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK--SFKG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  239 TPDYISPEVLMSQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDieMSKNAKDLICAF 318
Cdd:cd06632    164 SPYWMAPEVIMQKNSG--YGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIPDH--LSPDAKDFIRLC 239
                          250       260
                   ....*....|....*....|.
gi 1207153289  319 LSSREVRlgRTGVDEIKCHPF 339
Cdd:cd06632    240 LQRDPED--RPTASQLLEHPF 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
78-343 1.92e-34

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 134.35  E-value: 1.92e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14166      5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSS---LENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCmKMDSTGMVrc 233
Cdd:cd14166     82 VSGGELFDRILERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS-KMEQNGIM-- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFP--DDIemSKNA 311
Cdd:cd14166    159 STACGTPGYVAPEVLAQKP----YSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPfwDDI--SESA 232
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  312 KDLICAFLSSREVRlgRTGVDEIKCHPFFKND 343
Cdd:cd14166    233 KDFIRHLLEKNPSK--RYTCEKALSHPWIIGN 262
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
78-342 2.01e-34

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 134.00  E-value: 2.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05630      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcd 234
Cdd:cd05630     82 MNGGDLkfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIK-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYS----------ESLVgtygKIMDHKNSLTFpdd 304
Cdd:cd05630    160 GRVGTVGYMAPEVVKNE----RYTFSPDWWALGCLLYEMIAGQSPFQQrkkkikreevERLV----KEVPEEYSEKF--- 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  305 iemSKNAKDLiCAFLSSREV--RLG--RTGVDEIKCHPFFKN 342
Cdd:cd05630    229 ---SPQARSL-CSMLLCKDPaeRLGcrGGGAREVKEHPLFKK 266
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
76-281 4.52e-34

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 132.00  E-value: 4.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEmvkrsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd06612      3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE-----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGG---DLVTLTsNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVR 232
Cdd:cd06612     78 EYCGAGsvsDIMKIT-NKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDT-MAK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd06612    156 RNTVIGTPFWMAPEVIQEIG----YNNKADIWSLGITAIEMAEGKPPYS 200
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
76-279 7.74e-34

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 131.98  E-value: 7.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDSAFFWEERDIMAFSQ--SPWIVQLCCAFQDEKYLYL 153
Cdd:cd06609      1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID----LEEAEDEIEDIQQEIQFLSQcdSPYITKYYGSFLKGSKLWI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVRC 233
Cdd:cd06609     77 IMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTST-MSKR 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  234 DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06609    156 NTFVGTPFWMAPEVIKQSG----YDEKADIWSLGITAIELAKGEPP 197
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
77-340 8.45e-34

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 131.35  E-value: 8.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvKRSDSAFFWEERD---------IMAF---SQSPWIVQLCCA 144
Cdd:cd14004      1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFK----ERILVDTWVRDRKlgtvpleihILDTlnkRSHPNIVKLLDF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  145 FQDEKYLYLVME-FMPGGDLVTLT-SNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd14004     77 FEDDEFYYLVMEkHGSGMDLFDFIeRKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 MKMDSTgmvRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSeslvgtYGKIMDHKnsLTFP 302
Cdd:cd14004    157 AYIKSG---PFDTFVGTIDYAAPEVLR---GNPYGGKEQDIWALGVLLYTLVFKENPFYN------IEEILEAD--LRIP 222
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1207153289  303 DdiEMSKNAKDLICAFLsSREVRlGRTGVDEIKCHPFF 340
Cdd:cd14004    223 Y--AVSEDLIDLISRML-NRDVG-DRPTIEELLTDPWL 256
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
78-339 9.00e-34

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 131.38  E-value: 9.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERdIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14074      5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVR-CMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRNGHLKLADFGTCMKMDSTGMVrcD 234
Cdd:cd14074     84 GDGGDMYDYIMKHEngLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKL--E 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFY----SESLVgtygKIMDHKnsLTFPDDIemSKN 310
Cdd:cd14074    162 TSCGSLAYSAPEILL---GDEYDAPAVDIWSLGVILYMLVCGQPPFQeandSETLT----MIMDCK--YTVPAHV--SPE 230
                          250       260
                   ....*....|....*....|....*....
gi 1207153289  311 AKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14074    231 CKDLIRRMLIRDPKK--RASLEEIENHPW 257
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
84-339 1.70e-33

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 131.63  E-value: 1.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVK-----------------------RSDSAFFWEERDIMAFSQSPWIVQ 140
Cdd:cd14199     10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqpRGPIERVYQEIAILKKLDHPNVVK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  141 LCCAFQD--EKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLAD 218
Cdd:cd14199     90 LVEVLDDpsEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIAD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  219 FGTCMKMDSTGMVRCDTaVGTPDYISPEVLmSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknS 298
Cdd:cd14199    170 FGVSNEFEGSDALLTNT-VGTPAFMAPETL-SETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQ--P 245
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  299 LTFPDDIEMSKNAKDLICAFLSSREVrlGRTGVDEIKCHPF 339
Cdd:cd14199    246 LEFPDQPDISDDLKDLLFRMLDKNPE--SRISVPEIKLHPW 284
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
82-340 1.75e-33

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 130.77  E-value: 1.75e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAM------KQLSKFEMVKRsdsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14080      6 KTIGEGSYSKVKLAEYTKSGLKEKVackiidKKKAPKDFLEK----FLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG---TCmkMDSTGMV 231
Cdd:cd14080     82 EYAEHGDLLEYIQKRGaLSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLC--PDDDGDV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPDDIEM-SKN 310
Cdd:cd14080    160 LSKTFCGSAAYAAPEILQ---GIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRK--VRFPSSVKKlSPE 234
                          250       260       270
                   ....*....|....*....|....*....|
gi 1207153289  311 AKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14080    235 CKDLIDQLLEPDPTK--RATIEEILNHPWL 262
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
82-282 2.34e-33

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 130.07  E-value: 2.34e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14185      6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKED--MIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH----LKLADFGtcMKMDSTGMVRcdTA 236
Cdd:cd14185     84 DLFdAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDksttLKLADFG--LAKYVTGPIF--TV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd14185    160 CGTPTYVAPEILSEKG----YGLEVDMWAAGVILYILLCGFPPFRS 201
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
78-280 3.10e-33

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 129.82  E-value: 3.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14073      3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcdTA 236
Cdd:cd14073     83 ASGGELYDYISErRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQ--TF 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  237 VGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14073    161 CGSPLYASPEIV---NGTPYQGPEVDCWSLGVLLYTLVYGTMPF 201
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-315 1.45e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 128.19  E-value: 1.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDSAFF---WEERDIMAFSQSPWIVqlccafqdeKY------ 150
Cdd:cd06626      4 RGNKIGEGTFGKVYTAVNLDTGELMAMKEIR----FQDNDPKTIkeiADEMKVLEGLDHPNLV---------RYygvevh 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 ---LYLVMEFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM- 225
Cdd:cd06626     71 reeVYIFMEYCQEGTLEELLRHGRIlDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLk 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRC---DTAVGTPDYISPEVLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYseSLVGTYgKIMDH---KNSL 299
Cdd:cd06626    151 NNTTTMAPgevNSLVGTPAYMAPEVITGNKGEG-HGRAADIWSLGCVVLEMATGKRPWS--ELDNEW-AIMYHvgmGHKP 226
                          250
                   ....*....|....*.
gi 1207153289  300 TFPDDIEMSKNAKDLI 315
Cdd:cd06626    227 PIPDSLQLSPEGKDFL 242
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
81-319 1.49e-32

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 127.64  E-value: 1.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERdIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14072      5 LKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVR-IMKILNHPNIVKLFEVIETEKTLYLVMEYASG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcMKMDSTGMVRCDTAVGT 239
Cdd:cd14072     84 GEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFG--FSNEFTPGNKLDTFCGS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFpddiEMSKNAKDLICAFL 319
Cdd:cd14072    162 PPYAAPELFQ---GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKFL 234
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-315 1.72e-32

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 127.84  E-value: 1.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffweERDIMAFSQ--SPWIVQLCCAFQDEKYLYL 153
Cdd:cd14167      3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSI----ENEIAVLHKikHPNIVALDDIYESGGHLYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLvtltsnYD-IPEEwaQFYTA--------EVVLALDAIHSLGFIHRDIKPDNML---LDRNGHLKLADFGT 221
Cdd:cd14167     79 IMQLVSGGEL------FDrIVEK--GFYTErdasklifQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  222 CmKMDSTGMVrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTF 301
Cdd:cd14167    151 S-KIEGSGSV-MSTACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDS 224
                          250
                   ....*....|....*.
gi 1207153289  302 P--DDIemSKNAKDLI 315
Cdd:cd14167    225 PywDDI--SDSAKDFI 238
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
84-340 1.73e-32

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 127.81  E-value: 1.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHK--VSQQVYAMKQLSKfemvKRSDS------AFFWEERDIMAFSQSPWIVQLCCAFQDEKYLY-LV 154
Cdd:cd13994      1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRR----RDDESkrkdyvKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIP--EEWAQFYtAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM----DST 228
Cdd:cd13994     77 MEYCPGGDLFTLIEKADSLslEEKDCFF-KQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgmpaEKE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMVRCDtAVGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVGDTPF----YSESLVGTYGKIMDHKNSLTFPDD 304
Cdd:cd13994    156 SPMSAG-LCGSEPYMAPEVF---TSGSYDGRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIE 231
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207153289  305 IEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd13994    232 NLLPSECRRLIYRMLHPDPEK--RITIDEALNDPWV 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
77-341 3.81e-32

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 126.79  E-value: 3.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd06648      8 DLDNFVKIGEGSTGIVCIATDKSTGRQVAVK---KMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGMVRCDTA 236
Cdd:cd06648     85 FLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV-SKEVPRRKSL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsltfPDDIEMSKNAKDLIC 316
Cdd:cd06648    164 VGTPYWMAPEVISRLP----YGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNE-----PPKLKNLHKVSPRLR 234
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  317 AFLSSREVR--LGRTGVDEIKCHPFFK 341
Cdd:cd06648    235 SFLDRMLVRdpAQRATAAELLNHPFLA 261
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
77-373 4.03e-32

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 128.63  E-value: 4.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDEKYLYL 153
Cdd:cd14223      1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgmvR 232
Cdd:cd14223     81 ILDLMNGGDLHYHLSQHGVfSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKK---K 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDYISPEVLmsQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESlvgTYGKIMDHKNSLT----FPDDI--E 306
Cdd:cd14223    158 PHASVGTHGYMAPEVL--QKGVA-YDSSADWFSLGCMLFKLLRGHSPFRQHK---TKDKHEIDRMTLTmaveLPDSFspE 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  307 MSKNAKDLICAFLSSREVRLGRtGVDEIKCHPFFKNDQWTFDTIRDTMAPVVP-----ELSSDIDTSNFDDD 373
Cdd:cd14223    232 LRSLLEGLLQRDVNRRLGCMGR-GAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDEE 302
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
82-340 5.04e-32

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 126.23  E-value: 5.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEM--------VKRsdsaffweERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd14079      8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIksldmeekIRR--------EIQILKLFRHPHIIRLYEVIETPTDIFM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd14079     80 VMEYVSGGELFDyIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 cdTAVGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhkNSLTFPDdiEMSKNAK 312
Cdd:cd14079    160 --TSCGSPNYAAPEVI---SGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKS--GIYTIPS--HLSPGAR 230
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  313 DLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14079    231 DLIKRMLVVDPLK--RITIPEIRQHPWF 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
81-340 1.76e-31

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 124.27  E-value: 1.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsaffweERDIMA------FSQSPWIVQLCCAF--QDEKYLY 152
Cdd:cd05118      4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAA------LREIKLlkhlndVEGHPNIVKLLDVFehRGGNHLC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMpGGDLVTL--TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFGTCMKMDSTG 229
Cdd:cd05118     78 LVFELM-GMNLYELikDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFTSPP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MvrcDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVgtygkimDHKNSLTfpdDIEMSK 309
Cdd:cd05118    157 Y---TPYVATRWYRAPEVLL---GAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEV-------DQLAKIV---RLLGTP 220
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1207153289  310 NAKDLICAFL--SSREvrlgRTGVDEIKCHPFF 340
Cdd:cd05118    221 EALDLLSKMLkyDPAK----RITASQALAHPYF 249
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
72-373 1.98e-31

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 127.10  E-value: 1.98e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQS---PWIVQLCCAFQDE 148
Cdd:cd05633      1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd05633     81 DKLCFILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TgmvRCDTAVGTPDYISPEVLmsQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESLvgtygKIMDHKNSLTFPDDIEM 307
Cdd:cd05633    161 K---KPHASVGTHGYMAPEVL--QKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHKT-----KDKHEIDRMTLTVNVEL 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  308 ----SKNAKDLICAFLsSREV--RLG--RTGVDEIKCHPFFKNDQWTFDTIRDTMAPVVP-----ELSSDIDTSNFDDD 373
Cdd:cd05633    230 pdsfSPELKSLLEGLL-QRDVskRLGchGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDEE 307
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
136-340 2.56e-31

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 124.77  E-value: 2.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  136 PWIVQLCCAFQDEKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHL 214
Cdd:cd14093     69 PNIIELHDVFESPTFIFLVFELCRKGELFDyLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  215 KLADFGTCMKMDSTGMVRcdTAVGTPDYISPEVL---MSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGK 291
Cdd:cd14093    149 KISDFGFATRLDEGEKLR--ELCGTPGYLAPEVLkcsMYDNAPG-YGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRN 225
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  292 IMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14093    226 IMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKK--RLTAEEALEHPFF 272
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
80-315 4.48e-31

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 123.62  E-value: 4.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDSAFFWE----ERDIMAFS--QSPWIVQLCCAFQDEKYLYL 153
Cdd:cd06625      4 QGKLLGQGAFGQVYLCYDADTGRELAVKQVE----IDPINTEASKEvkalECEIQLLKnlQHERIVQYYGCLQDEKSLSI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD----ST 228
Cdd:cd06625     80 FMEYMPGGSVKDEIKAYGaLTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQticsST 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMvrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYgKIMDHKNSLTFPDDIem 307
Cdd:cd06625    160 GM---KSVTGTPYWMSPEVINGEG----YGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIF-KIATQPTNPQLPPHV-- 229

                   ....*...
gi 1207153289  308 SKNAKDLI 315
Cdd:cd06625    230 SEDARDFL 237
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
77-284 6.91e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 122.78  E-value: 6.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQL---SKFEMVKRSDsaffwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd08219      1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlpKSSSAVEDSR-----KEAVLLAKMKHPNIVAFKESFEADGHLYI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd08219     76 VMEYCDGGDLmqkIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  231 VRCdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd08219    156 YAC-TYVGTPYYVPPEIWENMP----YNNKSDIWSLGCILYELCTLKHPFQANS 204
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
76-280 7.49e-31

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 123.57  E-value: 7.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ------DEK 149
Cdd:cd06608      6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIM---DIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIkkdppgGDD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGG---DLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK 224
Cdd:cd06608     83 QLWLVMEYCGGGsvtDLVkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  225 MDSTGMVRcDTAVGTPDYISPEVLM-SQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06608    163 LDSTLGRR-NTFIGTPYWMAPEVIAcDQQPDASYDARCDVWSLGITAIELADGKPPL 218
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
84-339 7.51e-31

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 124.09  E-value: 7.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAV-QLVRHKVSQQVYAMKQLSKFEM----VKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd14096      9 IGEGAFSNVyKAVPLRNTGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL----VTLTSnydIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR------------------------ 210
Cdd:cd14096     89 DGGEIfhqiVRLTY---FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddetkvdege 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  211 ---------NGHLKLADFGTCMKM-DSTGMVRCdtavGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14096    166 fipgvggggIGIVKLADFGLSKQVwDSNTKTPC----GTVGYTAPEVVKDE----RYSKKVDMWALGCVLYTLLCGFPPF 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  281 YSESLVGTYGKIMDHKNSLTFP--DDIemSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14096    238 YDESIETLTEKISRGDYTFLSPwwDEI--SKSAKDLISHLLTVDPAK--RYDIDEFLAHPW 294
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
84-339 1.47e-30

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 122.01  E-value: 1.47e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQ-QVYAMKQLSKFEMVKRSDSAFFWEERdIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14121      3 LGSGTYATVYKAYRKSGArEVVAVKCVSKSSLNKASTENLLTEIE-LLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR--NGHLKLADFGTCMKM---DSTGMVRcdta 236
Cdd:cd14121     82 LSRFIRSRRTlPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSryNPVLKLADFGFAQHLkpnDEAHSLR---- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 vGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnSLTFPDDIEMSKNAKDLIC 316
Cdd:cd14121    158 -GSPLYMAPEMILKK----KYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSK-PIEIPTRPELSADCRDLLL 231
                          250       260
                   ....*....|....*....|...
gi 1207153289  317 AFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14121    232 RLLQRDPDR--RISFEEFFAHPF 252
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
76-339 3.35e-30

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 121.12  E-value: 3.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14186      1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDIP--EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDSTgmv 231
Cdd:cd14186     81 EMCHNGEMSRYLKNRKKPftEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGlaTQLKMPHE--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDIemSKNA 311
Cdd:cd14186    158 KHFTMCGTPNYISPEIATRSA----HGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVV--LADYEMPAFL--SREA 229
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  312 KDLICAFLssREVRLGRTGVDEIKCHPF 339
Cdd:cd14186    230 QDLIHQLL--RKNPADRLSLSSVLDHPF 255
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
78-340 3.86e-30

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 121.62  E-value: 3.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMK---------QLSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDE 148
Cdd:cd14181     12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKiievtaerlSPEQLEEVRSSTLK---EIHILRQVSGHPSIITLIDSYESS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd14181     89 TFIFLVFDLMRRGELFDyLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEP 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRcdTAVGTPDYISPEVL---MSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDD 304
Cdd:cd14181    169 GEKLR--ELCGTPGYLAPEILkcsMDETHPG-YGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEW 245
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207153289  305 IEMSKNAKDLICAFLS-SREVRLgrtGVDEIKCHPFF 340
Cdd:cd14181    246 DDRSSTVKDLISRLLVvDPEIRL---TAEQALQHPFF 279
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
84-320 4.20e-30

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 121.59  E-value: 4.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSDSaffwEERDI-MAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14091      8 IGKGSYSVCKRCIHKATGKEYAVKIIDK---SKRDPS----EEIEIlLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRNGH---LKLADFGTCMKM-DSTG--MVRCD 234
Cdd:cd14091     81 LLDrILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQLrAENGllMTPCY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAvgtpDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS---ESLVGTYGKIMDHKNSLTFPDDIEMSKNA 311
Cdd:cd14091    161 TA----NFVAPEVLKKQG----YDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARIGSGKIDLSGGNWDHVSDSA 232

                   ....*....
gi 1207153289  312 KDLICAFLS 320
Cdd:cd14091    233 KDLVRKMLH 241
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-358 9.59e-30

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 120.60  E-value: 9.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14086      1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR-DHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTltsnyDI------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCMKMD 226
Cdd:cd14086     80 DLVTGGELFE-----DIvarefySEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 STGMVRCDTAvGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIE 306
Cdd:cd14086    155 GDQQAWFGFA-GTPGYLSPEVLRKDP----YGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDT 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  307 MSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFKNdqwtfdtiRDTMAPVV 358
Cdd:cd14086    230 VTPEAKDLINQMLTVNPAK--RITAAEALKHPWICQ--------RDRVASMV 271
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
78-280 1.01e-29

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 120.27  E-value: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDIMA---FSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd06917      3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNL--DTDDDDVSDIQKEVALLSqlkLGQPKNIIKYYGSYLKGPSLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcD 234
Cdd:cd06917     81 MDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKR-S 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  235 TAVGTPDYISPEVLMSqggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06917    160 TFVGTPYWMAPEVITE---GKYYDTKADIWSLGITTYEMATGNPPY 202
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
83-361 1.08e-29

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 120.72  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVSQQVYAMK--QLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14094     10 VIGKGPFSVVRRCIHRETGQQFAVKivDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDL----VTLTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd14094     90 ADLcfeiVKRADAgFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLVA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTaVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSeSLVGTYGKIMDHKNSLTFPDDIEMSKNAK 312
Cdd:cd14094    170 GGR-VGTPHFMAPEVVKRE----PYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAK 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  313 DLICAFLSSREVRlgRTGVDEIKCHPFFKNDQwtFDTIRDTMAPVVPEL 361
Cdd:cd14094    244 DLVRRMLMLDPAE--RITVYEALNHPWIKERD--RYAYRIHLPETVEQL 288
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
87-340 1.34e-29

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 119.57  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   87 GAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRsdsaffwEERDIMAFSqSPWIVQLCCAFQDEKYLYLVMEFMPGGDL--- 163
Cdd:cd05576     10 GVIDKVLLVMDTRTQETFILKGLRKSSEYSR-------ERKTIIPRC-VPNMVCLRKYIISEESVFLVLQHAEGGKLwsy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 --------------------VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM 223
Cdd:cd05576     82 lskflndkeihqlfadlderLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  224 KMDSTgmvrCDTAVGTPDYISPEVlmsqGGTGYYGRECDWWSVGVFIYELLVGdtpfysESLVGTYGKIMDHKNSLTFPD 303
Cdd:cd05576    162 EVEDS----CDSDAIENMYCAPEV----GGISEETEACDWWSLGALLFELLTG------KALVECHPAGINTHTTLNIPE 227
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1207153289  304 DIemSKNAKDLICAFLSSREVR---LGRTGVDEIKCHPFF 340
Cdd:cd05576    228 WV--SEEARSLLQQLLQFNPTErlgAGVAGVEDIKSHPFF 265
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
84-340 1.34e-29

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 119.28  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQ--SPWIVQLCCAFQDE--KYLYLVMEFMP 159
Cdd:cd14119      1 LGEGSYGKVKEVLDTETLCRRAVKIL-KKRKLRRIPNGEANVKREIQILRRlnHRNVIKLVDVLYNEekQKLYMVMEYCV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS-TGMVRCDTA 236
Cdd:cd14119     80 GGLQEMLDSAPDkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLfAEDDTCTTS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVlmSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIEmsKNAKDLIC 316
Cdd:cd14119    160 QGSPAFQPPEI--ANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENI--GKGEYTIPDDVD--PDLQDLLR 233
                          250       260
                   ....*....|....*....|....*
gi 1207153289  317 AFLSSR-EVRLgrtGVDEIKCHPFF 340
Cdd:cd14119    234 GMLEKDpEKRF---TIEQIRQHPWF 255
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
82-315 1.49e-29

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 119.32  E-value: 1.49e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRsdsaffweERDI-MAFSQSPWIVQLC----CAFQDEKYLYLVME 156
Cdd:cd14089      7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARR--------EVELhWRASGCPHIVRIIdvyeNTYQGRKCLLVVME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTltsnyDIPEEWAQFYT----AEVV----LALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGtcMKM 225
Cdd:cd14089     79 CMEGGELFS-----RIQERADSAFTereaAEIMrqigSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFG--FAK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLV----GTYGKIMDhkNSLTF 301
Cdd:cd14089    152 ETTTKKSLQTPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaispGMKKRIRN--GQYEF 225
                          250
                   ....*....|....*.
gi 1207153289  302 PDD--IEMSKNAKDLI 315
Cdd:cd14089    226 PNPewSNVSEEAKDLI 241
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
80-370 2.27e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 120.10  E-value: 2.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvkRSDSAffwEERDIMAFSQS-PWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd14092     10 REEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-----RLDTS---REVQLLRLCQGhPNIVKLHEVFQDELHTYLVMELL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLVtltsnyDIPEEWAQFYTAE-------VVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFG-TCMKMDS 227
Cdd:cd14092     82 RGGELL------ERIRKKKRFTESEasrimrqLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGfARLKPEN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMvrcDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIE- 306
Cdd:cd14092    156 QPL---KTPCFTLPYAAPEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDFSFDGEe 232
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  307 ---MSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFKNDQWTFDTirDTMAPVVPELSSDIDTSNF 370
Cdd:cd14092    233 wknVSSEAKSLIQGLLTVDPSK--RLTMSELRNHPWLQGSSSPSST--PLMTPGVLSSSAAAVSTAL 295
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
84-345 2.38e-29

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 118.59  E-value: 2.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfweERDI--MAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14075     10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLL---SREIssMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDSTgmvrCDTAVG 238
Cdd:cd14075     87 ELYTkISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfsTHAKRGET----LNTFCG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  239 TPDYISPEVLMSqggTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhkNSLTFPDDIemSKNAKDLICAF 318
Cdd:cd14075    163 SPPYAAPELFKD---EHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILE--GTYTIPSYV--SEPCQELIRGI 235
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  319 LssREVRLGRTGVDEIkchpffKNDQW 345
Cdd:cd14075    236 L--QPVPSDRYSIDEI------KNSEW 254
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
77-281 3.04e-29

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 118.18  E-value: 3.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd06613      1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK---LEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLtsnYD----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVR 232
Cdd:cd06613     78 YCGGGSLQDI---YQvtgpLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAT-IAK 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGGTGYYGReCDWWSVGVFIYELLVGDTPFY 281
Cdd:cd06613    154 RKSFIGTPYWMAPEVAAVERKGGYDGK-CDIWALGITAIELAELQPPMF 201
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
84-319 5.53e-29

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 117.33  E-value: 5.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQlskFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAAKF---IKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 V--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH-LKLADFGTCMKMDSTGMVRcdTAVGT 239
Cdd:cd14103     78 FerVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLK--VLFGT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLmSQGGTGYygrECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFL 319
Cdd:cd14103    156 PEFVAPEVV-NYEPISY---ATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLL 231
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
76-341 5.55e-29

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 118.09  E-value: 5.55e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMK-------QLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDE 148
Cdd:cd14182      3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKiiditggGSFSPEEVQELREATLKEIDILRKVSGHPNIIQLKDTYETN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd14182     83 TFFFLVFDLMKKGELFDyLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRcdTAVGTPDYISPEVL---MSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDD 304
Cdd:cd14182    163 GEKLR--EVCGTPGYLAPEIIecsMDDNHPG-YGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEW 239
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207153289  305 IEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFK 341
Cdd:cd14182    240 DDRSDTVKDLISRFLVVQPQK--RYTAEEALAHPFFQ 274
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
77-339 5.61e-29

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 117.70  E-value: 5.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKvSQQVYAMKQLsKFEMVKRSDSAFFWEERDI-MAFSQSPWIVQLCCA--FQDEKYLYL 153
Cdd:cd14131      2 PYEILKQLGKGGSSKVYKVLNP-KKKIYALKRV-DLEGADEQTLQSYKNEIELlKKLKGSDRIIQLYDYevTDEDDYLYM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFmPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLdRNGHLKLADFG--TCMKMDST 228
Cdd:cd14131     80 VMEC-GEIDLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGiaKAIQNDTT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMVRcDTAVGTPDYISPEVL--MSQGGTGYY----GRECDWWSVGVFIYELLVGDTPFYseSLVGTYGK---IMDHKNSL 299
Cdd:cd14131    158 SIVR-DSQVGTLNYMSPEAIkdTSASGEGKPkskiGRPSDVWSLGCILYQMVYGKTPFQ--HITNPIAKlqaIIDPNHEI 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  300 TFPDdiEMSKNAKDLI--CAFLSSREvrlgRTGVDEIKCHPF 339
Cdd:cd14131    235 EFPD--IPNPDLIDVMkrCLQRDPKK----RPSIPELLNHPF 270
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
76-340 5.75e-29

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 117.84  E-value: 5.75e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSA-FFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd06610      1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRI---DLEKCQTSMdELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGdlvtltSNYDI----------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM- 223
Cdd:cd06610     78 MPLLSGG------SLLDImkssyprgglDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSAs 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  224 ---KMDSTGMVRcDTAVGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFY----SESLVGTYgkimdHK 296
Cdd:cd06610    152 latGGDRTRKVR-KTFVGTPCWMAPEVMEQVRG---YDFKADIWSFGITAIELATGAAPYSkyppMKVLMLTL-----QN 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  297 NSLTFPDDIEM---SKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd06610    223 DPPSLETGADYkkySKSFRKMISLCLQKDPSK--RPTAEELLKHKFF 267
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
75-340 6.37e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 118.55  E-value: 6.37e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFdrVKlIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd06659     23 LENY--VK-IGEGSTGVVCIAREKHSGRQVAVKMM---DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGMVRCD 234
Cdd:cd06659     97 MEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI-SKDVPKRK 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsltfPDDIEMSKNAKDL 314
Cdd:cd06659    176 SLVGTPYWMAPEVISRCP----YGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSP-----PPKLKNSHKASPV 246
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  315 ICAFLSSREVR--LGRTGVDEIKCHPFF 340
Cdd:cd06659    247 LRDFLERMLVRdpQERATAQELLDHPFL 274
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
78-340 7.78e-29

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 116.72  E-value: 7.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKrSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14071      2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDE-ENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcdTA 236
Cdd:cd14071     81 ASNGEIFDyLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK--TW 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFpddiEMSKNAKDLIC 316
Cdd:cd14071    159 CGSPPYAAPEVFE---GKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPF----FMSTDCEHLIR 231
                          250       260
                   ....*....|....*....|....
gi 1207153289  317 AFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14071    232 RMLVLDPSK--RLTIEQIKKHKWM 253
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
77-340 8.41e-29

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 117.42  E-value: 8.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQV-YAMKQLSKFEMVKrsDSAFFWEERDIMAFSQSPWIVQLCcAFQD-EKYLYLV 154
Cdd:cd14202      3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAK--SQTLLGKEIKILKELKHENIVALY-DFQEiANSVYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG---------HLKLADFGTCMK 224
Cdd:cd14202     80 MEYCNGGDLADyLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  225 MDSTGMVRcdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSES---LVGTYGKimdhKNSLTF 301
Cdd:cd14202    160 LQNNMMAA--TLCGSPMYMAPEVIMSQ----HYDAKADLWSIGTIIYQCLTGKAPFQASSpqdLRLFYEK----NKSLSP 229
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207153289  302 PDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14202    230 NIPRETSSHLRQLLLGLLQRNQKD--RMDFDEFFHHPFL 266
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
84-280 8.80e-29

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 117.07  E-value: 8.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAF----FWEERDIMA-FSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd13993      8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFqklpQLREIDLHRrVSRHPNIITLHDVFETEVAIYIVLEYC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLVTL-TSN--YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN-GHLKLADFGTCMkmdsTGMVRCD 234
Cdd:cd13993     88 PNGDLFEAiTENriYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT----TEKISMD 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  235 TAVGTPDYISPEVLMSQG--GTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd13993    164 FGVGSEFYMAPECFDEVGrsLKGYPCAAGDIWSLGIILLNLTFGRNPW 211
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
84-339 1.17e-28

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 116.31  E-value: 1.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHK-VSQQVYAMKQLSKFEMVKRSDsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14120      1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQN--LLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG---------HLKLADFGTCMKMDSTGMVR 232
Cdd:cd14120     79 LADyLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFLQDGMMAA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 cdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSES---LVGTYgkimdHKNSLTFPD-DIEMS 308
Cdd:cd14120    159 --TLCGSPMYMAPEVIMSL----QYDAKADLWSIGTIVYQCLTGKAPFQAQTpqeLKAFY-----EKNANLRPNiPSGTS 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  309 KNAKDLICAFLsSREVRlGRTGVDEIKCHPF 339
Cdd:cd14120    228 PALKDLLLGLL-KRNPK-DRIDFEDFFSHPF 256
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
84-339 1.82e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 116.24  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSdsaffwEERDIMAFSQS---PWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14010      8 IGRGKHSVVYKGRRKGTIEFVAIKCVDK---SKRP------EVLNEVRLTHElkhPNVLKFYEWYETSNHLWLVVEYCTG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG---------------TCMK 224
Cdd:cd14010     79 GDLETlLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGlarregeilkelfgqFSDE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  225 MDSTGMVRCDTAVGTPDYISPEVLMSqggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHK-NSLTFPD 303
Cdd:cd14010    159 GNVNKVSKKQAKRGTPYYMAPELFQG----GVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDpPPPPPKV 234
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207153289  304 DIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14010    235 SSKPSPDFKSLLKGLLEKDPAK--RLSWDELVKHPF 268
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
84-315 3.18e-28

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 115.76  E-value: 3.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14169     11 LGEGAFSEVVLAQERGSQRLVALKCIPKKAL--RGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD---RNGHLKLADFGTCmKMDSTGMVrcDTAVGT 239
Cdd:cd14169     89 FDrIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLS-KIEAQGML--STACGT 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  240 PDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFP--DDIemSKNAKDLI 315
Cdd:cd14169    166 PGYVAPELLEQKP----YGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPywDDI--SESAKDFI 237
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
78-315 3.74e-28

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 115.32  E-value: 3.74e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14087      3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET----KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFG---TCMKMDST 228
Cdd:cd14087     79 ATGGELfdrIIAKGSFT--ERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGlasTRKKGPNC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMvrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMS 308
Cdd:cd14087    157 LM---KTTCGTPEYIAPEILLRKP----YTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVS 229

                   ....*..
gi 1207153289  309 KNAKDLI 315
Cdd:cd14087    230 NLAKDFI 236
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
78-284 4.30e-28

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 115.88  E-value: 4.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqlsKF------EMVKRSdsaffwEERDIMAFSQ--SPWIVQLCCAFQDEK 149
Cdd:cd07833      3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK---KFkeseddEDVKKT------ALREVKVLRQlrHENIVNLKEAFRRKG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTLTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDST 228
Cdd:cd07833     74 RLYLVFEYVERTLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTAR 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  229 GMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd07833    154 PASPLTDYVATRWYRAPELLV---GDTNYGKPVDVWAIGCIMAELLDGEPLFPGDS 206
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
77-285 7.99e-28

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 114.29  E-value: 7.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMV---KRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd08224      1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMdakARQDCL---KEIDLLQQLNHPNIIKYLASFIENNELNI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYD-----IPEE--WAQFYtaEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:cd08224     78 VLELADAGDLSRLIKHFKkqkrlIPERtiWKYFV--QLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFS 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  227 STGMVrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESL 285
Cdd:cd08224    156 SKTTA-AHSLVGTPYYMSPERIREQG----YDFKSDIWSLGCLLYEMAALQSPFYGEKM 209
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
77-338 8.68e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 114.06  E-value: 8.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd08220      1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAAL-NEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGG---DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHL-KLADFGTCMKMDSTGmvR 232
Cdd:cd08220     80 YAPGGtlfEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKS--K 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSltfPDDIEMSKNAK 312
Cdd:cd08220    158 AYTVVGTPCYISPELCEGKP----YNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFA---PISDRYSEELR 230
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  313 DLICAFLSSREVRlgRTGVDEIKCHP 338
Cdd:cd08220    231 HLILSMLHLDPNK--RPTLSEIMAQP 254
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
78-293 8.88e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 114.14  E-value: 8.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQ--LSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd08218      2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEinISKMSPKEREESR---KEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG-MV 231
Cdd:cd08218     79 DYCDGGDLykrINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVeLA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  232 RcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd08218    159 R--TCIGTPYYLSPEICENKP----YNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII 214
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
78-285 1.00e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 113.90  E-value: 1.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd08225      2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHL-KLADFGTCMKMDSTgMVRC 233
Cdd:cd08225     81 CDGGDLmkrINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDS-MELA 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  234 DTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESL 285
Cdd:cd08225    160 YTCVGTPYYLSPEICQNRP----YNNKTDIWSLGCVLYELCTLKHPFEGNNL 207
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
78-339 1.27e-27

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 113.54  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDImafsQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14665      2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSL----RHPNIVRFKEVILTPTHLAIVMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG--HLKLADFGtcMKMDSTGMVRCD 234
Cdd:cd14665     78 AAGGELFERICNAGrFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG--YSKSSVLHSQPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYS----ESLVGTYGKIMDHKNSLtfPDDIEMSKN 310
Cdd:cd14665    156 STVGTPAYIAPEVLLKK---EYDGKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSI--PDYVHISPE 230
                          250       260
                   ....*....|....*....|....*....
gi 1207153289  311 AKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14665    231 CRHLISRIFVADPAT--RITIPEIRNHEW 257
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
78-293 1.32e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 114.59  E-value: 1.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSD----SAFfwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd07841      2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDginfTAL--REIKLLQELKHPNIIGLLDVFGHKSNINL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGgDLVTLTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmV 231
Cdd:cd07841     80 VFEFMET-DLEKVIKDKSIVLTPADIksYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPN-R 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  232 RCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd07841    158 KMTHQVVTRWYRAPELLF---GARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIF 216
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
82-339 1.65e-27

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 113.63  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFWEERDIMAFSQS----------PWIVQLCCAFQDEKYL 151
Cdd:cd06629      7 ELIGKGTYGRVYLAMNATTGEMLAVKQV---ELPKTSSDRADSRQKTVVDALKSeidtlkdldhPNIVQYLGFEETEDYF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd06629     84 SIFLEYVPGGSIGSCLRKYgKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRCDTAV-GTPDYISPEVLMSQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSK 309
Cdd:cd06629    164 NNGATSMqGSVFWMAPEVIHSQGQG--YSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPEDVNLSP 241
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  310 NAKDLI--CAFLSSREvrlgRTGVDEIKCHPF 339
Cdd:cd06629    242 EALDFLnaCFAIDPRD----RPTAAELLSHPF 269
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
84-340 3.44e-27

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 112.29  E-value: 3.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAmkqlSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14107     10 IGRGTFGFVKRVTHKGNGECCA----AKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL--DRNGHLKLADFGTCMKMDSTGMVRcdTAVGTP 240
Cdd:cd14107     86 LDrLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQF--SKYGSP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLS 320
Cdd:cd14107    164 EFVAPEIVHQEPVS----AATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQ 239
                          250       260
                   ....*....|....*....|
gi 1207153289  321 SREVRlgRTGVDEIKCHPFF 340
Cdd:cd14107    240 PDPEK--RPSASECLSHEWF 257
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
84-315 5.99e-27

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 111.78  E-value: 5.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALL-KEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIPEEWA-QFYTA-EVVLALDAIHSL--GFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRCDTA-- 236
Cdd:cd13978     80 KSLLEREIQDVPWSlRFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGlSKLGMKSISANRRRGTen 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 -VGTPDYISPEVLmsqgGTGYY--GRECDWWSVGVFIYELLVGDTPF--YSESLVGTYGKIMDHK---NSLTFPDDIEMS 308
Cdd:cd13978    160 lGGTPIYMAPEAF----DDFNKkpTSKSDVYSFAIVIWAVLTRKEPFenAINPLLIMQIVSKGDRpslDDIGRLKQIENV 235

                   ....*..
gi 1207153289  309 KNAKDLI 315
Cdd:cd13978    236 QELISLM 242
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
84-319 6.74e-27

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 112.43  E-value: 6.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSDSaffwEERDIM-AFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14175      9 IGVGSYSVCKRCVHKATNMEYAVKVIDK---SKRDPS----EEIEILlRYGQHPNIITLKDVYDDGKHVYLVTELMRGGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LV--TLTSNYdIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH---LKLADFGTCMKMDSTG---MVRC 233
Cdd:cd14175     82 LLdkILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENgllMTPC 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAvgtpDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFY---SESLVGTYGKIMDHKNSLTFPDDIEMSKN 310
Cdd:cd14175    161 YTA----NFVAPEVLKRQG----YDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWNTVSDA 232

                   ....*....
gi 1207153289  311 AKDLICAFL 319
Cdd:cd14175    233 AKDLVSKML 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
429-1138 7.64e-27

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 119.39  E-value: 7.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKA 508
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 GLETDRKRLLENEVSSLKEQLAELKkknqishlsaEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSL 588
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLE----------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  589 RELQERLAQLENSRLVLEQDKLSLQTslELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTL 668
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 EKEKNKqeidLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN-------QSIEAKSETLKDMEhKLLEERsakqqLENR 741
Cdd:TIGR02168  481 ERELAQ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIE-AALGGR-----LQAV 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  742 LMqlEKENSVLDCDYKQAKHELQ-----------------ELRSLKENLTEQVEVLNVRVQQET---------------- 788
Cdd:TIGR02168  551 VV--ENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPklrkalsyllggvlvv 628
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  789 --------QRK---------TLcQGDL----KVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQL 847
Cdd:TIGR02168  629 ddldnaleLAKklrpgyrivTL-DGDLvrpgGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  848 KEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDL 927
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  928 EKEkimkeleikdmIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKL----KHIQQKLEKIKEEEKQMKS 1003
Cdd:TIGR02168  788 EAQ-----------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQIEELSEDIES 856
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1004 LTVSYEKQiQVEKTLKIQAINKLAEVMKKTDGRPHQIN------NTDIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQR-- 1075
Cdd:TIGR02168  857 LAAEIEEL-EELIEELESELEALLNERASLEEALALLRseleelSEELRELESKRSELRRELEELREKLAQLELRLEGle 935
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1076 -EINDMQAMIAEESQVRLEMQMSLDSK-DSDIERLRSQLTSLsihsldTTSISSIGN-DLDSDEAY 1138
Cdd:TIGR02168  936 vRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRL------ENKIKELGPvNLAAIEEY 995
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
82-339 8.65e-27

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 111.28  E-value: 8.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14184      7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKC--CGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL----DRNGHLKLADFGTCMKMDSTGMVRCdta 236
Cdd:cd14184     85 DLFdAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGPLYTVC--- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 vGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLV--GTYGKIMDHKnsLTFP----DDIemSKN 310
Cdd:cd14184    162 -GTPTYVAPEIIAETG----YGLKVDIWAAGVITYILLCGFPPFRSENNLqeDLFDQILLGK--LEFPspywDNI--TDS 232
                          250       260       270
                   ....*....|....*....|....*....|
gi 1207153289  311 AKDLICAFLssrEVRL-GRTGVDEIKCHPF 339
Cdd:cd14184    233 AKELISHML---QVNVeARYTAEQILSHPW 259
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
84-279 1.19e-26

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 110.88  E-value: 1.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDsafFWEERDI-MAFSQSPWIVQ-LCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd13987      1 LGEGTYGKVLLAVHKGSGTKMALKFVPK-PSTKLKD---FLREYNIsLELSVHPHIIKtYDVAFETEDYYVFAQEYAPYG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRN-GHLKLADFGTCMKMDSTgmVRcdTAVG 238
Cdd:cd13987     77 DLFSiIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRRVGST--VK--RVSG 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  239 TPDYISPEVLMSQGGTGYYGREC-DWWSVGVFIYELLVGDTP 279
Cdd:cd13987    153 TIPYTAPEVCEAKKNEGFVVDPSiDVWAFGVLLFCCLTGNFP 194
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
84-319 1.20e-26

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 111.64  E-value: 1.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSDSaffwEERDIM-AFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14178     11 IGIGSYSVCKRCVHKATSTEYAVKIIDK---SKRDPS----EEIEILlRYGQHPNIITLKDVYDDGKFVYLVMELMRGGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LV--TLTSNYdIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH---LKLADFGTCMKMDSTG---MVRC 233
Cdd:cd14178     84 LLdrILRQKC-FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENgllMTPC 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAvgtpDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS---ESLVGTYGKIMDHKNSLTFPDDIEMSKN 310
Cdd:cd14178    163 YTA----NFVAPEVLKRQG----YDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSGGNWDSISDA 234

                   ....*....
gi 1207153289  311 AKDLICAFL 319
Cdd:cd14178    235 AKDIVSKML 243
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
78-273 1.61e-26

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 110.09  E-value: 1.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQlSKFEMVKRSDSAFFWEE-RDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd14050      3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-SRSRFRGEKDRKRKLEEvERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGmvRCDTA 236
Cdd:cd14050     82 LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKED--IHDAQ 159
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1207153289  237 VGTPDYISPEVLmsqggTGYYGRECDWWSVGVFIYEL 273
Cdd:cd14050    160 EGDPRYMAPELL-----QGSFTKAADIFSLGITILEL 191
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
82-341 2.09e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 110.21  E-value: 2.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSkFEMVKRSDSAF----FWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06630      6 PLLGTGAFSSCYQARDVKTGTLMAVKQVS-FCRNSSSEQEEvveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG-HLKLADFGTCMKMDS----TGMV 231
Cdd:cd06630     85 MAGGSVASLLSKYGaFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASkgtgAGEF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEM-SKN 310
Cdd:cd06630    165 Q-GQLLGTIAFMAPEVLRGEQ----YGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPEHlSPG 239
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  311 AKDLICAFLSSRevRLGRTGVDEIKCHPFFK 341
Cdd:cd06630    240 LRDVTLRCLELQ--PEDRPPARELLKHPVFT 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
76-344 2.60e-26

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 110.71  E-value: 2.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMvkrSDSAF--FWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd06622      1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEI-RLEL---DESKFnqIIMELDILHKAVSPYIVDFYGAFFIEGAVYM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYD----IPEEWAQFYTAEVVLALDAI-HSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDST 228
Cdd:cd06622     77 CMEYMDAGSLDKLYAGGVategIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVAS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 gmvRCDTAVGTPDYISPEVLMSQG--GTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKI--MDHKNSLTFPDD 304
Cdd:cd06622    157 ---LAKTNIGCQSYMAPERIKSGGpnQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLsaIVDGDPPTLPSG 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1207153289  305 ieMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFKNDQ 344
Cdd:cd06622    234 --YSDDAQDFVAKCLNKIPNR--RPTYAQLLEHPWLVKYK 269
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
82-339 2.93e-26

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 109.81  E-value: 2.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14082      9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQL-RNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTS--NYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG---HLKLADFGTCMKMDSTGMVRcdTA 236
Cdd:cd14082     88 MLEMILSseKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRR--SV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESlvgtygKIMD--HKNSLTFPDD--IEMSKNAK 312
Cdd:cd14082    166 VGTPAYLAPEVLRNKG----YNRSLDMWSVGVIIYVSLSGTFPFNEDE------DINDqiQNAAFMYPPNpwKEISPDAI 235
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  313 DLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14082    236 DLINNLLQVKMRK--RYSVDKSLSHPW 260
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
78-315 3.12e-26

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 109.63  E-value: 3.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06647      9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06647     86 LAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-STMV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES------LVGTYGKI-MDHKNSLT--FPD----- 303
Cdd:cd06647    165 GTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENplralyLIATNGTPeLQNPEKLSaiFRDflnrc 240
                          250
                   ....*....|....*
gi 1207153289  304 ---DIEMSKNAKDLI 315
Cdd:cd06647    241 lemDVEKRGSAKELL 255
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-319 3.38e-26

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 109.68  E-value: 3.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFD----RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd14113      3 DNFDsfysEVAELGRGRFSVVKKCDQRGTKRAVATKFVNK-KLMKRDQVT---HELGVLQSLQHPQLVGLLDTFETPTSY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMDS 227
Cdd:cd14113     79 ILVLEMADQGRLLDYVVRWgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDI-- 305
Cdd:cd14113    159 TYYIH--QLLGSPEFAAPEIILGNP----VSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNIC--RLDFSFPDDYfk 230
                          250
                   ....*....|....
gi 1207153289  306 EMSKNAKDLICAFL 319
Cdd:cd14113    231 GVSQKAKDFVCFLL 244
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
76-341 4.00e-26

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 110.15  E-value: 4.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd06616      6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRS-TVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMpggD--------LVTLTSNYDIPEEWAQFYTAEVVLALDAI-HSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM- 225
Cdd:cd06616     85 ELM---DisldkfykYVYEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQLv 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRcdtAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVG-------DTPFYSESLVgTYGK--IMDHK 296
Cdd:cd06616    162 DSIAKTR---DAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGkfpypkwNSVFDQLTQV-VKGDppILSNS 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  297 nsltfpDDIEMSKNAKDLICAFLsSREVRLgRTGVDEIKCHPFFK 341
Cdd:cd06616    238 ------EEREFSPSFVNFVNLCL-IKDESK-RPKYKELLKHPFIK 274
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
77-276 5.58e-26

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 108.62  E-value: 5.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQlSKFEMVKRSDSAFFWEERDI-MAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd13997      1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKK-SKKPFRGPKERARALREVEAhAALGQHPNIVRYYSSWEEGGHLYIQM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVtltsnyDIPEEWAQF----------YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd13997     80 ELCENGSLQ------DALEELSPIsklseaevwdLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  226 DSTGMVRcdtaVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd13997    154 ETSGDVE----EGDSRYLAPELLN---ENYTHLPKADIFSLGVTVYEAATG 197
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
78-339 5.72e-26

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 108.70  E-value: 5.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFweeRDIMAFS--QSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14662      2 YELVKDIGSGNFGVARLMRNKETKELVAVKYI---ERGLKIDENVQ---REIINHRslRHPNIIRFKEVVLTPTHLAIVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN--GHLKLADFGtcMKMDSTGMVR 232
Cdd:cd14662     76 EYAAGGELFERICNAGrFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFG--YSKSSVLHSQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYS----ESLVGTYGKIMDHKNSLtfPDDIEMS 308
Cdd:cd14662    154 PKSTVGTPAYIAPEVLSRK---EYDGKVADVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQYKI--PDYVRVS 228
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  309 KNAKDLI-CAFLSSREVRLgrtGVDEIKCHPF 339
Cdd:cd14662    229 QDCRHLLsRIFVANPAKRI---TIPEIKNHPW 257
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
75-275 1.22e-25

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 108.15  E-value: 1.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQL-SKFEMVKRSDsaffwEERDIMAFS--QSPWIVQLCCAFQDEKYL 151
Cdd:cd13996      5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIrLTEKSSASEK-----VLREVKALAklNHPNIVRYYTAWVEEPPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDL------VTLTSNYDIPEEWAQFYtaEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFG--TC 222
Cdd:cd13996     80 YIQMELCEGGTLrdwidrRNSSSKNDRKLALELFK--QILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGlaTS 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  223 MK--------MDSTGMVRCD---TAVGTPDYISPEvlmsQGGTGYYGRECDWWSVGVFIYELLV 275
Cdd:cd13996    158 IGnqkrelnnLNNNNNGNTSnnsVGIGTPLYASPE----QLDGENYNEKADIYSLGIILFEMLH 217
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
80-339 1.94e-25

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 107.62  E-value: 1.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQL------SKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd06628      4 KGALIGSGSFGSVYLGMNASSGELMAVKQVelpsvsAENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd06628     84 FLEYVPGGSVATLLNNYgAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLST 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAV-----GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImDHKNSLTFPDDIem 307
Cdd:cd06628    164 KNNGArpslqGSVFWMAPEVVKQTS----YTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKI-GENASPTIPSNI-- 236
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  308 SKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd06628    237 SSEARDFLEKTFEIDHNK--RPTADELLKHPF 266
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
78-280 2.43e-25

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 106.96  E-value: 2.43e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14161      5 YEFLETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcdTA 236
Cdd:cd14161     84 ASRGDLYDYISERQrLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQ--TY 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  237 VGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14161    162 CGSPLYASPEIV---NGRPYIGPEVDSWSLGVLLYILVHGTMPF 202
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
82-340 2.48e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 106.94  E-value: 2.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14189      7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTL-TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMvRCDTAVGTP 240
Cdd:cd14189     87 SLAHIwKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQ-RKKTICGTP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  241 DYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTfpddIEMSKNAKDLICAFLs 320
Cdd:cd14189    166 NYLAPEVLLRQG----HGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAGIL- 236
                          250       260
                   ....*....|....*....|
gi 1207153289  321 sREVRLGRTGVDEIKCHPFF 340
Cdd:cd14189    237 -KRNPGDRLTLDQILEHEFF 255
HR1_ROCK2 cd11638
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
494-560 2.65e-25

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2; ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212028 [Multi-domain]  Cd Length: 67  Bit Score: 100.39  E-value: 2.65e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  494 KVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKL 560
Cdd:cd11638      1 KALLQHKNTEYQRKAEHEADRKRNLENEVNSLKDQLEDLKKKNQNSQISNEKNIQLQRQLDEANALL 67
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
73-315 2.77e-25

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 107.53  E-value: 2.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   73 VKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQL---SKFEMVKRsdsafFWEERDIMAFSQSPWIVQLCCAFQDEK 149
Cdd:cd06620      2 LKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSVRKQ-----ILRELQILHECHSPYIVSFYGAFLNEN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 -YLYLVMEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM- 225
Cdd:cd06620     77 nNIIICMEYMDCGSLDKILKKKGpFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELi 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGmvrcDTAVGTPDYISPEVLmsQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSE-----SLVGTYGkIMD------ 294
Cdd:cd06620    157 NSIA----DTFVGTSTYMSPERI--QGGK--YSVKSDVWSLGLSIIELALGEFPFAGSnddddGYNGPMG-ILDllqriv 227
                          250       260
                   ....*....|....*....|.
gi 1207153289  295 HKNSLTFPDDIEMSKNAKDLI 315
Cdd:cd06620    228 NEPPPRLPKDRIFPKDLRDFV 248
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
53-342 2.94e-25

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 106.86  E-value: 2.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   53 NIDAFLSRyekaVCN-LKELQV----KLDDfdrvkligrGAFGAVQLVRHKVSQQVYAMKQLSK--FE----MVkrsdsa 121
Cdd:PHA03390     1 NMDKSLSE----LVQfLKNCEIvkklKLID---------GKFGKVSVLKHKPTQKLFVQKIIKAknFNaiepMV------ 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  122 ffweeRDIMAFSqsPWIVQLCCAFQDEKYLYLVMEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRD 200
Cdd:PHA03390    62 -----HQLMKDN--PNFIKLYYSVTTLKGHVLIMDYIKDGDLFdLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHND 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  201 IKPDNMLLDRN-GHLKLADFGTCMKMDSTGMVRcdtavGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:PHA03390   135 IKLENVLYDRAkDRIYLCDYGLCKIIGTPSCYD-----GTLDYFSPEKIKGH----NYDVSFDWWAVGVLTYELLTGKHP 205
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  280 FyseslVGTYGKIMD-------HKNSLTFPDDieMSKNAKDLICAFLS-SREVRLgrTGVDEIKCHPFFKN 342
Cdd:PHA03390   206 F-----KEDEDEELDlesllkrQQKKLPFIKN--VSKNANDFVQSMLKyNINYRL--TNYNEIIKHPFLKI 267
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
75-340 3.03e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 107.80  E-value: 3.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRvklIGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd06657     22 LDNFIK---IGEGSTGIVCIATVKSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGMVRCD 234
Cdd:cd06657     96 MEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKEVPRRK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknsltFPDDIEMSKNAKDL 314
Cdd:cd06657    175 SLVGTPYWMAPELISRLP----YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDN-----LPPKLKNLHKVSPS 245
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  315 ICAFLSSREVR--LGRTGVDEIKCHPFF 340
Cdd:cd06657    246 LKGFLDRLLVRdpAQRATAAELLKHPFL 273
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
84-341 3.32e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 107.43  E-value: 3.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd06658     30 IGEGSTGIVCIATEKHTGKQVAVK---KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdSTGMVRCDTAVGTPDYI 243
Cdd:cd06658    107 TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV-SKEVPKRKSLVGTPYWM 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  244 SPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDhknslTFPDDIEMSKNAKDLICAFLSSRE 323
Cdd:cd06658    186 APEVISRLP----YGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD-----NLPPRVKDSHKVSSVLRGFLDLML 256
                          250       260
                   ....*....|....*....|
gi 1207153289  324 VR--LGRTGVDEIKCHPFFK 341
Cdd:cd06658    257 VRepSQRATAQELLQHPFLK 276
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
75-339 3.52e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 107.16  E-value: 3.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFD---RVKLiGRGAFGAVQLVRHKVSQQVYAMKQLskfemVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDE--- 148
Cdd:cd14171      3 LEEYEvnwTQKL-GTGISGPVRVCVKKSTGERFALKIL-----LDRPKART--EVRLHMMCSGHPNIVQIYDVYANSvqf 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 -------KYLYLVMEFMPGGDLVTLTS-NYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLA 217
Cdd:cd14171     75 pgessprARLLIVMELMEGGELFDRISqHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLC 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  218 DFGTCmKMDSTGMVrcdTAVGTPDYISPEVLMSQ------------GGTGY-YGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14171    155 DFGFA-KVDQGDLM---TPQFTPYYVAPQVLEAQrrhrkersgiptSPTPYtYDKSCDMWSLGVIIYIMLCGYPPFYSEH 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  285 LVGTYGKIMDHK---NSLTFPDD--IEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14171    231 PSRTITKDMKRKimtGSYEFPEEewSQISEMAKDIVRKLLCVDPEE--RMTIEEVLHHPW 288
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
81-341 3.56e-25

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 107.20  E-value: 3.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSDSaffwEERDIMAFSQSPWIVQLCCAF------QDEKYLYLV 154
Cdd:cd14137      9 EKVIGSGSFGVVYQAKLLETGEVVAIK---KVLQDKRYKN----RELQIMRRLKHPNIVKLKYFFyssgekKDEVYLNLV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGgDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFGTCMKMDSt 228
Cdd:cd14137     82 MEYMPE-TLYRVIRHYSknkqtIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSAKRLVP- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 gmvrcdtavGTPD--YIS------PEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD------ 294
Cdd:cd14137    160 ---------GEPNvsYICsryyraPELIF---GATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKvlgtpt 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  295 ---------HKNSLTFPD------DIEMSKNAKDLICAFLSSREV-----RLgrTGVdEIKCHPFFK 341
Cdd:cd14137    228 reqikamnpNYTEFKFPQikphpwEKVFPKRTPPDAIDLLSKILVynpskRL--TAL-EALAHPFFD 291
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
77-341 4.15e-25

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 106.63  E-value: 4.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRH-KVSQQVYAMKQLSKFEMVKrsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14201      7 EYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSK--SQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG---------HLKLADFGTCMKM 225
Cdd:cd14201     85 EYCNGGDLADyLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRcdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTygKIMDHKNSLTFPD-D 304
Cdd:cd14201    165 QSNMMAA--TLCGSPMYMAPEVIMSQ----HYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL--RMFYEKNKNLQPSiP 236
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207153289  305 IEMSKNAKDLICAFLSSREVrlGRTGVDEIKCHPFFK 341
Cdd:cd14201    237 RETSPYLADLLLGLLQRNQK--DRMDFEAFFSHPFLE 271
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
83-283 5.16e-25

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 106.73  E-value: 5.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdSAFfweeRDIMAFSQ---SPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd14090      9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRS-RVF----REVETLHQcqgHPNILQLIEYFEDDERFYLVFEKMR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMDSTGMvRCD- 234
Cdd:cd14090     84 GGPLLShIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSST-SMTp 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  235 -------TAVGTPDYISPEVLMS-QGGTGYYGRECDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd14090    163 vttpellTPVGSAEYMAPEVVDAfVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGR 219
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
82-294 6.73e-25

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 105.67  E-value: 6.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSD-SAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14070      8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR-CDTAVG 238
Cdd:cd14070     88 GNLMHrIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDpFSTQCG 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  239 TPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSE--SLVGTYGKIMD 294
Cdd:cd14070    168 SPAYAAPELL----ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVD 221
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
80-340 6.84e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 105.79  E-value: 6.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd14187     11 RGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMvRCDTAVG 238
Cdd:cd14187     91 RRSLLELHKRRKaLTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGE-RKKTLCG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  239 TPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemSKNAKDLICAF 318
Cdd:cd14187    170 TPNYIAPEVLSKKG----HSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPKHI--NPVAASLIQKM 241
                          250       260
                   ....*....|....*....|..
gi 1207153289  319 LSSREVrlGRTGVDEIKCHPFF 340
Cdd:cd14187    242 LQTDPT--ARPTINELLNDEFF 261
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
80-340 7.20e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 105.48  E-value: 7.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd14188      5 RGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAVG 238
Cdd:cd14188     85 RRSMAhILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRR-RTICG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  239 TPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLtfPDdiEMSKNAKDLICAF 318
Cdd:cd14188    164 TPNYLSPEVLNKQG----HGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSL--PS--SLLAPAKHLIASM 235
                          250       260
                   ....*....|....*....|..
gi 1207153289  319 LSSREVrlGRTGVDEIKCHPFF 340
Cdd:cd14188    236 LSKNPE--DRPSLDEIIRHDFF 255
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
78-294 7.44e-25

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 106.03  E-value: 7.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSD----SAFfweeRDIMAFS--QSPWIVQLCCAFQDEKYL 151
Cdd:cd07829      1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK---KIRLDNEEEgipsTAL----REISLLKelKHPNIVKLLDVIHTENKL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGgDLVTLTSNY--DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFgtcmkmdstG 229
Cdd:cd07829     74 YLVFEYCDQ-DLKKYLDKRpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADF---------G 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  230 MVRcdtAVGTPD-----------YISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07829    144 LAR---AFGIPLrtythevvtlwYRAPEILL---GSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQ 213
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
75-273 7.58e-25

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 105.91  E-value: 7.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDSAFFWEERDIMAFS--QSPWIVQLCCAFQDEKYLY 152
Cdd:cd14046      5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK----LRSESKNNSRILREVMLLSrlNHQHVVRYYQAWIERANLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLTSNY---DIPEEWAQFytAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--------- 220
Cdd:cd14046     81 IQMEYCEKSTLRDLIDSGlfqDTDRLWRLF--RQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnklnv 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  221 --------------TCMKMDSTGMvrcdtaVGTPDYISPEVLmsQGGTGYYGRECDWWSVGVFIYEL 273
Cdd:cd14046    159 elatqdinkstsaaLGSSGDLTGN------VGTALYVAPEVQ--SGTKSTYNEKVDMYSLGIIFFEM 217
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
84-340 9.21e-25

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 105.25  E-value: 9.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLV-RHKVSQQVyAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ-DEKYLYLVMEFMPGG 161
Cdd:cd14165      9 LGEGSYAKVKSAySERLKCNV-AIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFEtSDGKVYIVMELGVQG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM--DSTG-MVRCDTAV 237
Cdd:cd14165     88 DLLEfIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRClrDENGrIVLSKTFC 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPfYSESLVGTYGKImDHKNSLTFPDDIEMSKNAKDLICA 317
Cdd:cd14165    168 GSAAYAAPEVLQ---GIPYDPRIYDIWSLGVILYIMVCGSMP-YDDSNVKKMLKI-QKEHRVRFPRSKNLTSECKDLIYR 242
                          250       260
                   ....*....|....*....|...
gi 1207153289  318 FLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14165    243 LLQPDVSQ--RLCIDEVLSHPWL 263
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
81-273 1.29e-24

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 105.31  E-value: 1.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQlskfeMVKRSDSaffWEE-------RDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd07830      4 IKQLGDGTFGSVYLARNKETGELVAIKK-----MKKKFYS---WEEcmnlrevKSLRKLNEHPNIVKLKEVFRENDELYF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGgDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS--- 227
Cdd:cd07830     76 VFEYMEG-NLYQLMKDRKgkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSrpp 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  228 -TgmvrcdTAVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYEL 273
Cdd:cd07830    155 yT------DYVSTRWYRAPEILLRS---TSYSSPVDIWALGCIMAEL 192
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
70-339 1.33e-24

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 105.18  E-value: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   70 ELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqlskfEMVKRSDSAF--FWEERDIMAFSQSPWIVQLCCAFQD 147
Cdd:cd06624      2 EYEYEYDESGERVVLGKGTFGVVYAARDLSTQVRIAIK-----EIPERDSREVqpLHEEIALHSRLSHKNIVQYLGSVSE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKYLYLVMEFMPGGDLVTLTSNYDIP----EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR-NGHLKLADFGTC 222
Cdd:cd06624     77 DGFFKIFMEQVPGGSLSALLRSKWGPlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 MKMDSTGMVrCDTAVGTPDYISPEVLmSQGGTGyYGRECDWWSVGVFIYELLVGDTPFYSES-------LVGTYgKImdH 295
Cdd:cd06624    157 KRLAGINPC-TETFTGTLQYMAPEVI-DKGQRG-YGPPADIWSLGCTIIEMATGKPPFIELGepqaamfKVGMF-KI--H 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  296 KNsltFPDdiEMSKNAKDLI-CAFLSSREvrlGRTGVDEIKCHPF 339
Cdd:cd06624    231 PE---IPE--SLSEEAKSFIlRCFEPDPD---KRATASDLLQDPF 267
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-315 1.66e-24

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 105.68  E-value: 1.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14085      3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKK-----TVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDL---VTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMDSTG 229
Cdd:cd14085     78 ELVTGGELfdrIVEKGYYS--ERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MVRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVG-TYGKIMDHKNSLTFP--DDIe 306
Cdd:cd14085    156 TMK--TVCGTPGYCAPEILRGCA----YGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFVSPwwDDV- 228

                   ....*....
gi 1207153289  307 mSKNAKDLI 315
Cdd:cd14085    229 -SLNAKDLV 236
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
427-988 1.69e-24

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 111.27  E-value: 1.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  427 NHTESNDLEKRLKKLEE---KFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNarqEAEDNLRSLEKEKVLLKHQRTQ 503
Cdd:TIGR04523  122 LEVELNKLEKQKKENKKnidKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN---LLEKEKLNIQKNIDKIKNKLLK 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  504 -----SVRKAGLEtdRKRLLENEVSSLKEQLAELKkkNQISHLSAEKNiHLERQLEEVSAKLQAELEESERLKKAQIEAF 578
Cdd:TIGR04523  199 lelllSNLKKKIQ--KNKSLESQISELKKQNNQLK--DNIEKKQQEIN-EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  579 RQSQQLELSLRELQERLAQLENSRLVLEQDKlslqtslelekrernaGSETITDLQGRIYGLEGELKHIKSSLSKAEVEK 658
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNQLKSEISDLNNQK----------------EQDWNKELKSELKNQEKKLEEIQNQISQNNKII 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  659 RQLQEDLTTLEKEKNKQEIDLSFKlkavQQSLEQEEAEHKTTKArlaDNNKINQSIEAKSETLKDMEHKLLEERSAKQQL 738
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEK----QRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  739 ENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQE 818
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  819 LNHLLELKLTLEKQNQELSKEREESEKQLKEMK---DQLEAEQyftKLYKTQIRELKEESD-----------EKVKLYKd 884
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEKLESEK---KEKESKISDLEDELNkddfelkkenlEKEIDEK- 566
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  885 aQQRIEDLQEERDSLASQLEVSLTKADseqlaritveeQYSDlEKEKIMKELEIKDMIarhrqdLAEKDGTINSLEESNR 964
Cdd:TIGR04523  567 -NKEIEELKQTQKSLKKKQEEKQELID-----------QKEK-EKKDLIKEIEEKEKK------ISSLEKELEKAKKENE 627
                          570       580
                   ....*....|....*....|....
gi 1207153289  965 TLTVDVANLASEKEELNNKLKHIQ 988
Cdd:TIGR04523  628 KLSSIIKNIKSKKNKLKQEVKQIK 651
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
82-315 1.84e-24

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 104.74  E-value: 1.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14106     14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAGG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCMKMDSTGMVRcdTAV 237
Cdd:cd14106     94 ELQTLLDEEEcLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGEGEEIR--EIL 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGGTGYygreCDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDI--EMSKNAKDLI 315
Cdd:cd14106    172 GTPDYVAPEILSYEPISLA----TDMWSIGVLTYVLLTGHSPFGGDDKQETFLNI--SQCNLDFPEELfkDVSPLAIDFI 245
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
76-319 1.95e-24

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 105.48  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemVKRSDSaffwEERDI-MAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd14177      4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDK---SKRDPS----EEIEIlMRYGQHPNIITLKDVYDDGRYVYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDL---VTLTSNYDIPEEWAQFYTaeVVLALDAIHSLGFIHRDIKPDNML-LDRNGH---LKLADFGTCMKM-D 226
Cdd:cd14177     77 TELMKGGELldrILRQKFFSEREASAVLYT--ITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLrG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 STGMVRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS-------ESLVgtygKIMDHKNSL 299
Cdd:cd14177    155 ENGLLL--TPCYTANFVAPEVLMRQG----YDAACDIWSLGVLLYTMLAGYTPFANgpndtpeEILL----RIGSGKFSL 224
                          250       260
                   ....*....|....*....|
gi 1207153289  300 TFPDDIEMSKNAKDLICAFL 319
Cdd:cd14177    225 SGGNWDTVSDAAKDLLSHML 244
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
82-343 2.07e-24

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 104.69  E-value: 2.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14183     12 RTIGDGNFAVVKECVERSTGREYALKIINKSKC--RGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL----DRNGHLKLADFGTCMKMDSTGMVRCdta 236
Cdd:cd14183     90 DLFdAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDGPLYTVC--- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 vGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF--YSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDL 314
Cdd:cd14183    167 -GTPTYVAPEIIAETG----YGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKEL 241
                          250       260
                   ....*....|....*....|....*....
gi 1207153289  315 ICAFLSSrEVRLGRTGVDEIKcHPFFKND 343
Cdd:cd14183    242 ITMMLQV-DVDQRYSALQVLE-HPWVNDD 268
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
77-339 2.20e-24

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 104.45  E-value: 2.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK----FEMVKRSDSAFFWEERDIMAFSQS--------PWIVQLCCA 144
Cdd:cd14077      2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRasnaGLKKEREKRLEKEISRDIRTIREAalssllnhPHICRLRDF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  145 FQDEKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM 223
Cdd:cd14077     82 LRTPNHYYMLFEYVDGGQLLDyIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  224 KMDSTGMVRcdTAVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKnsLTFPD 303
Cdd:cd14077    162 LYDPRRLLR--TFCGSLYFAAPELLQAQ---PYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGK--VEYPS 234
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207153289  304 DIemSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14077    235 YL--SSECKSLISRMLVVDPKK--RATLEQVLNHPW 266
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
80-320 2.45e-24

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 105.51  E-value: 2.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvkRSDSAffwEERDIMAF---SQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd14179     11 KDKPLGEGSFSICRKCLHKKTNQEYAVKIVSK-----RMEAN---TQREIAALklcEGHPNIVKLHEVYHDQLHTFLVME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTC-MKMDSTGMV 231
Cdd:cd14179     83 LLKGGELLErIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFArLKPPDNQPL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS--ESLVGTYG-KIMD--HKNSLTFPDDI- 305
Cdd:cd14179    163 K--TPCFTLHYAAPELLNYNG----YDESCDLWSLGVILYTMLSGQVPFQChdKSLTCTSAeEIMKkiKQGDFSFEGEAw 236
                          250
                   ....*....|....*.
gi 1207153289  306 -EMSKNAKDLICAFLS 320
Cdd:cd14179    237 kNVSQEAKDLIQGLLT 252
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
84-339 3.13e-24

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 104.10  E-value: 3.13e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQL------VRHKVSQQVyAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14076      9 LGEGEFGKVKLgwplpkANHRSGVQV-AIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTA 236
Cdd:cd14076     88 VSGGELFDyILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDLMSTS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQggTGYYGRECDWWSVGVFIYELLVGDTPF-------YSESLVGTYGKIMDhkNSLTFPDDIemSK 309
Cdd:cd14076    168 CGSPCYAAPELVVSD--SMYAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICN--TPLIFPEYV--TP 241
                          250       260       270
                   ....*....|....*....|....*....|
gi 1207153289  310 NAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14076    242 KARDLLRRILVPNPRK--RIRLSAIMRHAW 269
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
84-274 3.40e-24

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 104.28  E-value: 3.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQlskfeMVKRSDSAffwEE----RDIMA---FSQSPWIVQLCCAFQDEKY--LYLV 154
Cdd:cd07831      7 IGEGTFSEVLKAQSRKTGKYYAIKC-----MKKHFKSL---EQvnnlREIQAlrrLSPHPNILRLIEVLFDRKTgrLALV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGgDLVTLTSN--YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNgHLKLADFGTCMKMDSTGmvr 232
Cdd:cd07831     79 FELMDM-NLYELIKGrkRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCRGIYSKP--- 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 cdtavgtP--DYIS------PEVLMSqggTGYYGRECDWWSVGVFIYELL 274
Cdd:cd07831    154 -------PytEYIStrwyraPECLLT---DGYYGPKMDIWAVGCVFFEIL 193
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
61-355 4.67e-24

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 104.36  E-value: 4.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   61 YEKAVCNLKELqvklddFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQ 140
Cdd:cd14168      1 WKKQVEDIKKI------FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHENIVA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  141 LCCAFQDEKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKL 216
Cdd:cd14168     73 LEDIYESPNHLYLVMQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  217 ADFGTCmKMDSTGMVRcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHK 296
Cdd:cd14168    153 SDFGLS-KMEGKGDVM-STACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAD 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  297 NSLTFPDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFFKNDQWTFDTIRDTMA 355
Cdd:cd14168    227 YEFDSPYWDDISDSAKDFIRNLMEKDPNK--RYTCEQALRHPWIAGDTALCKNIHESVS 283
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
84-273 5.76e-24

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 103.96  E-value: 5.76e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG-- 161
Cdd:cd06644     20 LGDGAFGKVYKAKNKETGALAAAKVI---ETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGav 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVRCDTAVGTPD 241
Cdd:cd06644     97 DAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKT-LQRRDSFIGTPY 175
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207153289  242 YISPEVLMSQG-GTGYYGRECDWWSVGVFIYEL 273
Cdd:cd06644    176 WMAPEVVMCETmKDTPYDYKADIWSLGITLIEM 208
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
78-280 6.14e-24

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 103.80  E-value: 6.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemvkrsdsafFWEERD-----------IMAFSQSPWIVQL---CC 143
Cdd:cd07840      1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIR------------MENEKEgfpitaireikLLQKLDHPNVVRLkeiVT 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  144 AFQDEKY---LYLVMEFMPGgDLVTLTSNYDIPEEWAQ--FYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLAD 218
Cdd:cd07840     69 SKGSAKYkgsIYMVFEYMDH-DLTGLLDNPEVKFTESQikCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAD 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  219 FGTCMKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07840    148 FGLARPYTKENNADYTNRVITLWYRPPELLL---GATRYGPEVDMWSVGCILAELFTGKPIF 206
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
82-315 8.02e-24

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 102.80  E-value: 8.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLS---KFEMVKRSDSAFFWEERDIMAFSQSPwIVQL--CCAFQDEKYLYLVME 156
Cdd:cd06653      8 KLLGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDR-IVQYygCLRDPEEKKLSIFVE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK-----MDSTGM 230
Cdd:cd06653     87 YMPGGSVKDQLKAYGaLTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRiqticMSGTGI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 vrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIemSKN 310
Cdd:cd06653    167 ---KSVTGTPYWMSPEVISGEG----YGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPDGV--SDA 237

                   ....*
gi 1207153289  311 AKDLI 315
Cdd:cd06653    238 CRDFL 242
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
84-340 8.18e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 103.18  E-value: 8.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSkfeMVKRSD---SAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd07832      8 IGEGAHGIVFKAKDRETGETVALKKVA---LRKLEGgipNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 gDLVTLTSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVG 238
Cdd:cd07832     85 -SLSEVLRDEErpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHQVA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  239 TPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSES----------LVGT--------------YGKIM- 293
Cdd:cd07832    164 TRWYRAPELLY---GSRKYDEGVDLWAVGCIFAELLNGSPLFPGENdieqlaivlrTLGTpnektwpeltslpdYNKITf 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  294 -DHKNSL---TFPDdieMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd07832    241 pESKGIRleeIFPD---CSPEAIDLLKGLLVYNPKK--RLSAEEALRHPYF 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
78-340 1.03e-23

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 103.12  E-value: 1.03e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDS---AFFWEE----RDIMAFsQSPWIVQL--CCAFQD- 147
Cdd:cd07838      1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVR----VPLSEEgipLSTIREiallKQLESF-EHPNVVRLldVCHGPRt 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 --EKYLYLVMEFMPGgDLVTLTSNY---DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd07838     76 drELKLTLVFEHVDQ-DLATYLDKCpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 MKMDSTgMVRCdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD-------- 294
Cdd:cd07838    155 RIYSFE-MALT-SVVVTLWYRAPEVLLQS----SYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDviglpsee 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  295 --HKNSL----TFP--------DDI-EMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd07838    229 ewPRNSAlprsSFPsytprpfkSFVpEIDEEGLDLLKKMLTFNPHK--RISAFEALQHPYF 287
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
78-341 1.04e-23

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 103.26  E-value: 1.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06656     21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06656     98 LAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-STMV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES-LVGTYGKIMDHKNSLTFPDdiEMSKNAKDLIC 316
Cdd:cd06656    177 GTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPE--RLSAVFRDFLN 250
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  317 AFLssrEVRLGRTG-VDEIKCHPFFK 341
Cdd:cd06656    251 RCL---EMDVDRRGsAKELLQHPFLK 273
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
75-283 1.06e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 102.28  E-value: 1.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAmkqlSKFEMVKRS-DSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd14114      1 YDHYDILEELGTGAFGVVHRCTERATGNNFA----AKFIMTPHEsDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD--RNGHLKLADFGTCMKMDSTG 229
Cdd:cd14114     77 ILEFLSGGELFerIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  230 MVRCDTavGTPDYISPEVLMSQgGTGYYgreCDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd14114    157 SVKVTT--GTAEFAAPEIVERE-PVGFY---TDMWAVGVLSYVLLSGLSPFAGE 204
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
80-339 1.19e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 102.47  E-value: 1.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQQVYAMKQLS-KFEMVKRSDSAFFWE-ERDIMAFSQSPWIVQLCCAFQD--EKYLYLVM 155
Cdd:cd06651     11 RGKLLGQGAFGRVYLCYDVDTGRELAAKQVQfDPESPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK-----MDSTG 229
Cdd:cd06651     91 EYMPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticMSGTG 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 MvrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIemSK 309
Cdd:cd06651    171 I---RSVTGTPYWMSPEVISGEG----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHI--SE 241
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  310 NAKDLI-CAFLSSREvrlgRTGVDEIKCHPF 339
Cdd:cd06651    242 HARDFLgCIFVEARH----RPSAEELLRHPF 268
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-285 1.23e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 102.41  E-value: 1.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd08228      1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTG 229
Cdd:cd08228     81 LELADAGDLSQMIKYFKkqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG-RFFSSK 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  230 MVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESL 285
Cdd:cd08228    160 TTAAHSLVGTPYYMSPERIHENG----YNFKSDIWSLGCLLYEMAALQSPFYGDKM 211
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
84-279 1.76e-23

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 102.13  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd06611     13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELED---FMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGAL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIP--EEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVRCDTAVGTPD 241
Cdd:cd06611     90 DSIMLELERGltEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKST-LQKRDTFIGTPY 168
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207153289  242 YISPEVLMSQG-GTGYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06611    169 WMAPEVVACETfKDNPYDYKADIWSLGITLIELAQMEPP 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
426-985 1.91e-23

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 108.10  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  426 LNHTESN---------DLEKRLKKLE------EKFKhemQAKEELEN-KCRIANQRLEKLSKDLEEEVNARQEAEDNLRS 489
Cdd:COG1196    181 LEATEENlerledilgELERQLEPLErqaekaERYR---ELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  490 LEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKknQISHLsAEKNIHLERQLEEVSAKLQAELEESER 569
Cdd:COG1196    258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--DIARL-EERRRELEERLEELEEELAELEEELEE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  570 LKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKS 649
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  650 SLSKAEVEKRQLQEDLTTLEKEknkqeidlsfkLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLL 729
Cdd:COG1196    415 RLERLEEELEELEEALAELEEE-----------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  730 EERSAKQQLENRLMQLEKENSVLDCDYKQAKH---------ELQELRSLKENLTEQVE-----VLNVRVQQETQRKTLCQ 795
Cdd:COG1196    484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLlaglrglagAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAI 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  796 GDLKVQRQ---------EINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEM-KDQLEAEQYFTKLYK 865
Cdd:COG1196    564 EYLKAAKAgratflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLA 643
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  866 TQIRELKEESD--------------EKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEK 931
Cdd:COG1196    644 GRLREVTLEGEggsaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  932 IMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLK 985
Cdd:COG1196    724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
76-319 4.99e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 102.41  E-value: 4.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvKRSDSAffwEERDIM-AFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd14176     19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPT---EEIEILlRYGQHPNIITLKDVYDDGKYVYVV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH---LKLADFGTCMKMDSTG 229
Cdd:cd14176     92 TELMKGGELLdKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  230 ---MVRCDTAvgtpDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS---ESLVGTYGKIMDHKNSLTFPD 303
Cdd:cd14176    172 gllMTPCYTA----NFVAPEVLERQG----YDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGY 243
                          250
                   ....*....|....*.
gi 1207153289  304 DIEMSKNAKDLICAFL 319
Cdd:cd14176    244 WNSVSDTAKDLVSKML 259
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
84-284 5.05e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 100.48  E-value: 5.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvKRSDSAFFWEERD-------IMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd14194     13 LGSGQFAVVKKCREKSTGLQYAAKFIKK----RRTKSSRRGVSREdierevsILKEIQHPNVITLHEVYENKTDVILILE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNG---HLKLADFGTCMKMDSTGMV 231
Cdd:cd14194     89 LVAGGELFDfLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAHKIDFGNEF 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  232 RcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14194    169 K--NIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDT 215
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
844-924 5.33e-23

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) region encompassing a Rho-binding domain (RBD), and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 93.87  E-value: 5.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  844 EKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDaqqrieDLQEERDSLASQLEVSLTKADSEQLARITVEEQ 923
Cdd:cd22250      1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTRQIKQ------ELEDERESLSAQLELALAKADSEQLARSIAEEQ 74

                   .
gi 1207153289  924 Y 924
Cdd:cd22250     75 I 75
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
58-292 5.87e-23

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 100.84  E-value: 5.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   58 LSRYEKAVCNLKELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffweERDIMAF-SQSP 136
Cdd:cd06639      4 LFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEA----EYNILRSlPNHP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  137 WIVQLCCAF-QDEKY----LYLVMEFMPGG---DLVT--LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNM 206
Cdd:cd06639     80 NVVKFYGMFyKADQYvggqLWLVLELCNGGsvtELVKglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  207 LLDRNGHLKLADFGTCMKMDSTGMVRcDTAVGTPDYISPEVLMSQGGTGY-YGRECDWWSVGVFIYELLVGDTPFYSESL 285
Cdd:cd06639    160 LLTTEGGVKLVDFGVSAQLTSARLRR-NTSVGTPFWMAPEVIACEQQYDYsYDARCDVWSLGITAIELADGDPPLFDMHP 238

                   ....*..
gi 1207153289  286 VGTYGKI 292
Cdd:cd06639    239 VKALFKI 245
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
81-274 5.99e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 99.81  E-value: 5.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQ--LSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd08221      5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEvnLSRLSEKERRDAL---NEIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVrCDT 235
Cdd:cd08221     82 NGGNLhdkIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSM-AES 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207153289  236 AVGTPDYISPEVLmsQGGTgyYGRECDWWSVGVFIYELL 274
Cdd:cd08221    161 IVGTPYYMSPELV--QGVK--YNFKSDIWAVGCVLYELL 195
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
84-273 7.12e-23

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 100.49  E-value: 7.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG-- 161
Cdd:cd06643     13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELED---YMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGav 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVRCDTAVGTPD 241
Cdd:cd06643     90 DAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRT-LQRRDSFIGTPY 168
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207153289  242 YISPEVLMSQGGTGY-YGRECDWWSVGVFIYEL 273
Cdd:cd06643    169 WMAPEVVMCETSKDRpYDYKADVWSLGVTLIEM 201
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
82-339 8.11e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 99.73  E-value: 8.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLsKF--EMVKRSDSAFFWE-ERDIMAFSQSPWIVQLCCAFQD--EKYLYLVME 156
Cdd:cd06652      8 KLLGQGAFGRVYLCYDADTGRELAVKQV-QFdpESPETSKEVNALEcEIQLLKNLLHERIVQYYGCLRDpqERTLSIFME 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS-----TGM 230
Cdd:cd06652     87 YMPGGSIKDQLKSYGaLTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTiclsgTGM 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 vrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIemSKN 310
Cdd:cd06652    167 ---KSVTGTPYWMSPEVISGEG----YGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAHV--SDH 237
                          250       260
                   ....*....|....*....|....*....
gi 1207153289  311 AKDLICAFLSSREVrlgRTGVDEIKCHPF 339
Cdd:cd06652    238 CRDFLKRIFVEAKL---RPSADELLRHTF 263
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
84-283 1.02e-22

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 100.19  E-value: 1.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKF--EMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEK--YLYLVMEFMP 159
Cdd:cd06621      9 LGEGAGGSVTKCRLRNTKTIFALKTITTDpnPDVQKQ----ILRELEINKSCASPYIVKYYGAFLDEQdsSIGIAMEYCE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTL----------TSNYDIPEewaqfyTAEVVL-ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDST 228
Cdd:cd06621     85 GGSLDSIykkvkkkggrIGEKVLGK------IAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNS 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  229 GmvrCDTAVGTPDYISPEVLmsQGGTgyYGRECDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd06621    159 L---AGTFTGTSYYMAPERI--QGGP--YSITSDVWSLGLTLLEVAQNRFPFPPE 206
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
75-280 1.03e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 101.44  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQL--SKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLY 152
Cdd:PLN00034    73 LSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQ----ICREIEILRDVNHPNVVKCHDMFDHNGEIQ 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLvtltSNYDIPEEWAQFYTAEVVLA-LDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMV 231
Cdd:PLN00034   149 VLLEFMDGGSL----EGTHIADEQFLADVARQILSgIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQT-MD 223
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMSQGGTGYY-GRECDWWSVGVFIYELLVGDTPF 280
Cdd:PLN00034   224 PCNSSVGTIAYMSPERINTDLNHGAYdGYAGDIWSLGVSILEFYLGRFPF 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
78-284 1.10e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 100.18  E-value: 1.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06654     22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06654     99 LAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-STMV 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd06654    178 GTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMIEGEPPYLNEN 220
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
76-280 1.48e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 99.70  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffweERDIM-AFSQSPWIVQLCCAF--QDEK--- 149
Cdd:cd06638     18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEA----EYNILkALSDHPNVVKFYGMYykKDVKngd 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTLTSNY-----DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK 224
Cdd:cd06638     94 QLWLVLELCNGGSVTDLVKGFlkrgeRMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  225 MDSTGMVRcDTAVGTPDYISPEVLM-SQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06638    174 LTSTRLRR-NTSVGTPFWMAPEVIAcEQQLDSTYDARCDVWSLGITAIELGDGDPPL 229
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
76-340 1.57e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 98.92  E-value: 1.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14191      2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNG-HLKLADFGTCMKMDSTGMV 231
Cdd:cd14191     79 EMVSGGELFerIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtKIKLIDFGLARRLENAGSL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDI--EMSK 309
Cdd:cd14191    159 K--VLFGTPEFVAPEVINYEP----IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVT--SATWDFDDEAfdEISD 230
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  310 NAKDLICAFLsSREVRlGRTGVDEIKCHPFF 340
Cdd:cd14191    231 DAKDFISNLL-KKDMK-ARLTCTQCLQHPWL 259
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
428-980 2.77e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 104.25  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  428 HTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRK 507
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  508 AGLETDRKRLLENEVSSLKEQLAELKKK----NQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQ 583
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEEleeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  584 LELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQE 663
Cdd:COG1196    398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  664 DLTTLEKEknkqEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNK--------INQSIEAKSET------LKDMEHKLL 729
Cdd:COG1196    478 ALAELLEE----LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavaVLIGVEAAYEAaleaalAAALQNIVV 553
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  730 EERSAKQQLENRL----------MQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLK 799
Cdd:COG1196    554 EDDEVAAAAIEYLkaakagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  800 VQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQyftklykTQIRELKEESDEKV 879
Cdd:COG1196    634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE-------LELEEALLAEEEEE 706
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  880 KLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKdGTIN-- 957
Cdd:COG1196    707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-GPVNll 785
                          570       580
                   ....*....|....*....|....*....
gi 1207153289  958 ------SLEESNRTLTVDVANLASEKEEL 980
Cdd:COG1196    786 aieeyeELEERYDFLSEQREDLEEARETL 814
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
82-341 5.87e-22

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 97.79  E-value: 5.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14174      8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEK--NAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADF--GTCMKMDST----GMV 231
Cdd:cd14174     86 SILAhIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFdlGSGVKLNSActpiTTP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVL--MSQGGTgYYGRECDWWSVGVFIYELLVGDTPFY-----------SESLVGTYGKIMD--HK 296
Cdd:cd14174    166 ELTTPCGSAEYMAPEVVevFTDEAT-FYDKRCDLWSLGVILYIMLSGYPPFVghcgtdcgwdrGEVCRVCQNKLFEsiQE 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  297 NSLTFPDDI--EMSKNAKDLICAFLsSREVRLgRTGVDEIKCHPFFK 341
Cdd:cd14174    245 GKYEFPDKDwsHISSEAKDLISKLL-VRDAKE-RLSAAQVLQHPWVQ 289
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
78-280 6.90e-22

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 97.39  E-value: 6.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFE-----------MVKRsdsafFWEERDIMAFSQSpwIVQLCCAFQ 146
Cdd:cd06636     18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEdeeeeikleinMLKK-----YSHHRNIATYYGA--FIKKSPPGH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKyLYLVMEFMPGG---DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM 223
Cdd:cd06636     91 DDQ-LWLVMEFCGAGsvtDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  224 KMDSTgMVRCDTAVGTPDYISPEVLM-SQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06636    170 QLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDYRSDIWSLGITAIEMAEGAPPL 226
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-279 7.22e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 97.89  E-value: 7.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqLSKFEmVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd06615      1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARK-LIHLE-IKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGG--DLVtLTSNYDIPEEwaqfYTAEVVLA-------LDAIHSLgfIHRDIKPDNMLLDRNGHLKLADFGTC-MKM 225
Cdd:cd06615     79 EHMDGGslDQV-LKKAGRIPEN----ILGKISIAvlrgltyLREKHKI--MHRDVKPSNILVNSRGEIKLCDFGVSgQLI 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  226 DSTGmvrcDTAVGTPDYISPEVLmsQGgtGYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06615    152 DSMA----NSFVGTRSYMSPERL--QG--THYTVQSDIWSLGLSLVEMAIGRYP 197
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
146-286 7.82e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.80  E-value: 7.82e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK 224
Cdd:NF033483    77 EDGGIPYIVMEYVDGRTLKDyIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA 156
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  225 MDSTGMVRCDTAVGTPDYISPEvlmsQGGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLV 286
Cdd:NF033483   157 LSSTTMTQTNSVLGTVHYLSPE----QARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
77-272 8.17e-22

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 97.11  E-value: 8.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKV-SQQVYAMKQLsKFEMVKRSDSAFFWEERDI---MAFSQSPWIVQLCCAFQDEKYLY 152
Cdd:cd14052      1 RFANVELIGSGEFSQVYKVSERVpTGKVYAVKKL-KPNYAGAKDRLRRLEEVSIlreLTLDGHDNIVQLIDSWEYHGHLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLTSNY------DIPEEWAQFytAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM- 225
Cdd:cd14052     80 IQTELCENGSLDVFLSELgllgrlDEFRVWKIL--VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWp 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  226 DSTGMVRcdtaVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYE 272
Cdd:cd14052    158 LIRGIER----EGDREYIAPEILSEH----MYDKPADIFSLGLILLE 196
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
78-284 8.19e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 97.49  E-value: 8.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06655     21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQIN---LQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06655     98 LAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKR-STMV 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd06655    177 GTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNEN 219
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
84-320 8.75e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 98.02  E-value: 8.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvkRSDSAffwEERDIMAFSQS---PWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14180     14 LGEGSFSVCRKCRHRQSGQEYAVKIISR-----RMEAN---TQREVAALRLCqshPNIVALHEVLHDQYHTYLVMELLRG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTLTSNYDIPEEW-AQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCmKMDSTGMVRCDTA 236
Cdd:cd14180     86 GELLDRIKKKARFSESeASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA-RLRPQGSRPLQTP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGK---IMDHKNSLTFPDDIE----MSK 309
Cdd:cd14180    165 CFTLQYAAPELFSNQG----YDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHaadIMHKIKEGDFSLEGEawkgVSE 240
                          250
                   ....*....|.
gi 1207153289  310 NAKDLICAFLS 320
Cdd:cd14180    241 EAKDLVRGLLT 251
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
76-339 1.16e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 96.60  E-value: 1.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVK-LIGRGAFGAVQLVRHKVSQQVYAMKQLskFEMVK-RSDSAFFWEErdimafSQSPWIVQLCCAFQD----EK 149
Cdd:cd14172      3 DDYKLSKqVLGLGVNGKVLECFHRRTGQKCALKLL--YDSPKaRREVEHHWRA------SGGPHIVHILDVYENmhhgKR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTltsnyDIPEEWAQFYT----AEVV----LALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLAD 218
Cdd:cd14172     75 CLLIIMECMEGGELFS-----RIQERGDQAFTereaSEIMrdigTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  219 FGtcMKMDSTGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSES----LVGTYGKIMD 294
Cdd:cd14172    150 FG--FAKETTVQNALQTPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTgqaiSPGMKRRIRM 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  295 HKNSLTFPDDIEMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14172    224 GQYGFPNPEWAEVSEEAKQLIRHLLKTDPTE--RMTITQFMNHPW 266
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
84-319 1.28e-21

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 95.80  E-value: 1.28e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14115      1 IGRGRFSIVKKCLHKATRKDVAVKFVSK-KMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN---GHLKLADFGTCMKMdsTGMVRCDTAVGT 239
Cdd:cd14115     77 LDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI--SGHRHVHHLLGN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  240 PDYISPEVLmsQGGTGYYGreCDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDI--EMSKNAKDLICA 317
Cdd:cd14115    155 PEFAAPEVI--QGTPVSLA--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPDEYfgDVSQAARDFINV 228

                   ..
gi 1207153289  318 FL 319
Cdd:cd14115    229 IL 230
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
78-293 1.73e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 96.34  E-value: 1.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFE---MVKRSdsAFfweeRDIMAFSQ--SPWIVQLCCAFQDEKYLY 152
Cdd:cd07846      3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEddkMVKKI--AM----REIKMLKQlrHENLVNLIEVFRRKKRWY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLtSNYD--IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd07846     77 LVFEFVDHTVLDDL-EKYPngLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  231 VrCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd07846    156 V-YTDYVATRWYRAPELLV---GDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHII 214
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
77-306 1.93e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 96.03  E-value: 1.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVS-QQVYAMKQLSKFEMVKRSDSaffwEERD------------IMAFSQSPWIVQLCC 143
Cdd:cd08528      1 EYAVLELLGSGAFGCVYKVRKKSNgQTLLALKEINMTNPAFGRTE----QERDksvgdiisevniIKEQLRHPNIVRYYK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  144 AFQDEKYLYLVMEFMPGGDLVTLTS-----NYDIPEE--WAQFytAEVVLALDAIH-SLGFIHRDIKPDNMLLDRNGHLK 215
Cdd:cd08528     77 TFLENDRLYIVMELIEGAPLGEHFSslkekNEHFTEDriWNIF--VQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  216 LADFGTCmKMDSTGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH 295
Cdd:cd08528    155 ITDFGLA-KQKGPESSKMTSVVGTILYSCPEIVQNEP----YGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEA 229
                          250
                   ....*....|....*
gi 1207153289  296 K----NSLTFPDDIE 306
Cdd:cd08528    230 EyeplPEGMYSDDIT 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
452-1115 2.10e-21

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 101.55  E-value: 2.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  452 KEELENKCRIANQRLEKLSkDLEEEVnarqeaEDNLRSLEKE-KVLLKHQRTQS---VRKAGLETDRKRLLENEVSSLKE 527
Cdd:COG1196    174 KEEAERKLEATEENLERLE-DILGEL------ERQLEPLERQaEKAERYRELKEelkELEAELLLLKLRELEAELEELEA 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  528 QLAELkkknqishlsaeknihlERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQ 607
Cdd:COG1196    247 ELEEL-----------------EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  608 DKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEidlsfklkAVQ 687
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE--------EEL 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  688 QSLEQEEAEHKTTKARLAdnnkinQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEnsvldcdYKQAKHELQELR 767
Cdd:COG1196    382 EELAEELLEALRAAAELA------AQLEELEEAEEALLERLERLEEELEELEEALAELEEE-------EEEEEEALEEAA 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  768 SLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQL 847
Cdd:COG1196    449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  848 kEMKDQLEAEQYftklykTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEvsLTKADSEQLARITVEEQYSDL 927
Cdd:COG1196    529 -LIGVEAAYEAA------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP--LDKIRARAALAAALARGAIGA 599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  928 EKEKIMKELEIKDMIARHRQDLAE----KDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKS 1003
Cdd:COG1196    600 AVDLVASDLREADARYYVLGDTLLgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1004 LTVSYEKQIQVEKTLKIQAINKLAEvmkktdgrphqiNNTDIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQREINDMQAM 1083
Cdd:COG1196    680 ELEELAERLAEEELELEEALLAEEE------------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1207153289 1084 IAEESQVRLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:COG1196    748 LEEEALEELPEPPDLEELERELERLEREIEAL 779
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
84-319 2.12e-21

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 95.69  E-value: 2.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14097      9 LGQGSFGVVIEATHKETQTKWAIKKINR-EKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG-------HLKLADFGTCMKMDSTGMVRCDT 235
Cdd:cd14097     88 KELLLRKGFfSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQKYGLGEDMLQE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  236 AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDI--EMSKNAKD 313
Cdd:cd14097    168 TCGTPIYMAPEVISAHG----YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEI--RKGDLTFTQSVwqSVSDAAKN 241

                   ....*.
gi 1207153289  314 LICAFL 319
Cdd:cd14097    242 VLQQLL 247
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
81-294 2.33e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 95.18  E-value: 2.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEM--VKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd08222      5 VRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDLVTLTSNY-----DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLdRNGHLKLADFG-TCMKMDSTGMVr 232
Cdd:cd08222     85 EGGDLDDKISEYkksgtTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGiSRILMGTSDLA- 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  233 cDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd08222    163 -TTFTGTPYYMSPEVLKHEG----YNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVE 219
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
77-296 5.00e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 94.43  E-value: 5.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffwEERDIMAFSQ--SPWIVQLCCAFQDEK-YLYL 153
Cdd:cd08223      1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKA---AEQEAKLLSKlkHPNIVSYKESFEGEDgFLYI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgm 230
Cdd:cd08223     78 VMGFCEGGDLYTRLKEQKgvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS-- 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  231 vrCD---TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHK 296
Cdd:cd08223    156 --SDmatTLIGTPYYMSPELFSNKP----YNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGK 218
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
83-339 5.33e-21

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 94.43  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFG-------------AVQLVRHKVSQQVYAMKQLSKFEmvkrsdsaffwEERDIMAFSQSPWIVQLCCAFQDEK 149
Cdd:cd06631      8 VLGKGAYGtvycgltstgqliAVKQVELDTSDKEKAEKEYEKLQ-----------EEVDLLKTLKHVNIVGYLGTCLEDN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGT----CMK 224
Cdd:cd06631     77 VVSIFMEFVPGGSIASILARFGaLEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCakrlCIN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  225 MDSTGMVRCDTAV-GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSL-TFP 302
Cdd:cd06631    157 LSSGSQSQLLKSMrGTPYWMAPEVINETG----HGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVpRLP 232
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1207153289  303 DDieMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd06631    233 DK--FSPEARDFVHACLTRDQDE--RPSAEQLLKHPF 265
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
81-276 5.85e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 95.67  E-value: 5.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMV---KRSdsaffWEERDIMAFSQSPWIVQLCCAFQDEKY-----L 151
Cdd:cd07834      5 LKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvFDDLidaKRI-----LREIKILRHLKHENIIGLLDILRPPSPeefndV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGgDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd07834     80 YIVTELMET-DLhKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  231 VRCDTA-VGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVG 276
Cdd:cd07834    159 KGFLTEyVVTRWYRAPELLLSSKK---YTKAIDIWSVGCIFAELLTR 202
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
82-281 6.34e-21

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 94.10  E-value: 6.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAV-----QLVRHKVSQQVyAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQL--CCAfqDEKYLYLV 154
Cdd:pfam07714    5 EKLGEGAFGEVykgtlKGEGENTKIKV-AVKTLKEGADEEERED--FLEEASIMKKLDHPNIVKLlgVCT--QGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:pfam07714   80 TEYMPGGDLLDfLRKHkRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  233 CDTAVGTP-DYISPEVLMsqggTGYYGRECDWWSVGVFIYELL-VGDTPFY 281
Cdd:pfam07714  160 KRGGGKLPiKWMAPESLK----DGKFTSKSDVWSFGVLLWEIFtLGEQPYP 206
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
433-979 6.90e-21

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 99.86  E-value: 6.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELEnkcrianQRLEKLSKDLEEEVNARQE-------AEDNLRSLEKEKVLLKHQRTQSV 505
Cdd:pfam01576   79 ELESRLEEEEERSQQLQNEKKKMQ-------QHIQDLEEQLDEEEAARQKlqlekvtTEAKIKKLEEDILLLEDQNSKLS 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  506 RKagletdrKRLLENEVSSLKEQLAELKKKNQisHLSAEKNIHlERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLE 585
Cdd:pfam01576  152 KE-------RKLLEERISEFTSNLAEEEEKAK--SLSKLKNKH-EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:pfam01576  222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLekeknKQEIDLSFKLKAVQQSL----EQE--------EAEHKTTKARLAD-NNKINQSIEAKSETLKdmehkllEER 732
Cdd:pfam01576  302 EAL-----KTELEDTLDTTAAQQELrskrEQEvtelkkalEEETRSHEAQLQEmRQKHTQALEELTEQLE-------QAK 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  733 SAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVqQETQRktlcqgdlkvQRQEinsLRSSE 812
Cdd:pfam01576  370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARL-SESER----------QRAE---LAEKL 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEaeqyftklyktqirelkEESDEKVKLykdaQQRIEDL 892
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ-----------------EETRQKLNL----STRLRQL 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  893 QEERDSLASQLEvsltkadSEQLARITVEEQYSDLEKEkimkeleikdmIARHRQDLAEKDGTINSLEESNRTLTVDVAN 972
Cdd:pfam01576  495 EDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQ-----------LSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556

                   ....*..
gi 1207153289  973 LASEKEE 979
Cdd:pfam01576  557 LTQQLEE 563
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
72-280 7.72e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 94.75  E-value: 7.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfemvKRSDSAffwEER-------DIMAFSQ-SPWIVQLCC 143
Cdd:cd06618     11 KADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQM------RRSGNK---EENkrilmdlDVVLKSHdCPYIVKCYG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  144 AFQDEKYLYLVMEFMPG-GDLVTLTSNYDIPEEWAQFYTAEVVLALDAI---HslGFIHRDIKPDNMLLDRNGHLKLADF 219
Cdd:cd06618     82 YFITDSDVFICMELMSTcLDKLLKRIQGPIPEDILGKMTVSIVKALHYLkekH--GVIHRDVKPSNILLDESGNVKLCDF 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  220 GTCMKM-DStgMVRCDTAvGTPDYISPEVLMSQGGTGYYGReCDWWSVGVFIYELLVGDTPF 280
Cdd:cd06618    160 GISGRLvDS--KAKTRSA-GCAAYMAPERIDPPDNPKYDIR-ADVWSLGISLVELATGQFPY 217
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
82-281 1.08e-20

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 93.38  E-value: 1.08e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289    82 KLIGRGAFGAVQL-----VRHKVSQQVyAMKQLSkfEMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAfqDEKYLYLV 154
Cdd:smart00221    5 KKLGEGAFGEVYKgtlkgKGDGKEVEV-AVKTLK--EDASEQQIEEFLREARIMRKLDHPNIVKLlgVCT--EEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   155 MEFMPGGDLVTL---TSNYDIPeeWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:smart00221   80 MEYMPGGDLLDYlrkNRPKELS--LSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289   230 MVRCDTAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELL-VGDTPFY 281
Cdd:smart00221  158 YYKVKGGKLPIRWMAPESLK----EGKFTSKSDVWSFGVLLWEIFtLGEEPYP 206
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
78-273 1.14e-20

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 93.28  E-value: 1.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAffWEE--RDIMAFSQ--SPWIVQLCCAFQDEKYLYL 153
Cdd:cd06607      3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSY--SGKQSTEK--WQDiiKEVKFLRQlrHPNTIEYKGCYLREHTAWL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPG--GDLVTLTSNYDIPEEWAQFyTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcmkmdSTGMV 231
Cdd:cd06607     79 VMEYCLGsaSDIVEVHKKPLQEVEIAAI-CHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG------SASLV 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  232 R-CDTAVGTPDYISPEVLMSQgGTGYYGRECDWWSVGVFIYEL 273
Cdd:cd06607    152 CpANSFVGTPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIEL 193
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-285 1.89e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 93.56  E-value: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd08229     23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYD-----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTG 229
Cdd:cd08229    103 LELADAGDLSRMIKHFKkqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG-RFFSSK 181
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  230 MVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESL 285
Cdd:cd08229    182 TTAAHSLVGTPYYMSPERIHENG----YNFKSDIWSLGCLLYEMAALQSPFYGDKM 233
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
78-280 2.61e-20

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 92.81  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06642      6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06642     84 LGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR-NTFV 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06642    163 GTPFWMAPEVIKQSA----YDFKADIWSLGITAIELAKGEPPN 201
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
82-280 2.79e-20

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 92.78  E-value: 2.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14173      8 EVLGEGAYARVQTCINLITNKEYAVKIIEK--RPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL---DRNGHLKLADF--GTCMKMDS----TGMV 231
Cdd:cd14173     86 SILShIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFdlGSGIKLNSdcspISTP 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLMS-QGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14173    166 ELLTPCGSAEYMAPEVVEAfNEEASIYDKRCDLWSLGVILYIMLSGYPPF 215
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
433-1029 3.71e-20

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 97.44  E-value: 3.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKekvLLKHQRTQSVRKAGLEt 512
Cdd:PRK03918   190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES---LEGSKRKLEEKIRELE- 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLLENEVSSLKEQLAELKKKNQishlSAEKNIHLER---QLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLR 589
Cdd:PRK03918   266 ERIEELKKEIEELEEKVKELKELKE----KAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  590 ELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNagsetitdLQGRIYGLEGElkHIKSSLSKAEVEKRQLQEDLTTLE 669
Cdd:PRK03918   342 ELKKKLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT 411
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  670 KEKNKQEIDLSFKLKAVQQsLEQEEAEHKTTKARLADNNKINQsIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEN 749
Cdd:PRK03918   412 ARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  750 SvldcdykqAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTlcqGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTL 829
Cdd:PRK03918   490 K--------KESELIKLKELAEQLKELEEKLKKYNLEELEKKA---EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  830 EkqnqELSKEREESEKQLKEMKDQLEAEQYFT-KLYKTQIRELKEESDEKVKLyKDAQQRIEDLQEERDSLASQLEVSLT 908
Cdd:PRK03918   559 A----ELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  909 KADSEQLARITVEEQYSDLEKEKIMKELE-IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHI 987
Cdd:PRK03918   634 ELAETEKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  988 QqklekikEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEV 1029
Cdd:PRK03918   714 E-------KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
76-357 4.06e-20

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 92.49  E-value: 4.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDI-MAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:cd06617      1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRA--TVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWIC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPggdlvtlTSNYD-----------IPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd06617     79 MEVMD-------TSLDKfykkvydkgltIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGIS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 MKM-DStgMVRCDTAvGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGD-------TPFysESLvgtygKIMD 294
Cdd:cd06617    152 GYLvDS--VAKTIDA-GCKPYMAPERINPELNQKGYDVKSDVWSLGITMIELATGRfpydswkTPF--QQL-----KQVV 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  295 HKNSLTFPDDiEMSKNAKDLICAFLSSreVRLGRTGVDEIKCHPFFKNDQWTFDTIRDTMAPV 357
Cdd:cd06617    222 EEPSPQLPAE-KFSPEFQDFVNKCLKK--NYKERPNYPELLQHPFFELHLSKNTDVASFVSLI 281
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
76-339 5.98e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 91.56  E-value: 5.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWE---ERDIMAFSQSPWIVQLCCAFQDEKYLY 152
Cdd:cd14196      5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEierEVSILRQVLHPNIITLHDVYENRTDVV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNG---HLKLADFGTCMKMDS 227
Cdd:cd14196     85 LILELVSGGELFDfLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIED 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TgmVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdhkNSLTFPDDIEM 307
Cdd:cd14196    165 G--VEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANI----TAVSYDFDEEF 234
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207153289  308 ----SKNAKDLICAFLsSREVRlGRTGVDEIKCHPF 339
Cdd:cd14196    235 fshtSELAKDFIRKLL-VKETR-KRLTIQEALRHPW 268
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
78-280 7.83e-20

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 91.70  E-value: 7.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLS----KFEMVKRSDSAF--FWEERDIMAFSQSpWIVQLCCAFQDEkyL 151
Cdd:cd06637      8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDvtgdEEEEIKQEINMLkkYSHHRNIATYYGA-FIKKNPPGMDDQ--L 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGG---DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDST 228
Cdd:cd06637     85 WLVMEFCGAGsvtDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  229 gMVRCDTAVGTPDYISPEVLM-SQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06637    165 -VGRRNTFIGTPYWMAPEVIAcDENPDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
78-279 8.67e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 91.27  E-value: 8.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06640      6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06640     84 LGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR-NTFV 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06640    163 GTPFWMAPEVIQQSA----YDSKADIWSLGITAIELAKGEPP 200
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
72-279 1.02e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 92.04  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqLSKFEmVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd06650      1 ELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARK-LIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAI---HSLgfIHRDIKPDNMLLDRNGHLKLADFGTCMKM-D 226
Cdd:cd06650     79 SICMEHMDGGSLdQVLKKAGRIPEQILGKVSIAVIKGLTYLrekHKI--MHRDVKPSNILVNSRGEIKLCDFGVSGQLiD 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  227 STGmvrcDTAVGTPDYISPEVLMsqgGTgYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06650    157 SMA----NSFVGTRSYMSPERLQ---GT-HYSVQSDIWSMGLSLVEMAVGRYP 201
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
428-1112 1.03e-19

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 96.19  E-value: 1.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  428 HTESNDLEKRLKKLEEK---FKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKV-LLKHQRTQ 503
Cdd:pfam02463  180 EETENLAELIIDLEELKlqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQeEIESSKQE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  504 SVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEE----SERLKKAQIEAFR 579
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEkkkaEKELKKEKEEIEE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  580 QSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSEtitdlQGRIYGLEGELKHIKSSLSKAEVEKR 659
Cdd:pfam02463  340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-----AAKLKEEELELKSEEEKEAQLLLELA 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  660 QLQEDLTTLE--KEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQ 737
Cdd:pfam02463  415 RQLEDLLKEEkkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  738 LENRLMQLEKENSvldcdykqakhelqelrSLKENLTEQVEVLNVRVQQETQRKTLCQ-GDLKVQRQEINSLRSSEQQLK 816
Cdd:pfam02463  495 LEERSQKESKARS-----------------GLKVLLALIKDGVGGRIISAHGRLGDLGvAVENYKVAISTAVIVEVSATA 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  817 QELNHLLELKLTLEKQNQELSKEREESEK-QLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEE 895
Cdd:pfam02463  558 DEVEERQKLVRALTELPLGARKLRLLIPKlKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  896 RDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLAS 975
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  976 EKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQ-IQVEKTLKIQAINKLAEVMKKT-DGRPHQINNTDIRRKEKEIR 1053
Cdd:pfam02463  718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEkSRLKKEEKEEEKSELSLKEKELaEEREKTEKLKVEEEKEEKLK 797
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1054 QLQLQLRTEKEKLNHSIIKYQREINDMQAM----IAEESQVRLEMQMSLDSKDSDIERLRSQL 1112
Cdd:pfam02463  798 AQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKEEQKLEKLAEEELERLE 860
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
82-339 1.21e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 91.25  E-value: 1.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRsDSAFFWEErdimafSQSPWIVQLCCAF----QDEKYLYLVMEF 157
Cdd:cd14170      8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARR-EVELHWRA------SQCPHIVRIVDVYenlyAGRKCLLIVMEC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR---NGHLKLADFGtcMKMDSTGMV 231
Cdd:cd14170     81 LDGGELFSRIQDRGdqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFG--FAKETTSHN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLV----GTYGKIMDHKNSLTFPDDIEM 307
Cdd:cd14170    159 SLTTPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaispGMKTRIRMGQYEFPNPEWSEV 234
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  308 SKNAKDLICAFLSSREVRlgRTGVDEIKCHPF 339
Cdd:cd14170    235 SEEVKMLIRNLLKTEPTQ--RMTITEFMNHPW 264
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
76-284 1.45e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 90.83  E-value: 1.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPwIVQLCCAFQDEKYLYLVM 155
Cdd:cd07848      1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQEN-IVELKEAFRRRGKLYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCD 234
Cdd:cd07848     80 EYVEKNMLELLEEMPNgVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYT 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  235 TAVGTPDYISPEVLMSqggtGYYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd07848    160 EYVATRWYRSPELLLG----APYGKAVDMWSVGCILGELSDGQPLFPGES 205
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
82-281 1.67e-19

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 89.90  E-value: 1.67e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289    82 KLIGRGAFGAVQL-----VRHKVSQQVyAMKQLSkfEMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAfqDEKYLYLV 154
Cdd:smart00219    5 KKLGEGAFGEVYKgklkgKGGKKKVEV-AVKTLK--EDASEQQIEEFLREARIMRKLDHPNVVKLlgVCT--EEEPLYIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   155 MEFMPGGDLVTLTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:smart00219   80 MEYMEGGDLLSYLRKNRPKLSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYR 159
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1207153289   233 CDTAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELL-VGDTPFY 281
Cdd:smart00219  160 KRGGKLPIRWMAPESLK----EGKFTSKSDVWSFGVLLWEIFtLGEQPYP 205
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
76-319 1.98e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 89.85  E-value: 1.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvKRSDSAFFWEERD-------IMAFSQSPWIVQLCCAFQDE 148
Cdd:cd14105      5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKK----RRSKASRRGVSREdierevsILRQVLHPNIITLHDVFENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRN---GHLKLADFGTCM 223
Cdd:cd14105     81 TDVVLILELVAGGELFDfLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNvpiPRIKLIDFGLAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  224 KMDSTGMVRcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPD 303
Cdd:cd14105    161 KIEDGNEFK--NIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT--AVNYDFDD 232
                          250
                   ....*....|....*...
gi 1207153289  304 DI--EMSKNAKDLICAFL 319
Cdd:cd14105    233 EYfsNTSELAKDFIRQLL 250
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
78-279 2.05e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 90.13  E-value: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06641      6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRcDTAV 237
Cdd:cd06641     84 LGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKR-N*FV 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06641    163 GTPFWMAPEVIKQSA----YDSKADIWSLGITAIELARGEPP 200
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
76-281 3.05e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 89.33  E-value: 3.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd06645     11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVI---KLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTS-NYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVRCD 234
Cdd:cd06645     88 EFCGGGSLQDIYHvTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITAT-IAKRK 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  235 TAVGTPDYISPEVLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd06645    167 SFIGTPYWMAPEVAAVERKGG-YNQLCDIWAVGITAIELAELQPPMF 212
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
76-276 4.18e-19

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 90.44  E-value: 4.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFE---MVKRSdsaffWEERDIMAFSQSPWIVQL--------CCA 144
Cdd:cd07849      5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEhqtYCLRT-----LREIKILLRFKHENIIGIldiqrpptFES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  145 FQDekyLYLVMEFMPGgDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG---- 220
Cdd:cd07849     80 FKD---VYIVQELMET-DLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGlari 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  221 TCMKMDSTGMVrcDTAVGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVG 276
Cdd:cd07849    156 ADPEHDHTGFL--TEYVATRWYRAPEIMLNSKG---YTKAIDIWSVGCILAEMLSN 206
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
84-280 4.57e-19

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 88.65  E-value: 4.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKvSQQVyAMKQLsKFEMVKRsdsAFfweERDIMAFSQ--SPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14058      1 VGRGSFGVVCKARWR-NQIV-AVKII-ESESEKK---AF---EVEVRQLSRvdHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLvtltSNYDIPEEWAQFYTAEVVL--------ALDAIHSLG---FIHRDIKPDNMLLDRNGH-LKLADFGTCMKMdSTG 229
Cdd:cd14058     72 SL----YNVLHGKEPKPIYTAAHAMswalqcakGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTACDI-STH 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  230 MVrcdTAVGTPDYISPEVLmsQGGTgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14058    147 MT---NNKGSAAWMAPEVF--EGSK--YSEKCDVFSWGIILWEVITRRKPF 190
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
82-340 4.87e-19

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 88.34  E-value: 4.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQlskfemvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKY-LYLVMEFMPG 160
Cdd:cd14109     10 EDEKRAAQGAPFHVTERSTGRNFLAQL--------RYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLAST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT---LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLdRNGHLKLADFGTCMKMDSTGMVRCDtaV 237
Cdd:cd14109     82 IELVRdnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTTLI--Y 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICA 317
Cdd:cd14109    159 GSPEFVSPEIVNSYP----VTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKK 234
                          250       260
                   ....*....|....*....|...
gi 1207153289  318 FLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14109    235 LLVYIPES--RLTVDEALNHPWF 255
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
81-330 6.06e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 88.48  E-value: 6.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14192      9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVK---NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH-LKLADFGTCMKMDSTGMVRCDta 236
Cdd:cd14192     86 GELFdrITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVN-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLIC 316
Cdd:cd14192    164 FGTPEFLAPEVVNYD----FVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFIS 239
                          250
                   ....*....|....*
gi 1207153289  317 AFL-SSREVRLGRTG 330
Cdd:cd14192    240 RLLvKEKSCRMSATQ 254
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
72-279 6.25e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 89.72  E-value: 6.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAmKQLSKFEmVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd06649      1 ELKDDDFERISELGAGNGGVVTKVQHKPSGLIMA-RKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSL-GFIHRDIKPDNMLLDRNGHLKLADFGTCMKM-DST 228
Cdd:cd06649     79 SICMEHMDGGSLdQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLiDSM 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  229 GmvrcDTAVGTPDYISPEVLMsqgGTgYYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd06649    159 A----NSFVGTRSYMSPERLQ---GT-HYSVQSDIWSMGLSLVELAIGRYP 201
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
85-296 7.11e-19

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 87.96  E-value: 7.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   85 GRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLV 164
Cdd:cd14111     12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQG----VLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  165 -TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDYI 243
Cdd:cd14111     88 hSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTGTLEYM 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  244 SPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHK 296
Cdd:cd14111    168 APEMVKGE----PVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAK 216
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
77-280 7.12e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 88.40  E-value: 7.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLS---KFEMVKRSDSaffweERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd06619      2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPldiTVELQKQIMS-----ELEILYKCDSPYIIGFYGAFFVENRISI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSnydIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTcmkmdSTGMVR- 232
Cdd:cd06619     77 CTEFMDGGSLDVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGV-----STQLVNs 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  233 -CDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd06619    149 iAKTYVGTNAYMAPERISGE----QYGIHSDVWSLGISFMELALGRFPY 193
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
427-1137 1.07e-18

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 92.39  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  427 NHTESNDLEKRLKKLeekfkhemqaKEELENKcriaNQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQrtqsvr 506
Cdd:TIGR04523   31 QDTEEKQLEKKLKTI----------KNELKNK----EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDK------ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  507 kaglETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKKaqieafrQSQQLEL 586
Cdd:TIGR04523   91 ----LKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  587 SLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAgsetitdlqgriyglegeLKHIKSSLSKAEVEKRQLQEDLT 666
Cdd:TIGR04523  160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK------------------LELLLSNLKKKIQKNKSLESQIS 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  667 TLEKEKNKQEIDLSFKlkavQQSLEQEEAEHKTTKarladnNKINQSIEAKSETLKDMEHKLLEERSAKQ---QLENRLM 743
Cdd:TIGR04523  222 ELKKQNNQLKDNIEKK----QQEINEKTTEISNTQ------TQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLN 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  744 QLEKENSVLDcdyKQAKHELqeLRSLKENLTEQVEvlnvrvqqetqRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLL 823
Cdd:TIGR04523  292 QLKSEISDLN---NQKEQDW--NKELKSELKNQEK-----------KLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  824 ElkltlekQNQELSKEREESEKQLKEMKDqlEAEQYFTKLY--KTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLas 901
Cdd:TIGR04523  356 S-------ENSEKQRELEEKQNEIEKLKK--ENQSYKQEIKnlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL-- 424
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  902 qlevsltkadseqlaritvEEQYSDLEKEKIMKELEIKDmiarhrqdlaekdgtinsLEESNRTLTVDVANLASEKEELN 981
Cdd:TIGR04523  425 -------------------EKEIERLKETIIKNNSEIKD------------------LTNQDSVKELIIKNLDNTRESLE 467
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  982 NKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKTDGRPHQIN--NTDIRRKEKEIRQLQLQL 1059
Cdd:TIGR04523  468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklESEKKEKESKISDLEDEL 547
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1060 RTEKEKLNHSIIK-----YQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSLsihsldTTSISSIGNDLDS 1134
Cdd:TIGR04523  548 NKDDFELKKENLEkeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK------EKKISSLEKELEK 621

                   ...
gi 1207153289 1135 DEA 1137
Cdd:TIGR04523  622 AKK 624
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
82-340 1.26e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 87.29  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKfEMVKRsdsaffWEERD------------IMAFSQS-PWIVQLCCAFQDE 148
Cdd:cd14005      6 DLLGKGGFGTVYSGVRIRDGLPVAVKFVPK-SRVTE------WAMINgpvpvpleiallLKASKPGvPGVIRLLDWYERP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEF-MPGGDLVTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFGtCMKM 225
Cdd:cd14005     79 DGFLLIMERpEPCQDLFDFITERgALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG-CGAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRcdTAVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESlvgtygKIMDHKNsLTFPDdi 305
Cdd:cd14005    158 LKDSVYT--DFDGTRVYSPPEWIRHG---RYHGRPATVWSLGILLYDMLCGDIPFENDE------QILRGNV-LFRPR-- 223
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1207153289  306 eMSKNAKDLICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14005    224 -LSKECCDLISRCLQFDPSK--RPSLEQILSHPWF 255
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
78-274 1.46e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 87.95  E-value: 1.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLS-KFEMVKRSDSAFfweeRDIMAFSQ--SPWIVQLCCAFQDEKYLYLV 154
Cdd:cd07860      2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRlDTETEGVPSTAI----REISLLKElnHPNIVKLLDVIHTENKLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMpGGDL---VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMdstGM- 230
Cdd:cd07860     78 FEFL-HQDLkkfMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF---GVp 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  231 VRCDT-AVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELL 274
Cdd:cd07860    154 VRTYThEVVTLWYRAPEILL---GCKYYSTAVDIWSLGCIFAEMV 195
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
82-340 1.95e-18

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 86.58  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKF----EMVKRsdsaFFWEERDIMAFSQSPWIVQLCCAFQD-EKYLYLVME 156
Cdd:cd14163      6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeEFIQR----FLPRELQIVERLDHKNIIHVYEMLESaDGKIYLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLdRNGHLKLADFGTCMKMDSTGMVRCDT 235
Cdd:cd14163     82 LAEDGDVFDcVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGRELSQT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  236 AVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLvgtyGKIMDHKNS-LTFPDDIEMSKNAKDL 314
Cdd:cd14163    161 FCGSTAYAAPEVLQ---GVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDI----PKMLCQQQKgVSLPGHLGVSRTCQDL 233
                          250       260
                   ....*....|....*....|....*.
gi 1207153289  315 ICAFLSSREVRlgRTGVDEIKCHPFF 340
Cdd:cd14163    234 LKRLLEPDMVL--RPSIEEVSWHPWL 257
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
82-289 1.95e-18

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 86.90  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14198     14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAGG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTsnydIPEEWAQFYTAEVVLALDAI-------HSLGFIHRDIKPDNMLLDRN---GHLKLADFGTCMKMDSTGMV 231
Cdd:cd14198     94 EIFNLC----VPDLAEMVSENDIIRLIRQIlegvyylHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACEL 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  232 RcdTAVGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPFYSESLVGTY 289
Cdd:cd14198    170 R--EIMGTPEYLAPEILNYDPIT----TATDMWNIGVIAYMLLTHESPFVGEDNQETF 221
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
82-280 3.16e-18

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 86.05  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQL----VRHKVSQQVyAMKQLSKFEM-VKRSDsafFWEERDIMAFSQSPWIVQLC-CAFQDEKyLYLVM 155
Cdd:cd00192      1 KKLGEGAFGEVYKgklkGGDGKTVDV-AVKTLKEDASeSERKD---FLKEARVMKKLGHPNVVRLLgVCTEEEP-LYLVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT--------LTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd00192     76 EYMEGGDLLDflrksrpvFPSPEPSTLSLKDLlsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDI 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  226 DSTGMVRCDTavGTPDYI---SPEVLMsqggTGYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd00192    156 YDDDYYRKKT--GGKLPIrwmAPESLK----DGIFTSKSDVWSFGVLLWEIFTlGATPY 208
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
76-315 3.26e-18

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 86.23  E-value: 3.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14088      1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAA--KNEINILKMVKHPNILQLVDVFETRKEYFIFL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLV--TLTSNYdIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD---RNGHLKLADFGTCmKMDsTGM 230
Cdd:cd14088     79 ELATGREVFdwILDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLA-KLE-NGL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  231 VRcdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYG--------KIM--DHKNSLT 300
Cdd:cd14088    156 IK--EPCGTPEYLAPEVVGRQ----RYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknlfrKILagDYEFDSP 229
                          250
                   ....*....|....*
gi 1207153289  301 FPDDIemSKNAKDLI 315
Cdd:cd14088    230 YWDDI--SQAAKDLV 242
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
77-274 5.26e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 85.62  E-value: 5.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQ--------------LSKFEMVKRSDSAFFWEERDIMAFSQS--PWIVQ 140
Cdd:cd14047      7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRvklnnekaerevkaLAKLDHPNIVRYNGCWDGFDYDPETSSsnSSRSK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  141 lccafqdEKYLYLVMEFMPGGdlvTLTS-----NYDIPEEW-AQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHL 214
Cdd:cd14047     87 -------TKCLFIQMEFCEKG---TLESwiekrNGEKLDKVlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKV 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  215 KLADFGTCMKMdsTGMVRCDTAVGTPDYISPEvlmsQGGTGYYGRECDWWSVGVFIYELL 274
Cdd:cd14047    157 KIGDFGLVTSL--KNDGKRTKSKGTLSYMSPE----QISSQDYGKEVDIYALGLILFELL 210
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
83-284 5.67e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 88.92  E-value: 5.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVqLVRHKVSqqVYAMKQLSKFEMVK-RSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:PTZ00267    74 LVGRNPTTAA-FVATRGS--DPKEKVVAKFVMLNdERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGG 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DL-----VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM-DSTGMVRCDT 235
Cdd:PTZ00267   151 DLnkqikQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYsDSVSLDVASS 230
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  236 AVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:PTZ00267   231 FCGTPYYLAPELWERK----RYSKKADMWSLGVILYELLTLHRPFKGPS 275
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
84-280 7.01e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 85.96  E-value: 7.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQlSKFEMVKRSDSAFFWE-ERDIMAFSQSPWIVQlCCAFQDEKYL-------YLVM 155
Cdd:cd13989      1 LGSGGFGYVTLWKHQDTGEYVAIKK-CRQELSPSDKNRERWClEVQIMKKLNHPNVVS-ARDVPPELEKlspndlpLLAM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDL---VTLTSNY-DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRNGHL--KLADFGTCMKMDST 228
Cdd:cd13989     79 EYCSGGDLrkvLNQPENCcGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKELDQG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  229 GMvrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd13989    159 SL--CTSFVGTLQYLAPELFESKK----YTCTVDYWSFGTLAFECITGYRPF 204
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
81-287 7.76e-18

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 85.46  E-value: 7.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMvKRSDSAFfwEERDIM-AFSQSPWIVQLC-CAFQD---EKYLYLVM 155
Cdd:cd13985      5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE-EQLRVAI--KEIEIMkRLCGHPNIVQYYdSAILSsegRKEVLLLM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGG--DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMV 231
Cdd:cd13985     82 EYCPGSlvDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLER 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  232 RCDTAV--------GTPDYISPEVLmsqGGTGYY--GRECDWWSVGVFIYELLVGDTPFYSESLVG 287
Cdd:cd13985    162 AEEVNIieeeiqknTTPMYRAPEMI---DLYSKKpiGEKADIWALGCLLYKLCFFKLPFDESSKLA 224
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
72-281 8.38e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 89.80  E-value: 8.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEErDIMAFSQSPWIVQLCCAFQDE--K 149
Cdd:PTZ00266     9 ESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEV-NVMRELKHKNIVRYIDRFLNKanQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLV-TLTSNY----DIPEEWAQFYTAEVVLALDAIHSLG-------FIHRDIKPDNMLL--------- 208
Cdd:PTZ00266    88 KLYILMEFCDAGDLSrNIQKCYkmfgKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLstgirhigk 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  209 ------DRNGH--LKLADFGTCMKMDSTGMVRcdTAVGTPDYISPEVLMSQggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:PTZ00266   168 itaqanNLNGRpiAKIGDFGLSKNIGIESMAH--SCVGTPYYWSPELLLHE--TKSYDDKSDMWALGCIIYELCSGKTPF 243

                   .
gi 1207153289  281 Y 281
Cdd:PTZ00266   244 H 244
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
77-284 8.60e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 85.55  E-value: 8.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd07861      1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI-RLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMpGGDLV----TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMkmdSTGM-V 231
Cdd:cd07861     80 FL-SMDLKkyldSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLAR---AFGIpV 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  232 RCDT-AVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd07861    156 RVYThEVVTLWYRAPEVLL---GSPRYSTPVDIWSIGTIFAEMATKKPLFHGDS 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
425-773 8.61e-18

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 90.12  E-value: 8.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  425 GLNHTESNDLEKR--LKKLEEKFkhemqakEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRT 502
Cdd:TIGR02168  664 GSAKTNSSILERRreIEELEEKI-------EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  503 QSVRKAGLETDRKRLLENEVSSLKEQLAELKKKnqishlsAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAfrqsq 582
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEER-------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----- 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  583 qlelsLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRErnagsetITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQ 662
Cdd:TIGR02168  805 -----LDELRAELTLLNEEAANLRERLESLERRIAATERR-------LEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  663 EDLTTLEKEKNKQEIDL-SFKLKAVQQSLEQEEAEHKTTKAR---LADNNKINQsIEAKSETLKDMEHKLLEERSAKQQL 738
Cdd:TIGR02168  873 SELEALLNERASLEEALaLLRSELEELSEELRELESKRSELRrelEELREKLAQ-LELRLEGLEVRIDNLQERLSEEYSL 951
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1207153289  739 EnrLMQLEKENSVLDCDYKQAKHELQELRSLKENL 773
Cdd:TIGR02168  952 T--LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
84-294 8.62e-18

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 86.65  E-value: 8.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMV---KRSdsaffWEERDIMAFSQSPWIVQLCCAFQ------DEKYLYL 153
Cdd:cd07855     13 IGSGAYGVVCSAIDTKSGQKVAIKKIPNaFDVVttaKRT-----LRELKILRHFKHDNIIAIRDILRpkvpyaDFKDVYV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGgDLVTLT-SNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd07855     88 VLDLMES-DLHHIIhSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEH 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  233 C---DTAVGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07855    167 KyfmTEYVATRWYRAPELMLSLPE---YTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILT 228
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
83-315 9.05e-18

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 85.45  E-value: 9.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAV----QLVRH-----KVSQQVYAMKQLSKFEMVKRSDsaffwEERDIMAFSQSPWIVQLCCAFQ-DEKYLY 152
Cdd:cd13990      7 LLGKGGFSEVykafDLVEQryvacKIHQLNKDWSEEKKQNYIKHAL-----REYEIHKSLDHPRIVKLYDVFEiDTDSFC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSL--GFIHRDIKPDNMLLDRN---GHLKLADFGTCMKMD 226
Cdd:cd13990     82 TVLEYCDGNDLDFyLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKIMD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 -----STGMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPF----YSESLVgtYGKIMDHKN 297
Cdd:cd13990    162 desynSDGMELTSQGAGTYWYLPPECFVVGKTPPKISSKVDVWSVGVIFYQMLYGRKPFghnqSQEAIL--EENTILKAT 239
                          250
                   ....*....|....*...
gi 1207153289  298 SLTFPDDIEMSKNAKDLI 315
Cdd:cd13990    240 EVEFPSKPVVSSEAKDFI 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
76-276 9.48e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 85.50  E-value: 9.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFE---MVKRSdsAFfweeRDIMAFSQ--SPWIVQLCCAFQDEKY 150
Cdd:cd07847      1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEddpVIKKI--AL----REIRMLKQlkHPNLVNLIEVFRRKRK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd07847     75 LHLVFEYCDHTVLNELEKNpRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  230 MVRCDTaVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd07847    155 DDYTDY-VATRWYRAPELLV---GDTQYGPPVDVWAIGCVFAELLTG 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
416-951 1.13e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.23  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  416 SEEDIIEDHGLNHTESNDLEKRLKKLEEkfkhemqAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKV 495
Cdd:COG1196    296 ELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  496 LLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQIshlSAEKNIHLERQLEEVSAKLQAELEESERLKKAQI 575
Cdd:COG1196    369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA---LLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  576 EAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYG-LEGELKHIKSSLSKA 654
Cdd:COG1196    446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGA 525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  655 EVEKRQLQEDLTT-LEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERS 733
Cdd:COG1196    526 VAVLIGVEAAYEAaLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA 605
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  734 AKQQLEN----RLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLR 809
Cdd:COG1196    606 SDLREADaryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  810 SSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQyftKLYKTQIRELKEESDEKVKLYKDAQQRI 889
Cdd:COG1196    686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER---EELLEELLEEEELLEEEALEELPEPPDL 762
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  890 EDLQEERDSLASQLE----VSLTkADsEQLARI-----TVEEQYSDLEKEKimKELE--IKDMIARHRQDLAE 951
Cdd:COG1196    763 EELERELERLEREIEalgpVNLL-AI-EEYEELeerydFLSEQREDLEEAR--ETLEeaIEEIDRETRERFLE 831
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
77-281 1.22e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 84.70  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqLSKFEmvKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd06646     10 DYELIQRVGSGTYGDVYKARNLHTGELAAVK-IIKLE--PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLtsnYDIPEEWAQFYTA----EVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgMVR 232
Cdd:cd06646     87 YCGGGSLQDI---YHVTGPLSELQIAyvcrETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITAT-IAK 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd06646    163 RKSFIGTPYWMAPEVAAVEKNGG-YNQLCDIWAVGITAIELAELQPPMF 210
Rho_Binding pfam08912
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding ...
967-1034 1.25e-17

Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding domain-containing proteins (such as ROCK) to Rho, resulting in activation of the GTPase which in turn modulates the phosphorylation of various signalling proteins. This domain is within an amphipathic alpha-helical coiled-coil and interacts with Rho through predominantly hydrophobic interactions.


Pssm-ID: 462630 [Multi-domain]  Cd Length: 68  Bit Score: 78.47  E-value: 1.25e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  967 TVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKTD 1034
Cdd:pfam08912    1 TKDVENLAKEKEELNNKLKEQQEELEKAKEEEEEIEKLKASYEKQLNTERTLKTQAVNKLAEIMNRKD 68
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
81-294 1.32e-17

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 85.42  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGA--VQLVRHKVSQQVYAMKqlsKFEMVKRS--DSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd08216      3 LYEIGKCFKGGgvVHLAKHKPTNTLVAVK---KINLESDSkeDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGG---DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMvRC 233
Cdd:cd08216     80 LMAYGscrDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGK-RQ 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  234 DTAVGTPDYI-------SPEVLmSQGGTGyYGRECDWWSVGVFIYELLVGDTPF--------YSESLVGTYGKIMD 294
Cdd:cd08216    159 RVVHDFPKSSeknlpwlSPEVL-QQNLLG-YNEKSDIYSVGITACELANGVVPFsdmpatqmLLEKVRGTTPQLLD 232
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
84-274 1.56e-17

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 84.08  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFemvkrSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIPEEWAQfytaEVVLALDA------IHSLGFIHRDIKPDNMLL---DRNGHLKLADFGTCMKMDSTGMVRCD 234
Cdd:cd14065     76 EELLKSMDEQLPWSQ----RVSLAKDIasgmayLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKPD 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  235 -----TAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELL 274
Cdd:cd14065    152 rkkrlTVVGSPYWMAPEMLRGE----SYDEKVDVFSFGIVLCEII 192
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
78-274 1.66e-17

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 84.65  E-value: 1.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd07835      1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI-RLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MpggDL-----VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFgtcmkmdstGMVR 232
Cdd:cd07835     80 L---DLdlkkyMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF---------GLAR 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  233 cdtAVGTPD-----------YISPEVLMsqgGTGYYGRECDWWSVGVFIYELL 274
Cdd:cd07835    148 ---AFGVPVrtythevvtlwYRAPEILL---GSKHYSTPVDIWSVGCIFAEMV 194
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
84-341 2.13e-17

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 83.90  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWE---ERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14195     13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEierEVNILREIQHPNIITLHDIFENKTDVVLILELVSG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNG---HLKLADFGTCMKMDSTGMVRcdT 235
Cdd:cd14195     93 GELFDfLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIEAGNEFK--N 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  236 AVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdhkNSLTFPDDIEMSKNAKDLI 315
Cdd:cd14195    171 IFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGETKQETLTNI----SAVNYDFDEEYFSNTSELA 242
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  316 CAFLSSREVR--LGRTGVDEIKCHPFFK 341
Cdd:cd14195    243 KDFIRRLLVKdpKKRMTIAQSLEHSWIK 270
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
75-276 2.15e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 85.30  E-value: 2.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskFEMVKRSDSA---FfweeRDIM---AFSQSPWIVQLCCAFQDE 148
Cdd:cd07852      6 LRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKI--FDAFRNATDAqrtF----REIMflqELNDHPNIIKLLNVIRAE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 --KYLYLVMEFMPGgDL-VTLTSNydIPEE-WAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG---- 220
Cdd:cd07852     80 ndKDIYLVFEYMET-DLhAVIRAN--ILEDiHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGlars 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  221 -TCMKMDSTGMVRCDTaVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd07852    157 lSQLEEDDENPVLTDY-VATRWYRAPEILL---GSTRYTKGVDMWSVGCILGEMLLG 209
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
76-281 2.87e-17

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 83.04  E-value: 2.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKvsQQVYAMKQLSKFEMVKR-----SDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKY 150
Cdd:cd14019      1 NKYRIIEKIGEGTFSSVYKAEDK--LHDLYDRNKGRLVALKHiyptsSPSRILNELECLERLGGSNNVSGLITAFRNEDQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYDIPEewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR-NGHLKLADFGTCMKMDSTG 229
Cdd:cd14019     79 VVAVLPYIEHDDFRDFYRKMSLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNReTGKGVLVDFGLAQREEDRP 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  230 MVRCDTAvGTPDYISPEVLM---SQggtgyyGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd14019    157 EQRAPRA-GTRGFRAPEVLFkcpHQ------TTAIDIWSAGVILLSILSGRFPFF 204
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
78-284 3.18e-17

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 83.76  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAmkqlSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd14104      2 YMIAEELGRGQFGIVHRCVETSSKKTYM----AKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTL--TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL--DRNGHLKLADFGTCMKMDSTGMVRc 233
Cdd:cd14104     78 ISGVDIFERitTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKPGDKFR- 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  234 dTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14104    157 -LQYTSAEFYAPEVHQHE----SVSTATDMWSLGCLVYVLLSGINPFEAET 202
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
433-1076 4.04e-17

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 87.82  E-value: 4.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNAR-QEAEDNLRSLE-KEKVLLKHQRTQSVRKAGL 510
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLErSIAEKERELEDAEERLAKL 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  511 ETDRKRLLEnEVSSLKEQLAELKKK-----NQISHLSAEKNIhLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLE 585
Cdd:TIGR02169  328 EAEIDKLLA-EIEELEREIEEERKRrdkltEEYAELKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAQLENSRLVLEQDklslqtsLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLEKEKNKQEIDLSfKLKAVQQSLEQEEAEHKTTKARLADNNK-----INQSIEAKSETLKDMEH-------------- 726
Cdd:TIGR02169  479 DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQgvhgtVAQLGSVGERYATAIEVaagnrlnnvvvedd 557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  727 -------KLLEERSA---------KQQLENRLMQLEKENSVLD-------CDYKQAKHELQELRS--LKENLTEQVEVL- 780
Cdd:TIGR02169  558 avakeaiELLKRRKAgratflplnKMRDERRDLSILSEDGVIGfavdlveFDPKYEPAFKYVFGDtlVVEDIEAARRLMg 637
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  781 NVR-VQQE-------------TQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQ 846
Cdd:TIGR02169  638 KYRmVTLEgelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  847 LKE-MKDQLEAEQYFTKLyKTQIRELKEESDEKvklykdaQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYS 925
Cdd:TIGR02169  718 IGEiEKEIEQLEQEEEKL-KERLEELEEDLSSL-------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  926 DLEKEKIMKEL-EIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSL 1004
Cdd:TIGR02169  790 HSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1005 TVSYEKQI-QVEKTLKiqainklaevmkktdgrphqinntDIrrkEKEIRQLQLQLRTEKEKLNHSIIKYQRE 1076
Cdd:TIGR02169  870 LEELEAALrDLESRLG------------------------DL---KKERDELEAQLRELERKIEELEAQIEKK 915
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
84-274 4.11e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 83.08  E-value: 4.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKF-EMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14221      1 LGKGCFGQAIKVTHRETGEVMVMKELIRFdEETQRT----FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTLTSNYDIPEEWAQ--FYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM--------DSTGMVR 232
Cdd:cd14221     77 LRGIIKSMDSHYPWSQrvSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdektqpeGLRSLKK 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  233 CD-----TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL 274
Cdd:cd14221    157 PDrkkryTVVGNPYWMAPEMINGRS----YDEKVDVFSFGIVLCEII 199
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
83-341 4.57e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 82.59  E-value: 4.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVqLVRHKVS--QQVyAMKQLSK---FEMVKRSDS-------AFFWEerdIMAFSQSPWIVQLCCAFQDEKY 150
Cdd:cd14101      7 LLGKGGFGTV-YAGHRISdgLQV-AIKQISRnrvQQWSKLPGVnpvpnevALLQS---VGGGPGHRGVIRLLDWFEIPEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEF-MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFGTCMKMDS 227
Cdd:cd14101     82 FLLVLERpQHCQDLFDyITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATLKD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  228 TGMVRCDtavGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESlvgtygKIMdhKNSLTFPDDIem 307
Cdd:cd14101    162 SMYTDFD---GTRVYSPPEWILYH---QYHALPATVWSLGILLYDMVCGDIPFERDT------DIL--KAKPSFNKRV-- 225
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1207153289  308 SKNAKDLICAFLSSREVrlGRTGVDEIKCHPFFK 341
Cdd:cd14101    226 SNDCRSLIRSCLAYNPS--DRPSLEQILLHPWMM 257
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
543-1115 5.30e-17

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 87.00  E-value: 5.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  543 AEKNIHLERQLEEVSAKLQAELEESER----LKKAQIEAFRQSQQLELSLRELQERLAQLeNSRLVLEQDKLS------- 611
Cdd:TIGR04523   28 ANKQDTEEKQLEKKLKTIKNELKNKEKelknLDKNLNKDEEKINNSNNKIKILEQQIKDL-NDKLKKNKDKINklnsdls 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  612 ---------------LQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQE 676
Cdd:TIGR04523  107 kinseikndkeqknkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  677 IDLS------FKLKAVQQSLEQEEAEHKTTKARLAD----NNKINQSIEAKSETLKDMEHKLL-----------EERSAK 735
Cdd:TIGR04523  187 KNIDkiknklLKLELLLSNLKKKIQKNKSLESQISElkkqNNQLKDNIEKKQQEINEKTTEISntqtqlnqlkdEQNKIK 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  736 QQLENRLMQLEKEN---SVLDCDYKQAKHELQELRSLKENltEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSE 812
Cdd:TIGR04523  267 KQLSEKQKELEQNNkkiKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELNHllelkltLEKQNQELSKEREESEKQLKEMKDqlEAEQYFTKLY--KTQIRELKEESDEKVKLYKDAQQRIE 890
Cdd:TIGR04523  345 SQLKKELTN-------SESENSEKQRELEEKQNEIEKLKK--ENQSYKQEIKnlESQINDLESKIQNQEKLNQQKDEQIK 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  891 DLQEERDSLASQLEVSLTKadseqlaRITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDV 970
Cdd:TIGR04523  416 KLQQEKELLEKEIERLKET-------IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  971 ANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSyEKQIQVEKTLKIQAINKL-AEVMKKTDGRPHQINNTDIRRKE 1049
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLeDELNKDDFELKKENLEKEIDEKN 567
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289 1050 KEIRQLQLQ---LRTEKEKLNHSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:TIGR04523  568 KEIEELKQTqksLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
83-302 5.78e-17

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 82.44  E-value: 5.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAV-------QLVRHKVSQQvYAMKQLSKFEMVKRSDSAFFWEERdimafsqSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14061      1 VIGVGGFGKVyrgiwrgEEVAVKAARQ-DPDEDISVTLENVRQEARLFWMLR-------HPNIIALRGVCLQPPNLCLVM 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDIPEE----WAqfytAEVVLALDAIHSLG---FIHRDIKPDNMLLDR--------NGHLKLADFG 220
Cdd:cd14061     73 EYARGGALNRVLAGRKIPPHvlvdWA----IQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  221 TCMKMDSTgmVRCDTAvGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYGKIMdhkNSL 299
Cdd:cd14061    149 LAREWHKT--TRMSAA-GTYAWMAPEVIKSS----TFSKASDVWSYGVLLWELLTGEVPYKGiDGLAVAYGVAV---NKL 218

                   ...
gi 1207153289  300 TFP 302
Cdd:cd14061    219 TLP 221
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
430-898 6.75e-17

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 86.66  E-value: 6.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKcriaNQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAG 509
Cdd:PRK03918   308 ELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 LETD-----------RKRLLENEVSSLKEQLAELKK-----KNQISHLSAEKNI-----------HLERQLEEVSAKLQA 562
Cdd:PRK03918   384 LTPEklekeleelekAKEEIEEEISKITARIGELKKeikelKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKR 463
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  563 ELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLEnsrlVLEQDKlSLQTSLE---LEKRERNAgsETITDLQGRIYG 639
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE----LAEQLK-ELEEKLKkynLEELEKKA--EEYEKLKEKLIK 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  640 LEGELKHIKSSLSKAEvekrQLQEDLTTLEKEKnkqeidlsfklkavqQSLEQEEAEHKTTKARLAdnnkiNQSIEAKSE 719
Cdd:PRK03918   537 LKGEIKSLKKELEKLE----ELKKKLAELEKKL---------------DELEEELAELLKELEELG-----FESVEELEE 592
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  720 TLKDME---HKLLEERSAKQQLENRLMQLEKENSVLDcdykQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTlcQG 796
Cdd:PRK03918   593 RLKELEpfyNEYLELKDAEKELEREEKELKKLEEELD----KAFEELAETEKRLEELRKELEELEKKYSEEEYEEL--RE 666
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  797 DLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKqLKEMKDQLEAEQYFTKLYKTqirELKEESD 876
Cdd:PRK03918   667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKKYKA---LLKERAL 742
                          490       500
                   ....*....|....*....|..
gi 1207153289  877 EKVKlyKDAQQRIEDLQEERDS 898
Cdd:PRK03918   743 SKVG--EIASEIFEELTEGKYS 762
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
466-1102 7.86e-17

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 86.71  E-value: 7.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  466 LEKLSKDLEEEVNARQ----EAEDNLRSLEKEK------VLLKHQ-------RTQSVRKAGLeTDRKRLLENEVSSLKEQ 528
Cdd:pfam15921  222 ISKILRELDTEISYLKgrifPVEDQLEALKSESqnkielLLQQHQdrieqliSEHEVEITGL-TEKASSARSQANSIQSQ 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  529 LAELKK--KNQIS----HLSaeknihlerQLEEVSAKLQAELEESERLKKAQIEAFRQsqQLELSLRELQErlAQLENSR 602
Cdd:pfam15921  301 LEIIQEqaRNQNSmymrQLS---------DLESTVSQLRSELREAKRMYEDKIEELEK--QLVLANSELTE--ARTERDQ 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  603 LVLEQDKL--SLQTSL-ELEKRERNAGSETITD--LQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEI 677
Cdd:pfam15921  368 FSQESGNLddQLQKLLaDLHKREKELSLEKEQNkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  678 DLSFKLKAVQQSLEQEE---AEHKTTKARLadnNKINQSIEAKSETLKDMEHKLLEERSAKQQLENrlmQLEKENSVLDC 754
Cdd:pfam15921  448 RQMAAIQGKNESLEKVSsltAQLESTKEML---RKVVEELTAKKMTLESSERTVSDLTASLQEKER---AIEATNAEITK 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  755 DYKQAKHELQELRSLKenlTEQVEVLNVRVQQETQRKTLCQGD--LKVQRQEINSLrsseQQLKQELNHLLELKLTLEKQ 832
Cdd:pfam15921  522 LRSRVDLKLQELQHLK---NEGDHLRNVQTECEALKLQMAEKDkvIEILRQQIENM----TQLVGQHGRTAGAMQVEKAQ 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  833 NQELSKEREESEKQLKEMKDQLEAeqyftklyktQIRELKEE-SD---EKVKLYKDAQQR---IEDLQEERDSLASQLEV 905
Cdd:pfam15921  595 LEKEINDRRLELQEFKILKDKKDA----------KIRELEARvSDlelEKVKLVNAGSERlraVKDIKQERDQLLNEVKT 664
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  906 SLTKADSeqlaritVEEQYsdlekekimkeleikDMIARHRQDLAEKdgtinsLEESNRTLTVDVANLASEKEELNNKLK 985
Cdd:pfam15921  665 SRNELNS-------LSEDY---------------EVLKRNFRNKSEE------METTTNKLKMQLKSAQSELEQTRNTLK 716
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  986 HIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTlKIQAI-------NKLAEVMKKTDGRPHQINNTDIRRKEK---EIRQL 1055
Cdd:pfam15921  717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLeeamtnaNKEKHFLKEEKNKLSQELSTVATEKNKmagELEVL 795
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289 1056 QLQLRTEKEKLNH---SIIKYQREINDMQAMIAEESQ--VRLEMQMSLDSKD 1102
Cdd:pfam15921  796 RSQERRLKEKVANmevALDKASLQFAECQDIIQRQEQesVRLKLQHTLDVKE 847
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
547-894 8.27e-17

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 86.65  E-value: 8.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  547 IHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAG 626
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  627 SETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLE----------KEKNKQEIDLSFKLKAVQQSLEQEEAE 696
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  697 HKTTKARLADnnkINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEnsvldcdYKQAKHELQELRSLKENLTEQ 776
Cdd:TIGR02168  833 IAATERRLED---LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-------RASLEEALALLRSELEELSEE 902
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  777 VEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQE-LSKEREESEKQLKEMKDQLE 855
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKIK 982
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  856 A---------EQYftklyktqiRELKEESDEKVKLYKDAQQRIEDLQE 894
Cdd:TIGR02168  983 ElgpvnlaaiEEY---------EELKERYDFLTAQKEDLTEAKETLEE 1021
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
84-319 1.23e-16

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 81.44  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ-DEKYLYLVMEFMPGGD 162
Cdd:cd14164      8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVMEAAATDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG-HLKLADFGTCMKMDSTGMVRcDTAVGTPD 241
Cdd:cd14164     88 LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELS-TTFCGSRA 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  242 YISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFySESLVgtyGKIMDHKNSLTFPDDIEMSKNAKDLICAFL 319
Cdd:cd14164    167 YTPPEVIL---GTPYDPKKYDVWSLGVVLYVMVTGTMPF-DETNV---RRLRLQQRGVLYPSGVALEEPCRALIRTLL 237
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
76-280 1.28e-16

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 82.27  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEmvkRSDSAF---FWEERDIMAFSQSPWIVQL--CCAFQDEKY 150
Cdd:cd07843      5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL-KME---KEKEGFpitSLREINILLKLQHPNIVTVkeVVVGSNLDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGgDLVTLTSNYDIPeewaqFYTAEV-------VLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCM 223
Cdd:cd07843     81 IYMVMEYVEH-DLKSLMETMKQP-----FLQSEVkclmlqlLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAR 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  224 KMDS-----TGMVrcdtaVgTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07843    155 EYGSplkpyTQLV-----V-TLWYRAPELLL---GAKEYSTAIDMWSVGCIFAELLTKKPLF 207
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
78-294 1.43e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 82.79  E-value: 1.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAF------QDEKY 150
Cdd:cd07878     17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpFQSLIHARRTY--RELRLLKHMKHENVIGLLDVFtpatsiENFNE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMpGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS--T 228
Cdd:cd07878     95 VYLVTNLM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDemT 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  229 GMvrcdtaVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07878    174 GY------VATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIME 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
452-791 1.69e-16

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 85.89  E-value: 1.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  452 KEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAgletdrkRLLENEVSSLKEQLAE 531
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL-------EELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  532 LKKKnqISHLSAEKNihlerQLEEVSAKLQAELEESE-RLKKAQI-EAFRQSQQLELSLRELQERLAQLENSRLVLEQDK 609
Cdd:TIGR02169  756 VKSE--LKELEARIE-----ELEEDLHKLEEALNDLEaRLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  610 LSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNkqeiDLSFKLKAVQQS 689
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD----ELEAQLRELERK 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  690 LEQEEAEHKTTKARLADnnkINQSIEAKSETLKDMEHKLLEERSA-------------KQQLENRLMQLEKENSVLDCDY 756
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSE---LKAKLEALEEELSEIEDPKGEDEEIpeeelsledvqaeLQRVEEEIRALEPVNMLAIQEY 981
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1207153289  757 KQAKHELQELRSLKENLTEQVEVLNVRVQQETQRK 791
Cdd:TIGR02169  982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
75-274 1.89e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 81.46  E-value: 1.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAF--------- 145
Cdd:cd14048      5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVL--REVRALAKLDHPGIVRYFNAWlerppegwq 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 --QDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYT----AEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADF 219
Cdd:cd14048     83 ekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDF 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  220 GTCMKMD-----------STGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL 274
Cdd:cd14048    163 GLVTAMDqgepeqtvltpMPAYAKHTGQVGTRLYMSPEQIHGNQ----YSEKVDIFALGLILFELI 224
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
82-284 1.96e-16

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 81.00  E-value: 1.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKqLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEkyLYLVMEFMPGG 161
Cdd:cd14025      2 EKVGSGGFGQVYKVRHKHWKTWLAIK-CPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDSTGMVRCDTAV 237
Cdd:cd14025     79 SLEKLLASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGlaKWNGLSHSHDLSRDGLR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQG---GTGYygrecDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14025    159 GTIAYLPPERFKEKNrcpDTKH-----DVYSFAIVIWGILTQKKPFAGEN 203
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
71-302 1.97e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 81.24  E-value: 1.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   71 LQVKLDDFDRVKLIGRGAFG------------AVQLVRHK----VSQQVYAMKQLSK-FEMVKRsdsaffweerdimafs 133
Cdd:cd14145      1 LEIDFSELVLEEIIGIGGFGkvyraiwigdevAVKAARHDpdedISQTIENVRQEAKlFAMLKH---------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  134 qsPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHS---LGFIHRDIKPDNMLLDR 210
Cdd:cd14145     65 --PNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILE 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  211 --------NGHLKLADFGTCMKMDSTGMVrcdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd14145    143 kvengdlsNKILKITDFGLAREWHRTTKM---SAAGTYAWMAPEVIRSS----MFSKGSDVWSYGVLLWELLTGEVPFRG 215
                          250       260
                   ....*....|....*....|.
gi 1207153289  283 -ESLVGTYGKIMdhkNSLTFP 302
Cdd:cd14145    216 iDGLAVAYGVAM---NKLSLP 233
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
76-340 2.05e-16

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 80.72  E-value: 2.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAmkqlSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd14108      2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFA----AKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG--HLKLADFGTCMKMDSTGMVRC 233
Cdd:cd14108     78 ELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQYC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DtaVGTPDYISPEVLMSQGGTGYygreCDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKD 313
Cdd:cd14108    158 K--YGTPEFVAPEIVNQSPVSKV----TDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKG 231
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  314 LICAFLSSREVrlgRTGVDEIKCHPFF 340
Cdd:cd14108    232 FIIKVLVSDRL---RPDAEETLEHPWF 255
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
84-282 3.12e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 81.62  E-value: 3.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG-- 161
Cdd:cd06633     29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLGSas 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDIPEEWAQFyTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTgmvrcDTAVGTPD 241
Cdd:cd06633    109 DLLEVHKKPLQEVEIAAI-THGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPA-----NSFVGTPY 182
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  242 YISPEVLMSQgGTGYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd06633    183 WMAPEVILAM-DEGQYDGKVDIWSLGITCIELAERKPPLFN 222
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
407-1089 3.14e-16

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 84.64  E-value: 3.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  407 QLLTQQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKlskdlEEEVNARQEAEDN 486
Cdd:TIGR00618  197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK-----QQLLKQLRARIEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  487 LRSLEKEKVLLKHQRTQSVRKAGLETDRKRLLENEvSSLKEQLAELKkknqishlSAEKNIHLERQLEEVSAKLQAELEE 566
Cdd:TIGR00618  272 LRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE-QQAQRIHTELQ--------SKMRSRAKLLMKRAAHVKQQSSIEE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  567 SERLKK---AQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERnagsETITDLQGRIYGLege 643
Cdd:TIGR00618  343 QRRLLQtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL----DILQREQATIDTR--- 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  644 lkhiksslskaEVEKRQLQEDLTTLEKeknkqEIDLSFKLKAVQQSLEQEEAEHKTTKARLAdnNKINQSIEAKSETLKD 723
Cdd:TIGR00618  416 -----------TSAFRDLQGQLAHAKK-----QQELQQRYAELCAAAITCTAQCEKLEKIHL--QESAQSLKEREQQLQT 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  724 MEHKLLEERSAKQQLENRLmQLEKENSVLDCdyKQAKHELQELRSLKEnlteqVEVLNVRVQQETQRKTLCQGDLKVQRQ 803
Cdd:TIGR00618  478 KEQIHLQETRKKAVVLARL-LELQEEPCPLC--GSCIHPNPARQDIDN-----PGPLTRRMQRGEQTYAQLETSEEDVYH 549
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  804 EINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYK 883
Cdd:TIGR00618  550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  884 DA---QQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELE-IKDMIARHRQDLAEKDGTINSL 959
Cdd:TIGR00618  630 VRlhlQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQsEKEQLTYWKEMLAQCQTLLREL 709
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  960 EESNRTLTVDVANL----ASEKEELNNKLKHIQQKLEK-IKEEEKQMKSLTVSYEKQIQvEKTLKIQAINKLAEVMKKTD 1034
Cdd:TIGR00618  710 ETHIEEYDREFNEIenasSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHFNNNE-EVTAALQTGAELSHLAAEIQ 788
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289 1035 GRPHQINN--TDIRRKEKEIRQlqlQLRTEKEKLNHSIIKYQREINDMQAMIAEESQ 1089
Cdd:TIGR00618  789 FFNRLREEdtHLLKTLEAEIGQ---EIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
432-904 3.18e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 84.73  E-value: 3.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  432 NDLEKRLKKLEEKFKHEMQAKEELEnkcrianqRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQrtqsVRKAGLE 511
Cdd:PRK03918   269 EELKKEIEELEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER----IKELEEK 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  512 TDRKRLLENEVSSLKEQLAELKKknqiSHLSAEKNIHLERQLEEVSAKLqaELEESERLKKAQIEAFRQSQQLELSLREL 591
Cdd:PRK03918   337 EERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKI 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  592 QERLAQLENSRlvlEQDKLSLQtslELEKRERN---AGSETITDLQGRI---YGLegELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:PRK03918   411 TARIGELKKEI---KELKKAIE---ELKKAKGKcpvCGRELTEEHRKELleeYTA--ELKRIEKELKEIEEKERKLRKEL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLEKEKNKQEidlsfKLKAVQQSLEQ-EEAEHKTTKARLADnnkinqsIEAKSETLKDMEHKLLEERSAKQQLE---NR 741
Cdd:PRK03918   483 RELEKVLKKES-----ELIKLKELAEQlKELEEKLKKYNLEE-------LEKKAEEYEKLKEKLIKLKGEIKSLKkelEK 550
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  742 LMQLEKENSVLDCDYKQAKHELQEL-RSLKENLTEQVEVLNVRVQQetqrktlcqgdLKVQRQEINSLRSSEQQLKQELN 820
Cdd:PRK03918   551 LEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKE-----------LEPFYNEYLELKDAEKELEREEK 619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  821 HLLELKLTLEKQNQELS---KEREESEKQLKEMKDQLEAEQYftklyktqiRELKEESDEKVKLYKDAQQRIEDLQEERD 897
Cdd:PRK03918   620 ELKKLEEELDKAFEELAeteKRLEELRKELEELEKKYSEEEY---------EELREEYLELSRELAGLRAELEELEKRRE 690

                   ....*..
gi 1207153289  898 SLASQLE 904
Cdd:PRK03918   691 EIKKTLE 697
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
84-280 3.91e-16

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 81.00  E-value: 3.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfwEERDIMAFSQSPWIVQLCcAFQDE---KYLYLVMEFMPG 160
Cdd:cd13988      1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQM--REFEVLKKLNHKNIVKLF-AIEEElttRHKVLVMELCPC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTL----TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML--LDRNGH--LKLADFGTCMK-MDSTGMV 231
Cdd:cd13988     78 GSLYTVleepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARElEDDEQFV 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  232 rcdTAVGTPDYISPE-----VLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd13988    158 ---SLYGTEEYLHPDmyeraVLRKDHQKK-YGATVDLWSIGVTFYHAATGSLPF 207
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
76-300 3.98e-16

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 81.54  E-value: 3.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FE---MVKRSdsaffWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd07880     15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpFQselFAKRA-----YRELRLLKHMKHENVIGLLDVFTPDLSL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 ------YLVMEFMpGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd07880     90 drfhdfYLVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQT 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  226 DS--TGMVRcdtavgTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFyseslvgtygKIMDHKNSLT 300
Cdd:cd07880    169 DSemTGYVV------TRWYRAPEVILNW---MHYTQTVDIWSVGCIMAEMLTGKPLF----------KGHDHLDQLM 226
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
84-282 4.33e-16

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 80.01  E-value: 4.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKvSQQVYAMKQLskFEMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAFQDEKYLylVMEFMPGG 161
Cdd:cd14066      1 IGSGGFGTVYKGVLE-NGTVVAVKRL--NEMNCAASKKEFLTELEMLGRLRHPNLVRLlgYCLESDEKLL--VYEYMPNG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLV-TLTSNYDIPE-EWAQFY--TAEVVLALDAIHSLGF---IHRDIKPDNMLLDRNGHLKLADFGTCMKMD-STGMVRC 233
Cdd:cd14066     76 SLEdRLHCHKGSPPlPWPQRLkiAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIPpSESVSKT 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  234 DTAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd14066    156 SAVKGTIGYLAPEYIR----TGRVSTKSDVYSFGVVLLELLTGKPAVDE 200
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
82-340 4.70e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 79.96  E-value: 4.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVqlvrHKVSQQVYAMKQLSKFEMVKRS-DSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14190     10 EVLGGGKFGKV----HTCTEKRTGLKLAAKVINKQNSkDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRNGHL-KLADFGTCMKMDSTGMVRCDta 236
Cdd:cd14190     86 GELFerIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQvKIIDFGLARRYNPREKLKVN-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhKNSLTFPDDI--EMSKNAKDl 314
Cdd:cd14190    164 FGTPEFLSPEVVNYD----QVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVL--MGNWYFDEETfeHVSDEAKD- 236
                          250       260
                   ....*....|....*....|....*...
gi 1207153289  315 icaFLSSREVRLGRTGVDEIKC--HPFF 340
Cdd:cd14190    237 ---FVSNLIIKERSARMSATQClkHPWL 261
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
76-280 7.89e-16

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 80.85  E-value: 7.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMV---KRSdsaffWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd07877     17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpFQSIihaKRT-----YRELRLLKHMKHENVIGLLDVFTPARSL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 ------YLVMEFMpGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd07877     92 eefndvYLVTHLM-GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHT 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  226 DS--TGMvrcdtaVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07877    171 DDemTGY------VATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLTGRTLF 218
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
138-287 8.35e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 78.86  E-value: 8.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  138 IVQLCCAFQDEKYLYLVMEF-MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHL 214
Cdd:cd14100     67 VIRLLDWFERPDSFVLVLERpEPVQDLFDfITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGEL 146
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  215 KLADFGTCMKMDSTGMVRCDtavGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPF-YSESLVG 287
Cdd:cd14100    147 KLIDFGSGALLKDTVYTDFD---GTRVYSPPEWIRFH---RYHGRSAAVWSLGILLYDMVCGDIPFeHDEEIIR 214
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
84-283 8.35e-16

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 79.35  E-value: 8.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKvSQQVyAMKQLSKfEMVKRSDSAFFWEERDImAFSQSPWIVQL-----CCAFQDekYLYLVMEFM 158
Cdd:cd13979     11 LGSGGFGSVYKATYK-GETV-AVKIVRR-RRKNRASRQSFWAELNA-ARLRHENIVRVlaaetGTDFAS--LGLIIMEYC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL--VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMV--RCD 234
Cdd:cd13979     85 GNGTLqqLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVgtPRS 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  235 TAVGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd13979    165 HIGGTYTYRAPELLKGERVT----PKADIYSFGITLWQMLTRELPYAGL 209
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
81-280 8.71e-16

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 81.97  E-value: 8.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFG----AVqlVRHKVSQQVYAMKQLskfeMVKRSDSAFFweERDIMAFSQS----------PWIVQLCCAFQ 146
Cdd:COG5752     37 IKPLGQGGFGrtflAV--DEDIPSHPHCVIKQF----YFPEQGPSSF--QKAVELFRQEavrldelgkhPQIPELLAYFE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMPGGDLVT---LTSNYDIPEEWAqfYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNGHLKLADFGTC 222
Cdd:COG5752    109 QDQRLYLVQEFIEGQTLAQeleKKGVFSESQIWQ--LLKDLLPVLQFIHSRNVIHRDIKPANiIRRRSDGKLVLIDFGVA 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  223 MKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRecDWWSVGVFIYELLVGDTPF 280
Cdd:COG5752    187 KLLTITALLQTGTIIGTPEYMAPEQLR---GKVFPAS--DLYSLGVTCIYLLTGVSPF 239
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
81-294 9.54e-16

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 80.42  E-value: 9.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMV---KRSdsafFWEERDIMAFSQSPWIVQLCC--------AFQDe 148
Cdd:cd07851     20 LSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpFQSAihaKRT----YRELRLLKHMKHENVIGLLDVftpassleDFQD- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 kyLYLVMEFMpGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS- 227
Cdd:cd07851     95 --VYLVTHLM-GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDe 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  228 -TGMvrcdtaVGTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07851    172 mTGY------VATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMN 230
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
84-294 1.02e-15

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 80.31  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSK-FE---MVKRSdsaffWEERDIMAFSQSPWIVQLCCAF-QDEKYLYLVMEFM 158
Cdd:cd07856     18 VGMGAFGLVCSARDQLTGQNVAVKKIMKpFStpvLAKRT-----YRELKLLKHLRHENIISLSDIFiSPLEDIYFVTELL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 pGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS--TGMvrcdta 236
Cdd:cd07856     93 -GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPqmTGY------ 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  237 VGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07856    166 VSTRYYRAPEIMLTWQK---YDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITE 220
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
410-1067 1.05e-15

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 83.10  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  410 TQQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKE---ELENKCRIANQRLEKLSKDLEEEVNARQEAEDN 486
Cdd:pfam02463  351 REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeelELKSEEEKEAQLLLELARQLEDLLKEEKKEELE 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  487 LRSlEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHlERQLEEVSAKLQAELEE 566
Cdd:pfam02463  431 ILE-EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS-RQKLEERSQKESKARSG 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  567 SERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLqgriygLEGELKH 646
Cdd:pfam02463  509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPL------GARKLRL 582
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  647 IKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAV-------QQSLEQEEAEHKTTKARLADNNKINQSIEAKSE 719
Cdd:pfam02463  583 LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkvvegilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  720 TLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKtlcQGDLK 799
Cdd:pfam02463  663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI---NEELK 739
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  800 VQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEmkDQLEAeqyFTKLYKTQIRELKEESDEKV 879
Cdd:pfam02463  740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE--EEKEE---KLKAQEEELRALEEELKEEA 814
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  880 KLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMK----ELEIKDMIARHRQDLAEKDGT 955
Cdd:pfam02463  815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLqellLKEEELEEQKLKDELESKEEK 894
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  956 --------------INSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQ 1021
Cdd:pfam02463  895 ekeekkeleeesqkLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289 1022 AINKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLRTEKEKLN 1067
Cdd:pfam02463  975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
82-309 1.21e-15

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 80.15  E-value: 1.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYL------YLV 154
Cdd:cd07850      6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSRpFQNVTHAKRAY--RELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMpGGDLVTLTsNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVrcD 234
Cdd:cd07850     84 MELM-DANLCQVI-QMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMM--T 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  235 TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHknsLTFPDDIEMSK 309
Cdd:cd07850    160 PYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQ---LGTPSDEFMSR 227
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
84-280 1.33e-15

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 78.25  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQlSKFEMVKRSDSAFFWEERDIMAFSQsPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDNTEVAVKT-CRETLPPDLKRKFLQEARILKQYDH-PNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNydipeEWAQFYTAEVV-LALDAIHSLGF------IHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTA 236
Cdd:cd05041     81 LTFLRK-----KGARLTVKQLLqMCLDAAAGMEYleskncIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDGL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  237 VGTP-DYISPEVLmsqgGTGYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05041    156 KQIPiKWTAPEAL----NYGRYTSESDVWSFGILLWEIFsLGATPY 197
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
84-280 1.93e-15

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 78.81  E-value: 1.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKqLSKFEM-VKRSDSaffW-EERDIMAFSQSPWIVQLCCAFQDEKYL-----YLVME 156
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIK-SCRLELsVKNKDR---WcHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAME 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNydiPEEWAQFYTAEVVLALDAI-------HSLGFIHRDIKPDNMLL-DRNGHL--KLADFGTCMKMD 226
Cdd:cd14039     77 YCSGGDLRKLLNK---PENCCGLKESQVLSLLSDIgsgiqylHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLD 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  227 STGMvrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14039    154 QGSL--CTSFVGTLQYLAPELFENKS----YTVTVDYWSFGTMVFECIAGFRPF 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
653-981 2.55e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.03  E-value: 2.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  653 KAEVEKR--QLQEDLTTLE---KEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADN-NKINQSIEAKSETLKDMEH 726
Cdd:TIGR02168  174 RKETERKleRTRENLDRLEdilNELERQLKSLERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEELKEAEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  727 KLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEIN 806
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  807 SLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQ 886
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  887 QRIEDLQEERDSLASQLEVSLTKADSEQLARI------------TVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDG 954
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEELeeeleelqeeleRLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
                          330       340
                   ....*....|....*....|....*..
gi 1207153289  955 tINSLEESNRTLTVDVANLASEKEELN 981
Cdd:TIGR02168  494 -LERLQENLEGFSEGVKALLKNQSGLS 519
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
82-319 3.14e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 77.26  E-value: 3.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVqlvrHKVSQQVYAMKQLSKFEMVK-RSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14193     10 EILGGGRFGQV----HKCEEKSSGLKLAAKIIKARsQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLV--TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML-LDRNGH-LKLADFGTCMKMDSTGMVRCDta 236
Cdd:cd14193     86 GELFdrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVN-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  237 VGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLIC 316
Cdd:cd14193    164 FGTPEFLAPEVVNYE----FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFIS 239

                   ...
gi 1207153289  317 AFL 319
Cdd:cd14193    240 KLL 242
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
83-302 3.87e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 76.95  E-value: 3.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFG------------AVQLVRHKVSQQVYAMKqlskfEMVkRSDSAFFWeerdimaFSQSPWIVQLCCAFQDEKY 150
Cdd:cd14148      1 IIGVGGFGkvykglwrgeevAVKAARQDPDEDIAVTA-----ENV-RQEARLFW-------MLQHPNIIALRGVCLNPPH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGF---IHRDIKPDNML-LDR-------NGHLKLADF 219
Cdd:cd14148     68 LCLVMEYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILiLEPienddlsGKTLKITDF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  220 GTCMKMDSTGMVrcdTAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYGKIMdhkNS 298
Cdd:cd14148    148 GLAREWHKTTKM---SAAGTYAWMAPEVIR----LSLFSKSSDVWSFGVLLWELLTGEVPYREiDALAVAYGVAM---NK 217

                   ....
gi 1207153289  299 LTFP 302
Cdd:cd14148    218 LTLP 221
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
434-1115 3.99e-15

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 80.99  E-value: 3.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  434 LEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEkvllkhqrTQSVRKAGLETD 513
Cdd:pfam01576  382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE--------LESVSSLLNEAE 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  514 RKRL-LENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKKAqieafrqsqqLElslRELQ 592
Cdd:pfam01576  454 GKNIkLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRN----------VE---RQLS 520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  593 ERLAQLENSRLVLEQDKLSLQTSLELEKRernagsetitdLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEK 672
Cdd:pfam01576  521 TLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  673 NKQEIDLSfKLKAVQQSLEQEEAEHKTTKARLADN-NKINQSIEAKSETLKDMEHKLLEERSAKQQLE--NRLMQLEKEN 749
Cdd:pfam01576  590 DHQRQLVS-NLEKKQKKFDQMLAEEKAISARYAEErDRAEAEAREKETRALSLARALEEALEAKEELErtNKQLRAEMED 668
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  750 SVLDCDykQAKHELQELRSLKENLTEQVEVLNVRVQQ---ETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNhlLELK 826
Cdd:pfam01576  669 LVSSKD--DVGKNVHELERSKRALEQQVEEMKTQLEEledELQATEDAKLRLEVNMQALKAQFERDLQARDEQG--EEKR 744
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  827 LTLEKQNQELSKEREESEKQ--------------LKEMKDQLEA-----EQYFTKLYKTQ------IRELKE-------- 873
Cdd:pfam01576  745 RQLVKQVRELEAELEDERKQraqavaakkkleldLKELEAQIDAankgrEEAVKQLKKLQaqmkdlQRELEEarasrdei 824
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  874 -----ESDEKVK-LYKDAQQRIEDL----------QEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEkimkele 937
Cdd:pfam01576  825 laqskESEKKLKnLEAELLQLQEDLaaserarrqaQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEE------- 897
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  938 ikdmiarhrqdLAEKDGTINSLEESNRTLTVDVANLASEkeeLNNKLKHIQQKLEKIKEEEKQMKSLTV---SYEKQIQV 1014
Cdd:pfam01576  898 -----------LEEEQSNTELLNDRLRKSTLQVEQLTTE---LAAERSTSQKSESARQQLERQNKELKAklqEMEGTVKS 963
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1015 EKTLKIQAIN-KLAEVMKKTD--GRPHQINNTDIRRKEKEIRQLQLQLRTEK----------EKLNHSIIKYQREINDMQ 1081
Cdd:pfam01576  964 KFKSSIAALEaKIAQLEEQLEqeSRERQAANKLVRRTEKKLKEVLLQVEDERrhadqykdqaEKGNSRMKQLKRQLEEAE 1043
                          730       740       750
                   ....*....|....*....|....*....|....
gi 1207153289 1082 AMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:pfam01576 1044 EEASRANAARRKLQRELDDATESNESMNREVSTL 1077
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-280 4.72e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 76.53  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEF-MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLADFGTCMKMDSTG 229
Cdd:cd14102     81 IVMERpEPVKDLFDfITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKDTV 160
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  230 MVRCDtavGTPDYISPEVLMSQGgtgYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14102    161 YTDFD---GTRVYSPPEWIRYHR---YHGRSATVWSLGVLLYDMVCGDIPF 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
435-1116 6.21e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.49  E-value: 6.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  435 EKRLKKLEE-----KFKhemQAKEELENKCRIANQRLEKLskdleeevnarqeaEDNLRSLEKEKVLLKHQRTQSVR--- 506
Cdd:TIGR02168  155 EERRAIFEEaagisKYK---ERRKETERKLERTRENLDRL--------------EDILNELERQLKSLERQAEKAERyke 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  507 -KAGLETDRKRLLENEVSSLKEQLAELK---KKNQISHLSAEKNIH-LERQLEEVSAKLQAELEESERLKKAQIEAFRQS 581
Cdd:TIGR02168  218 lKAELRELELALLVLRLEELREELEELQeelKEAEEELEELTAELQeLEEKLEELRLEVSELEEEIEELQKELYALANEI 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  582 QQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKhiksslskaevEKRQL 661
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-----------ELEAE 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  662 QEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADnnkINQSIEAKSETLKDMEHKLLEERSAKQQlenr 741
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER---LEDRRERLQQEIEELLKKLEEAELKELQ---- 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  742 lMQLEKENSVLDcdykQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNH 821
Cdd:TIGR02168  440 -AELEELEEELE----ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  822 LLELKLTLEkQNQELSKEREESEK----------QLKEMKDQLEAEQYFTKLYKTQI--------------------REL 871
Cdd:TIGR02168  515 QSGLSGILG-VLSELISVDEGYEAaieaalggrlQAVVVENLNAAKKAIAFLKQNELgrvtflpldsikgteiqgndREI 593
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  872 KEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQ---------------YSDLEKEKIMKEL 936
Cdd:TIGR02168  594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvITGGSAKTNSSIL 673
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  937 EIKDMIARHRQDLAEkdgtinsLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQ--- 1013
Cdd:TIGR02168  674 ERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqle 746
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1014 --------------VEKTLKIQAINKLAEVMK-------------KTDGRPHQINNTDIRRKEKEIRQLQ---LQLRTEK 1063
Cdd:TIGR02168  747 eriaqlskelteleAEIEELEERLEEAEEELAeaeaeieeleaqiEQLKEELKALREALDELRAELTLLNeeaANLRERL 826
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1064 EKLNHSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSLS 1116
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
77-276 7.43e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 77.02  E-value: 7.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKqlsKFEMVKRSDSAFFWEERDIMAFSQ--SPWIVQL--CCAFQDEKYLY 152
Cdd:cd07845      8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALK---KVRMDNERDGIPISSLREITLLLNlrHPNIVELkeVVVGKHLDSIF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGgDLVTLTSNYDIPeewaqFYTAEV------VL-ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd07845     85 LVMEYCEQ-DLASLLDNMPTP-----FSESQVkclmlqLLrGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTY 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  226 DSTGMVRCDTAVgTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd07845    159 GLPAKPMTPKVV-TLWYRAPELLL---GCTTYTTAIDMWAVGCILAELLAH 205
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
84-285 7.61e-15

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 76.40  E-value: 7.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRsdsaFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd13991     14 IGRGSFGEVHRMEDKQTGFQCAVKKVR----LEV----FRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTL-TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG-HLKLADFGTCMKMDSTGMVRC----DTAV 237
Cdd:cd13991     86 GQLiKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDGLGKSlftgDYIP 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  238 GTPDYISPEVLMsqggtgyyGREC----DWWSVGVFIYELLVGDTP---FYSESL 285
Cdd:cd13991    166 GTETHMAPEVVL--------GKPCdakvDVWSSCCMMLHMLNGCHPwtqYYSGPL 212
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
548-1109 7.98e-15

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 80.11  E-value: 7.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  548 HLERQLEEVSAKLQAElEESERLKKAQ----IEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLqTSLELEKRER 623
Cdd:PRK03918   173 EIKRRIERLEKFIKRT-ENIEELIKEKekelEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-EELEKELESL 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  624 NagsetitdlqGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEidLSFKLKAVQQSLEQEEAEHKTTKAR 703
Cdd:PRK03918   251 E----------GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE--EYIKLSEFYEEYLDELREIEKRLSR 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  704 LadNNKINqSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDcDYKQAKHELQELRSLKENLTeqVEVLNVR 783
Cdd:PRK03918   319 L--EEEIN-GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLT--PEKLEKE 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  784 VQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELN-------------------HLLELKLTLEKQNQELSKEREESE 844
Cdd:PRK03918   393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIE 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  845 KQLKEMKDQ-------LEAEQYFTKLYKT--QIRELKEESDE--KVKLYKDAQQrIEDLQEERDSLASQ---LEVSLTKA 910
Cdd:PRK03918   473 EKERKLRKElrelekvLKKESELIKLKELaeQLKELEEKLKKynLEELEKKAEE-YEKLKEKLIKLKGEiksLKKELEKL 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  911 DSEQLARITVEEQYSDLEKEKimKELEiKDMIARHRQDLAEKDGTINSLEESNRTLtVDVANLASEKEELNNKLKHIQQK 990
Cdd:PRK03918   552 EELKKKLAELEKKLDELEEEL--AELL-KELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEE 627
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  991 lekikeeekqmksLTVSYEKQIQVEKTLKiQAINKLAEVMKKTDGRPHQinntDIRRKEKEIRQLQLQLRTEKEKLNHSI 1070
Cdd:PRK03918   628 -------------LDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYE----ELREEYLELSRELAGLRAELEELEKRR 689
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1207153289 1071 IKYQREINDMQAMIAEESQVRLEMQmSLDSKDSDIERLR 1109
Cdd:PRK03918   690 EEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELR 727
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
74-276 8.29e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 76.97  E-value: 8.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLskfeMVKRSDSAF---FWEERDIMAFSQSPWIVQLCCAFQDE-- 148
Cdd:cd07866      6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKI----LMHNEKDGFpitALREIKILKKLKHPNVVPLIDMAVERpd 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 ------KYLYLVMEFMpGGDLVTLTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG 220
Cdd:cd07866     82 kskrkrGSVYMVTPYM-DHDLSGLLENPSVKLTESQIkcYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFG 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  221 ----------------TCMKMDSTGMVRcdtavgTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd07866    161 larpydgpppnpkgggGGGTRKYTNLVV------TRWYRPPELLL---GERRYTTAVDIWGIGCVFAEMFTR 223
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
406-1107 9.24e-15

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 80.09  E-value: 9.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  406 DQLLTQQNK-CSEEDIIEDHglnHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRlEKLSKDLEEE-VNARQEA 483
Cdd:TIGR00606  224 DQITSKEAQlESSREIVKSY---ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQM-EKDNSELELKmEKVFQGT 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  484 EDNLRSLEkekvllkHQRTQSVRKAGLETDRkrlLENEVSSLKEQLAELKKK-----NQISHLSAEKNIH----LERQLE 554
Cdd:TIGR00606  300 DEQLNDLY-------HNHQRTVREKERELVD---CQRELEKLNKERRLLNQEktellVEQGRLQLQADRHqehiRARDSL 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  555 EVSAKLQAELEESERlkKAQIEafRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQ 634
Cdd:TIGR00606  370 IQSLATRLELDGFER--GPFSE--RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  635 GRIYGLE-GELKHIKSSLSKAEVEKR---QLQEDLTTLEKEKNKQEIDLSFK-LKAVQQSLEQEEAEHKTTKARLADNnk 709
Cdd:TIGR00606  446 KEILEKKqEELKFVIKELQQLEGSSDrilELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQE-- 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  710 iNQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDY---KQAKHELQELRSLKENLTEQVEVLNVRVQQ 786
Cdd:TIGR00606  524 -MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELAS 602
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  787 ETQRKTLCQGDLKvqrqeinslRSSEQQLKQELNhllelkLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKT 866
Cdd:TIGR00606  603 LEQNKNHINNELE---------SKEEQLSSYEDK------LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  867 QIRELKEES-------DEKVKLYKDAQQRIEDLQEERDSLASQLEVS------LTKADSEQLARITVEEQYSDLeKEKIM 933
Cdd:TIGR00606  668 FITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTeselkkKEKRRDEMLGLAPGRQSIIDL-KEKEI 746
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  934 KELEIKDM-----IARHRQDLAEKD---GTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLT 1005
Cdd:TIGR00606  747 PELRNKLQkvnrdIQRLKNDIEEQEtllGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ 826
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1006 VSYEKQIQVEKTLKIqaINKLAEVMKKTDGRPHQINNtdIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQREINDMQAMIA 1085
Cdd:TIGR00606  827 VNQEKQEKQHELDTV--VSKIELNRKLIQDQQEQIQH--LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
                          730       740
                   ....*....|....*....|..
gi 1207153289 1086 EESQVRLEMQMSLDSKDSDIER 1107
Cdd:TIGR00606  903 EIKDAKEQDSPLETFLEKDQQE 924
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
83-302 9.42e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 76.23  E-value: 9.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVSQ-QVYAMKQLSKFEMVKRSDSAffWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGG 161
Cdd:cd14146      1 IIGVGGFGKVYRATWKGQEvAVKAARQDPDEDIKATAESV--RQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DL----------VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGF---IHRDIKPDNMLLDR--------NGHLKLADFG 220
Cdd:cd14146     79 TLnralaaanaaPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEkiehddicNKTLKITDFG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  221 TCMKMDSTGMVrcdTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYGKIMdhkNSL 299
Cdd:cd14146    159 LAREWHRTTKM---SAAGTYAWMAPEVIKSS----LFSKGSDIWSYGVLLWELLTGEVPYRGiDGLAVAYGVAV---NKL 228

                   ...
gi 1207153289  300 TFP 302
Cdd:cd14146    229 TLP 231
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
431-1115 1.05e-14

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 79.63  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  431 SNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSlEKEKVLLKHQRTQSVRKAGL 510
Cdd:TIGR00618  189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  511 ETDRKRLLENEVSSLKEQLAELKKKNQIShLSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRE 590
Cdd:TIGR00618  268 RIEELRAQEAVLEETQERINRARKAAPLA-AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  591 LQERLAQLENSRLVLEQDKLSL-QTSLELEKRERnagsetITDLQGRIYGLEGELKHIKSSLSK-----AEVEKRQLQED 664
Cdd:TIGR00618  347 LQTLHSQEIHIRDAHEVATSIReISCQQHTLTQH------IHTLQQQKTTLTQKLQSLCKELDIlqreqATIDTRTSAFR 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  665 LTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLAdnNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLmQ 744
Cdd:TIGR00618  421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL--QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL-L 497
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  745 LEKENSVLDCdyKQAKHELQELRSLKEnlteqVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRsseqqlkqelnhlle 824
Cdd:TIGR00618  498 ELQEEPCPLC--GSCIHPNPARQDIDN-----PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER--------------- 555
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  825 lkltlekqnqelskereeseKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLE 904
Cdd:TIGR00618  556 --------------------KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  905 VSLTKADSEQ--------LARITVEEQYSDLEKEKIMKEL---EIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANL 973
Cdd:TIGR00618  616 ALLRKLQPEQdlqdvrlhLQQCSQELALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  974 ASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLaevMKKTDGRPHQINNTDIRRKEKEIr 1053
Cdd:TIGR00618  696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL---MHQARTVLKARTEAHFNNNEEVT- 771
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1054 qLQLQLRTEKEKLNHSIIKYQREINDMQAMIAE-ESQVRLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:TIGR00618  772 -AALQTGAELSHLAAEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
81-244 1.06e-14

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 75.96  E-value: 1.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMkqlsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMpG 160
Cdd:cd14016      5 VKKIGSGSFGEVYLGIDLKTGEEVAI----KIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLL-G 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTLTSNYDipeewaQFYTAEVVL--------ALDAIHSLGFIHRDIKPDNMLLDRNGHLK---LADFGTCMK-MDS- 227
Cdd:cd14016     80 PSLEDLFNKCG------RKFSLKTVLmladqmisRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKKyRDPr 153
                          170       180
                   ....*....|....*....|.
gi 1207153289  228 TG----MVRCDTAVGTPDYIS 244
Cdd:cd14016    154 TGkhipYREGKSLTGTARYAS 174
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
76-273 1.09e-14

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 76.41  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQlSKFEMVKRS-DSAFFWEERDIMAFSQSPWIVQLCCAFQDEK----Y 150
Cdd:cd07837      1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKK-TRLEMEEEGvPSTALREVSLLQMLSQSIYIVRLLDVEHVEEngkpL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGG-----DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN-GHLKLADFGTCMK 224
Cdd:cd07837     80 LYLVFEYLDTDlkkfiDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGRA 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  225 MdSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYEL 273
Cdd:cd07837    160 F-TIPIKSYTHEIVTLWYRAPEVLL---GSTHYSTPVDMWSVGCIFAEM 204
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
83-325 1.23e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.15  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAV----------QLVRHKVSQ-------QVYAMKQLSKFEMVKRSDsaFFWEErdimafsqspwivqlcCAF 145
Cdd:PTZ00036    73 IIGNGSFGVVyeaicidtseKVAIKKVLQdpqyknrELLIMKNLNHINIIFLKD--YYYTE----------------CFK 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEKYLYL--VMEFMPGGDLVTLT----SNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH-LKLAD 218
Cdd:PTZ00036   135 KNEKNIFLnvVMEFIPQTVHKYMKhyarNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCD 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  219 FGTCMKMdsTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNS 298
Cdd:PTZ00036   215 FGSAKNL--LAGQRSVSYICSRFYRAPELML---GATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGT 289
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  299 LTFPDDIEMSKNAKDLICAFLSSREVR 325
Cdd:PTZ00036   290 PTEDQLKEMNPNYADIKFPDVKPKDLK 316
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
115-340 1.25e-14

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 75.77  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  115 VKRSDSAFF-WEERDIMAFSQS---PWIVQLCCAFQDEKYLYLVMEFMPggdlVTLTSNYDIPEEWAQF-------YTA- 182
Cdd:cd13982     30 VKRLLPEFFdFADREVQLLRESdehPNVIRYFCTEKDRQFLYIALELCA----ASLQDLVESPRESKLFlrpglepVRLl 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  183 -EVVLALDAIHSLGFIHRDIKPDNMLLDR-----NGHLKLADFGTCMKMDS-TGMVRCDTAV-GTPDYISPEVLmSQGGT 254
Cdd:cd13982    106 rQIASGLAHLHSLNIVHRDLKPQNILISTpnahgNVRAMISDFGLCKKLDVgRSSFSRRSGVaGTSGWIAPEML-SGSTK 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  255 GYYGRECDWWSVG-VFIYELLVGDTPFYSeSLVGTYgKIMDHKNSLTFP-DDIEMSKNAKDLICAFLSSREvrLGRTGVD 332
Cdd:cd13982    185 RRQTRAVDIFSLGcVFYYVLSGGSHPFGD-KLEREA-NILKGKYSLDKLlSLGEHGPEAQDLIERMIDFDP--EKRPSAE 260

                   ....*...
gi 1207153289  333 EIKCHPFF 340
Cdd:cd13982    261 EVLNHPFF 268
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
434-1139 1.38e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 79.34  E-value: 1.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  434 LEKRLKKLEEKFKHEmqakEELENKCRIANQRLEKLSKDlEEEVNARQEAEDNLRSLEKeKVLLKhqrtqsvRKAGLETD 513
Cdd:TIGR02169  172 KEKALEELEEVEENI----ERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEG-YELLK-------EKEALERQ 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  514 RKRLlENEVSSLKEQLAELKKknQISHLSAEKNiHLERQLEEVSAKLQAELEESERLKKAQIEAF--------RQSQQLE 585
Cdd:TIGR02169  239 KEAI-ERQLASLEEELEKLTE--EISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiasleRSIAEKE 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLEKEKNKQEIDLSFKLKAVQQsLEQEEAEHKTTKARL-ADNNKINQSIEAKSETLKDMEHKLLE-------ERSAKQQ 737
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQR-LSEELADLNAAIAGIeAKINELEEEKEDKALEIKKQEWKLEQlaadlskYEQELYD 473
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  738 LENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQ-------QETQRKTLCQGDLKV---------- 800
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaQLGSVGERYATAIEVaagnrlnnvv 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  801 ---------------QRQ-------EINSLRSSEQQ-------------------------------------------- 814
Cdd:TIGR02169  554 veddavakeaiellkRRKagratflPLNKMRDERRDlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaar 633
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  815 ----------LKQEL--------NHLLELKLTLEKQNQELSKEREESEKqLKEMKDQLEAEQyftklykTQIRELKEESD 876
Cdd:TIGR02169  634 rlmgkyrmvtLEGELfeksgamtGGSRAPRGGILFSRSEPAELQRLRER-LEGLKRELSSLQ-------SELRRIENRLD 705
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  877 EKVKLYKDAQQRIEDLQEERDSLASQLEvsltkADSEQLARItvEEQYSDLEKEKIMKELEIKDMIARhrqdLAEKDGTI 956
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEE-----KLKERLEEL--EEDLSSLEQEIENVKSELKELEAR----IEELEEDL 774
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  957 NSLEESNRTLTVDVANlaSEKEELNNKLKHIQQKLEKIKEEEKQMKSLT--VSYEKQIQVEKTLKIQAINKLAEVMKKTD 1034
Cdd:TIGR02169  775 HKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLnrLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1035 GRPHQINNTDIRRKEKEIRQLQLQLRTEKEKLnhsiIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTS 1114
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          810       820
                   ....*....|....*....|....*
gi 1207153289 1115 LSihsldtTSISSIGNDLDSDEAYP 1139
Cdd:TIGR02169  929 LE------EELSEIEDPKGEDEEIP 947
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
430-987 1.62e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 79.34  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAG 509
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 LETDRKRLLENEVSSLKEQLAELKKKnqISHLSAEKNI------HLERQLEEVSAKLQAELEESERLKKAQieafrqsQQ 583
Cdd:TIGR02169  410 RLQEELQRLSEELADLNAAIAGIEAK--INELEEEKEDkaleikKQEWKLEQLAADLSKYEQELYDLKEEY-------DR 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  584 LELSLRELQERLAQLENSRLVLEQ---------------------------------------------------DKLSL 612
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEErvrggraveevlkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvveDDAVA 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  613 QTSLELEKReRNAGSETITDL---------------------------------------------------------QG 635
Cdd:TIGR02169  561 KEAIELLKR-RKAGRATFLPLnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgKY 639
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  636 RIYGLEGEL-------------KHIKSSLSKAEVEK-RQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTK 701
Cdd:TIGR02169  640 RMVTLEGELfeksgamtggsraPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  702 ARLADNNKINQSIEAKSETLKDMEHKLleeRSAKQQLENRLMQLEKENSVLDcDYKQAKHELQE-LRSLKENLTEQvEVL 780
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARIE-ELEEDLHKLEEaLNDLEARLSHS-RIP 794
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  781 NVRVQQETQRKTLCQGDLKVQ--RQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQ 858
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLReiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  859 YFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKAD--SEQLARI------TVEEQYSDLEKE 930
Cdd:TIGR02169  875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELSEIedpkgeDEEIPEEELSLE 954
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  931 KIMKELE--------IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHI 987
Cdd:TIGR02169  955 DVQAELQrveeeiraLEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
84-274 2.40e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 74.85  E-value: 2.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKF-EMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14154      1 LGKGFFGQAIKVTHRETGEVMVMKELIRFdEEAQRN----FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTLTSNYDIPEEWAQ--FYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-----------TCMKMDSTG 229
Cdd:cd14154     77 LKDVLKDMARPLPWAQrvRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGlarliveerlpSGNMSPSET 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  230 MVRCD--------TAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL 274
Cdd:cd14154    157 LRHLKspdrkkryTVVGNPYWMAPEMLNGRS----YDEKVDIFSFGIVLCEII 205
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
77-302 2.60e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 74.68  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKL---IGRGAFGAV-------QLVRHKVSQQVYAMKQLSKFEMVKrsdsaffwEERDIMAFSQSPWIVQLCCAFQ 146
Cdd:cd14147      1 SFQELRLeevIGIGGFGKVyrgswrgELVAVKAARQDPDEDISVTAESVR--------QEARLFAMLAHPNIIALKAVCL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHS---LGFIHRDIKPDNMLLDRNGH--------LK 215
Cdd:cd14147     73 EEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCealVPVIHRDLKSNNILLLQPIEnddmehktLK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  216 LADFGTCMKMDSTGMVrcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYS-ESLVGTYGKIMd 294
Cdd:cd14147    153 ITDFGLAREWHKTTQM---SAAGTYAWMAPEVIKAST----FSKGSDVWSFGVLLWELLTGEVPYRGiDCLAVAYGVAV- 224

                   ....*...
gi 1207153289  295 hkNSLTFP 302
Cdd:cd14147    225 --NKLTLP 230
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
405-979 2.66e-14

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 78.29  E-value: 2.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  405 EDQLLT---QQNKCSEE-----DIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEE 476
Cdd:pfam01576  137 EEDILLledQNSKLSKErklleERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGE 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  477 VNARQEAEDNLRSL-------------EKEKVLLKHQRTQSVRKAGLETDRKrlLENEVSSLKEQL---------AELKK 534
Cdd:pfam01576  217 STDLQEQIAELQAQiaelraqlakkeeELQAALARLEEETAQKNNALKKIRE--LEAQISELQEDLeseraarnkAEKQR 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  535 KNQISHLSAEKNiHLERQLEEVSAK-------------LQAELEESERLKKAQIEAFRQ--SQQLElslrELQERLAQLE 599
Cdd:pfam01576  295 RDLGEELEALKT-ELEDTLDTTAAQqelrskreqevteLKKALEEETRSHEAQLQEMRQkhTQALE----ELTEQLEQAK 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  600 NSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQE----------DLTTLE 669
Cdd:pfam01576  370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEklsklqseleSVSSLL 449
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  670 KEKNKQEIDLSFKLKAVQ------QSLEQEEaehktTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLM 743
Cdd:pfam01576  450 NEAEGKNIKLSKDVSSLEsqlqdtQELLQEE-----TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  744 QL-------EKENSVLDC---DYKQAKHELQELRSLKENLTEQVEVL---NVRVQQETQRKTLcqgDLKVQRQEINSLRS 810
Cdd:pfam01576  525 QLsdmkkklEEDAGTLEAleeGKKRLQRELEALTQQLEEKAAAYDKLektKNRLQQELDDLLV---DLDHQRQLVSNLEK 601
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  811 SEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIE 890
Cdd:pfam01576  602 KQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH 681
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  891 DLQEERDSLASQLEVslTKADSEQLaritvEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDgtiNSLEESNRTLTVDV 970
Cdd:pfam01576  682 ELERSKRALEQQVEE--MKTQLEEL-----EDELQATEDAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQV 751

                   ....*....
gi 1207153289  971 ANLASEKEE 979
Cdd:pfam01576  752 RELEAELED 760
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
76-281 3.68e-14

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 74.89  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLS--KFEMVKRsdsaffweERDIM-AFSQSPWIVQLCCAFQDE--KY 150
Cdd:cd14132     18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKpvKKKKIKR--------EIKILqNLRGGPNIVKLLDVVKDPqsKT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTL---TSNYDIpeewaQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH-LKLADFG-----T 221
Cdd:cd14132     90 PSLIFEYVNNTDFKTLyptLTDYDI-----RYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGlaefyH 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  222 CMKMDStgmVRcdtaVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd14132    165 PGQEYN---VR----VASRYYKGPELLV---DYQYYDYSLDMWSLGCMLASMIFRKEPFF 214
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
153-321 4.24e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 76.83  E-value: 4.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVT-----LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKM-- 225
Cdd:PTZ00283   116 LVLDYANAGDLRQeiksrAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFS-KMya 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 ----DSTGMVRCdtavGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLvgtyGKIMDHKNSLTF 301
Cdd:PTZ00283   195 atvsDDVGRTFC----GTPYYVAPEIWRRKP----YSKKADMFSLGVLLYELLTLKRPFDGENM----EEVMHKTLAGRY 262
                          170       180
                   ....*....|....*....|...
gi 1207153289  302 ---PDDIemSKNAKDLICAFLSS 321
Cdd:PTZ00283   263 dplPPSI--SPEMQEIVTALLSS 283
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
80-282 5.79e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 73.95  E-value: 5.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRH-----KVSQQVyAMKQLSKfeMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAFQDEKYLY 152
Cdd:cd05038      8 FIKQLGEGHFGSVELCRYdplgdNTGEQV-AVKSLQP--SGEEQHMSDFKREIEILRTLDHEYIVKYkgVCESPGRRSLR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLvtltSNYdIPEEWAQFYTAEVVL-------ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTcmkm 225
Cdd:cd05038     85 LIMEYLPSGSL----RDY-LQRHRDQIDLKRLLLfasqickGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL---- 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  226 dsTGMVRCDT---AVGTPD-----YISPEVLMsqggTGYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd05038    156 --AKVLPEDKeyyYVKEPGespifWYAPECLR----ESRFSSASDVWSFGVTLYELFTYGDPSQS 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
554-935 6.55e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 77.42  E-value: 6.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  554 EEVSAKLQAELEESERLKkaqieafRQSQQLELSLRELQERLAQLENSRLVLEQDKlslqtSLELEKRERNAgsetiTDL 633
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQ-----ALLKEKREYEG-----YEL 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  634 QGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARL-ADNNKINQ 712
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  713 SIEAKSETLKDMEhklleERSAKQQLENRLMQLEKENSvldcdykqaKHELQELRSLKENLTEQV-------EVLNVRVQ 785
Cdd:TIGR02169  309 SIAEKERELEDAE-----ERLAKLEAEIDKLLAEIEEL---------EREIEEERKRRDKLTEEYaelkeelEDLRAELE 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  786 QETQRktlcqgdLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYK 865
Cdd:TIGR02169  375 EVDKE-------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  866 TQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQL-EVSLTKADSEQLARITVEEQYSDLEKEKIMKE 935
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
84-283 6.89e-14

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 73.41  E-value: 6.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSkfemVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14110     11 INRGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 V-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTPDY 242
Cdd:cd14110     87 LyNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVET 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  243 ISPEVLMSQGGtgyyGRECDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd14110    167 MAPELLEGQGA----GPQTDIWAIGVTAFIMLSADYPVSSD 203
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
153-280 7.18e-14

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 72.91  E-value: 7.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLV-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD--STG 229
Cdd:cd14059     58 ILMEYCPYGQLYeVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSekSTK 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  230 MvrcdTAVGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14059    138 M----SFAGTVAWMAPEVIRNEPCS----EKVDIWSFGVVLWELLTGEIPY 180
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
436-1088 7.84e-14

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 76.68  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  436 KRLKKLEEKFKHEMQAKEE--LENKCRIANQRL---------EKLSKDLEEEVNARQE------AEDNLRSLEKEKVLLK 498
Cdd:pfam05483   88 EKIKKWKVSIEAELKQKENklQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDlikennATRHLCNLLKETCARS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  499 HQRTQSVRKAGLETDRKRL-LENEVSSLKEQLAELKKKNQISHLsaeknihlerqleEVSAKLQAELEESERLKKA-QIE 576
Cdd:pfam05483  168 AEKTKKYEYEREETRQVYMdLNNNIEKMILAFEELRVQAENARL-------------EMHFKLKEDHEKIQHLEEEyKKE 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  577 AFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQtslELEKRERnAGSETITDLQGRIYGLEGELKHIKSSLSKAEV 656
Cdd:pfam05483  235 INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN---QLEEKTK-LQDENLKELIEKKDHLTKELEDIKMSLQRSMS 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  657 EKRQLQEDLttlekeknkqeidlSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEhklleeRSAKQ 736
Cdd:pfam05483  311 TQKALEEDL--------------QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL------RTEQQ 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  737 QLENRLMQLEkensVLDCDYKQAKHELQELRSLKENltEQVEVLNVRVQQETQRKTLcqgDLKVQRQEI-NSLRSSEQQL 815
Cdd:pfam05483  371 RLEKNEDQLK----IITMELQKKSSELEEMTKFKNN--KEVELEELKKILAEDEKLL---DEKKQFEKIaEELKGKEQEL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  816 KQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEE 895
Cdd:pfam05483  442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  896 RDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLas 975
Cdd:pfam05483  522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL-- 599
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  976 eKEELNNKLKHIQQKLekikeeekqmksltvsyekqiQVEKTLKiqainklaevmKKTDGRPHQINNTDIRrkekeIRQL 1055
Cdd:pfam05483  600 -KKQIENKNKNIEELH---------------------QENKALK-----------KKGSAENKQLNAYEIK-----VNKL 641
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1207153289 1056 QLQLRTEKEKLNHSIIKYQREINDMQamIAEES 1088
Cdd:pfam05483  642 ELELASAKQKFEEIIDNYQKEIEDKK--ISEEK 672
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
78-282 8.15e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 74.32  E-value: 8.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06635     27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGG--DLVTLTSNyDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTcmkmdSTGMVRCDT 235
Cdd:cd06635    107 CLGSasDLLEVHKK-PLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGS-----ASIASPANS 180
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  236 AVGTPDYISPEVLMSQgGTGYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd06635    181 FVGTPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIELAERKPPLFN 226
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
430-976 1.00e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 76.62  E-value: 1.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEaednLRSLEKEKVLLKHQRTQSVRKAG 509
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIAETERERE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 LETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKnihLERQLEEVSAKlQAELEESERLKKAQIEAFR-QSQQLELSL 588
Cdd:PRK02224   276 ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA---VEARREELEDR-DEELRDRLEECRVAAQAHNeEAESLREDA 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  589 RELQERLAQLENSRLVLEQDklslqtsLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTL 668
Cdd:PRK02224   352 DDLEERAEELREEAAELESE-------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 ekekNKQEIDLSFKLKAVQQSLeqEEAEhkttkaRLADNNKINQSieakSETLKDMEH--KLLEERSAKQQLENRLMQLE 746
Cdd:PRK02224   425 ----REREAELEATLRTARERV--EEAE------ALLEAGKCPEC----GQPVEGSPHveTIEEDRERVEELEAELEDLE 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  747 KENSVLDCDYKQAKhELQELRSLKENLTEQVEVLNVRVqqETQRKTLCQgdlkvQRQEINSLRSSEQQLKQELNHLLELK 826
Cdd:PRK02224   489 EEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELI--AERRETIEE-----KRERAEELRERAAELEAEAEEKREAA 560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  827 LTLEKQNQELSKEREESEKQLKEMKDQLEA-EQYFTKL-----YKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLA 900
Cdd:PRK02224   561 AEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  901 SQLE---VSLTKADSEQ----LARIT-----VEEQYSDLEKEKIMKELEIKDM--IARHRQDLAEKDGTINSLEESNRTL 966
Cdd:PRK02224   641 AEFDearIEEAREDKERaeeyLEQVEekldeLREERDDLQAEIGAVENELEELeeLRERREALENRVEALEALYDEAEEL 720
                          570
                   ....*....|
gi 1207153289  967 TVDVANLASE 976
Cdd:PRK02224   721 ESMYGDLRAE 730
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
84-319 1.04e-13

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 73.05  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14197     17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGEI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VtltsNYDIPEEWAQFYTAEVVLALDAI-------HSLGFIHRDIKPDNMLLDRN---GHLKLADFGTCMKMDSTGMVRc 233
Cdd:cd14197     97 F----NQCVADREEAFKEKDVKRLMKQIlegvsflHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELR- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 dTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKD 313
Cdd:cd14197    172 -EIMGTPEYVAPEILSYEP----ISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAID 246

                   ....*.
gi 1207153289  314 LICAFL 319
Cdd:cd14197    247 FIKTLL 252
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
78-293 1.04e-13

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 74.17  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FE---MVKRSdsaffWEERDIMAFSQSPWIVQL------CCAFQD 147
Cdd:cd07879     17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpFQseiFAKRA-----YRELTLLKHMQHENVIGLldvftsAVSGDE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKYLYLVMEFMPGgDLVTLTSnYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd07879     92 FQDFYLVMPYMQT-DLQKIMG-HPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADA 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  228 --TGMVRcdtavgTPDYISPEVLMSQggtGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd07879    170 emTGYVV------TRWYRAPEVILNW---MHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIL 228
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
78-282 1.23e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 73.52  E-value: 1.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd06634     17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGG--DLVTLTSNyDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTcmkmdSTGMVRCDT 235
Cdd:cd06634     97 CLGSasDLLEVHKK-PLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGS-----ASIMAPANS 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  236 AVGTPDYISPEVLMSQgGTGYYGRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:cd06634    171 FVGTPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIELAERKPPLFN 216
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
81-315 2.03e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 73.17  E-value: 2.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMV---KRSD------SAFFWEE----RDIMAFSQSPwivqlccAFQ 146
Cdd:cd07858     10 IKPIGRGAYGIVCSAKNSETNEKVAIKKIANaFDNRidaKRTLreikllRHLDHENviaiKDIMPPPHRE-------AFN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DekyLYLVMEFMpGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd07858     83 D---VYIVYELM-DTDLhQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 DSTGMVRCDTAVgTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMdhkNSLTFPDDI 305
Cdd:cd07858    159 SEKGDFMTEYVV-TRWYRAPELLLNCSE---YTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLIT---ELLGSPSEE 231
                          250
                   ....*....|....
gi 1207153289  306 EM----SKNAKDLI 315
Cdd:cd07858    232 DLgfirNEKARRYI 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
471-985 2.12e-13

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 75.19  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  471 KDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQsvrkagletdrkrlLENEVSSLKEQLAELKKKNQISHLSAEKNiHLE 550
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEE--------------LEAELEELREELEKLEKLLQLLPLYQELE-ALE 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  551 RQLEEVSAKLQAELEESERLKkaqiEAFRQSQQLELSLRELQERLAQLENsrlvleqdklslQTSLELEKRERNAgSETI 630
Cdd:COG4717    139 AELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLE------------QLSLATEEELQDL-AEEL 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  631 TDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKI 710
Cdd:COG4717    202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  711 NQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEnsvldcdykQAKHELQELRSLKENLTEQVEVLNVRVQQetqr 790
Cdd:COG4717    282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE---------ELEELLAALGLPPDLSPEELLELLDRIEE---- 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  791 ktlcqgdlkvQRQEINSLRSSEQQLKQElnhllelkltlekqnqelskEREESEKQLKEMKDQLEAEQYFTKLyktqire 870
Cdd:COG4717    349 ----------LQELLREAEELEEELQLE--------------------ELEQEIAALLAEAGVEDEEELRAAL------- 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  871 lkeesdEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLaritvEEQYSDLEKEkimkELEIKDMIARHRQDLA 950
Cdd:COG4717    392 ------EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-----EEELEELEEE----LEELEEELEELREELA 456
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1207153289  951 EKDGTINSLEESNRtltvdVANLASEKEELNNKLK 985
Cdd:COG4717    457 ELEAELEQLEEDGE-----LAELLQELEELKAELR 486
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
82-292 2.56e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 72.87  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFW-----------EERDIMAFSQSPWIVQLCCAFQDEKY 150
Cdd:PTZ00024    15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlRELKIMNEIKHENIMGLVDVYVEGDF 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:PTZ00024    95 INLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPPY 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  231 VRCDTAVGTPD-------------YISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKI 292
Cdd:PTZ00024   175 SDTLSKDETMQrreemtskvvtlwYRAPELLM---GAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRI 246
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
75-281 3.58e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 71.77  E-value: 3.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLV 154
Cdd:PLN00009     1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKI-RLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMpggDLvTLTSNYDIPEEWA------QFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDR-NGHLKLADFGTCMKMds 227
Cdd:PLN00009    80 FEYL---DL-DLKKHMDSSPDFAknprliKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAF-- 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  228 tGM-VRCDT-AVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVfIYELLVGDTPFY 281
Cdd:PLN00009   154 -GIpVRTFThEVVTLWYRAPEILL---GSRHYSTPVDIWSVGC-IFAEMVNQKPLF 204
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
138-283 3.93e-13

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 71.02  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  138 IVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD--RNGHLK 215
Cdd:cd14112     62 VQRLIAAFKPSNFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVK 141
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  216 LADFGTCMKMDSTGMVrcdTAVGTPDYISPEVLmsQGGTGYYgRECDWWSVGVFIYELLVGDTPFYSE 283
Cdd:cd14112    142 LVDFGRAQKVSKLGKV---PVDGDTDWASPEFH--NPETPIT-VQSDIWGLGVLTFCLLSGFHPFTSE 203
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
84-280 4.88e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 71.53  E-value: 4.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSaffWE-ERDIMAFSQSPWIVQLCCAFQDEKYL------YLVME 156
Cdd:cd14038      2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRER---WClEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGGDLVTLTSNYD----IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD----RNGHlKLADFGTCMKMDST 228
Cdd:cd14038     79 YCQGGDLRKYLNQFEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgeqRLIH-KIIDLGYAKELDQG 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  229 GMvrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14038    158 SL--CTSFVGTLQYLAPELLEQQK----YTVTVDYWSFGTLAFECITGFRPF 203
PTZ00121 PTZ00121
MAEBL; Provisional
430-927 5.23e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 5.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIAN--QRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRK 507
Cdd:PTZ00121  1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  508 AGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKnihleRQLEEVSAKLQaELEESERLKKAQIEAfRQSQQLELS 587
Cdd:PTZ00121  1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-----KKADEAKKKAE-EAKKADEAKKKAEEA-KKAEEAKKK 1465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  588 L---RELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRiygleGELKHIKSSLSKAEvEKRQLQED 664
Cdd:PTZ00121  1466 AeeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK-----AEEAKKADEAKKAE-EAKKADEA 1539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  665 LTTLEKEK-----NKQEIDLSFKLKAVQQSLEQEE----AEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAK 735
Cdd:PTZ00121  1540 KKAEEKKKadelkKAEELKKAEEKKKAEEAKKAEEdknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  736 QQLEnrlmQLEKENSVLDCDYKQAKHELQELRSlKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQL 815
Cdd:PTZ00121  1620 IKAE----ELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  816 KQE------LNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEqyftklyKTQIRELKEESDEKVKLYKDAQQRI 889
Cdd:PTZ00121  1695 KKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-------KKKAEEAKKDEEEKKKIAHLKKEEE 1767
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1207153289  890 EDLQEERDSLASQLEVSLTKADSEQlaRITVEEQYSDL 927
Cdd:PTZ00121  1768 KKAEEIRKEKEAVIEEELDEEDEKR--RMEVDKKIKDI 1803
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
430-1132 6.44e-13

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 73.93  E-value: 6.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENK----CRIANQRLEKLSKDLEEEVNARQEAED----NLRSLEKEKVLLKHQR 501
Cdd:TIGR00606  406 EAKTAAQLCADLQSKERLKQEQADEIRDEkkglGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAER 485
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  502 TQSvrKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLE--RQLEEVSAKLQAELEESERLKK------- 572
Cdd:TIGR00606  486 ELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtrTQMEMLTKDKMDKDEQIRKIKSrhsdelt 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  573 AQIEAFRQSQQLELSLREL-------QERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRiYGLEGELK 645
Cdd:TIGR00606  564 SLLGYFPNKKQLEDWLHSKskeinqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLE 642
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  646 HIKSSLSKAEVEKRQL-------------------------QEDLTTlEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTT 700
Cdd:TIGR00606  643 RLKEEIEKSSKQRAMLagatavysqfitqltdenqsccpvcQRVFQT-EAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  701 KARladNNKINQSIEAKSETLKDMEHKLLEERSAKQQLeNRLMQLEKENsvLDCDYKQAKHELQELRSLKENLTEQVEVL 780
Cdd:TIGR00606  722 EKR---RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-NRDIQRLKND--IEEQETLLGTIMPEEESAKVCLTDVTIME 795
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  781 NVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYF 860
Cdd:TIGR00606  796 RFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  861 TKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKAdseqlaritvEEQYSDLEKEKIMKELEIKD 940
Cdd:TIGR00606  876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK----------EELISSKETSNKKAQDKVND 945
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  941 MiarhRQDLAEKDGTINSLEESNRTLTVDvaNLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKI 1020
Cdd:TIGR00606  946 I----KEKVKNIHGYMKDIENKIQDGKDD--YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQD 1019
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1021 QAI-----NKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLR----------TEKEKLNHSIIKYQREINDMQAMIA 1085
Cdd:TIGR00606 1020 NLTlrkreNELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDlikrnhvlalGRQKGYEKEIKHFKKELREPQFRDA 1099
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1086 EESQVRLEMQMS---LDSKDSDIERLRSQLTSLSIHSLDTTSISSIGNDL 1132
Cdd:TIGR00606 1100 EEKYREMMIVMRtteLVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDL 1149
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
78-281 6.81e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 70.92  E-value: 6.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd07839      2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVR-LDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MpGGDLVTL--TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMkmdSTGM-VRCD 234
Cdd:cd07839     81 C-DQDLKKYfdSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR---AFGIpVRCY 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  235 TA-VGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFY 281
Cdd:cd07839    157 SAeVVTLWYRPPDVLF---GAKLYSTSIDMWSAGCIFAELANAGRPLF 201
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
82-286 7.00e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 71.74  E-value: 7.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVkrSDSAFFWEERDIMAFSQSPWIVQ-----LCCAFQDEKYLYLVM 155
Cdd:cd07859      6 EVIGKGSYGVVCSAIDTHTGEKVAIKKINDvFEHV--SDATRILREIKLLRLLRHPDIVEikhimLPPSRREFKDIYVVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMpGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM--DSTGMVR 232
Cdd:cd07859     84 ELM-ESDLHQvIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAfnDTPTAIF 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  233 CDTAVGTPDYISPEVLMSqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLV 286
Cdd:cd07859    163 WTDYVATRWYRAPELCGS--FFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVV 214
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
84-280 8.37e-13

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 70.25  E-value: 8.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVqlVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCA-FQDEKYLYLVMEFMPGGD 162
Cdd:cd14064      1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQYVSGGS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTL--TSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLLDRNGHLKLADFGTC---MKMDSTGMVRcdt 235
Cdd:cd14064     79 LFSLlhEQKRVIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESrflQSLDEDNMTK--- 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  236 AVGTPDYISPEVLmSQggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14064    156 QPGNLRWMAPEVF-TQ--CTRYSIKADVFSYALCLWELLTGEIPF 197
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
426-944 1.08e-12

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 72.88  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  426 LNHTESNDLEKRLKKLEEKfkhemqakeelENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKhqrtqsv 505
Cdd:COG4717     68 LNLKELKELEEELKEAEEK-----------EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  506 rkagletdrkrlLENEVSSLKEQLAElkkknqishlsaeknihLERQLEEVSAKLQaeleeserlkkaqieafrQSQQLE 585
Cdd:COG4717    130 ------------LYQELEALEAELAE-----------------LPERLEELEERLE------------------ELRELE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAQLENsRLVLEQDKLSLQTSLELEKRErnagsETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:COG4717    163 EELEELEAELAELQE-ELEELLEQLSLATEEELQDLA-----EELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  666 TTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQL 745
Cdd:COG4717    237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  746 EKE--NSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKtlcqgdlkvqrqeinsLRSSEQQLKQELNHLL 823
Cdd:COG4717    317 EEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----------------LEELEQEIAALLAEAG 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  824 ELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTK--LYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLAS 901
Cdd:COG4717    381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEelLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  902 QLEvslTKADSEQLARItvEEQYSDLEKEkiMKELEIKDMIAR 944
Cdd:COG4717    461 ELE---QLEEDGELAEL--LQELEELKAE--LRELAEEWAALK 496
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
179-315 1.10e-12

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 70.51  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  179 FYtaEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH-LKLADFGTCMKMDSTGMVRCDTAvGTPDYISPEVLmsqGGTGYY 257
Cdd:cd13974    138 FY--DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQR-GSPAYISPDVL---SGKPYL 211
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  258 GRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIEMSKNAKDLI 315
Cdd:cd13974    212 GKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKI--KAAEYTIPEDGRVSENTVCLI 267
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
83-280 1.48e-12

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 69.57  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVQLVRHKVsqQVYAMKQLSK----------FEMVKRSDSA--------FFWEERDIMAFSQSPWIVQLCCA 144
Cdd:cd14000      1 LLGDGGFGSVYRASYKG--EPVAVKIFNKhtssnfanvpADTMLRHLRAtdamknfrLLRQELTVLSHLHHPSIVYLLGI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  145 fqDEKYLYLVMEFMPGGDLVTLTSNY-----DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNML---LDRNGHL-- 214
Cdd:cd14000     79 --GIHPLMLVLELAPLGSLDHLLQQDsrsfaSLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIii 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  215 KLADFGTCMKMDSTGMVrcdTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14000    157 KIADYGISRQCCRMGAK---GSEGTPGFRAPEIAR---GNVIYNEKVDVFSFGMLLYEILSGGAPM 216
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
75-283 1.51e-12

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 69.84  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSkFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQD--EKYLY 152
Cdd:cd14049      5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKIL-IKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEhvQLMLY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMP-------------GGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD-RNGHLKLA 217
Cdd:cd14049     84 IQMQLCElslwdwivernkrPCEEEFKSAPYTpVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIG 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  218 DFGTCMKM------DSTGMVRCD-----TAVGTPDYISPEVLmsQGgtGYYGRECDWWSVGVFIYELLVgdtPFYSE 283
Cdd:cd14049    164 DFGLACPDilqdgnDSTTMSRLNglthtSGVGTCLYAAPEQL--EG--SHYDFKSDMYSIGVILLELFQ---PFGTE 233
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
84-280 1.55e-12

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 69.45  E-value: 1.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKvSQQVYAMKQLSKfEMVKRSDSAFfWEERDIMAFSQSPWIVQL--CCAFQDEKYLylVMEFMPGG 161
Cdd:cd14664      1 IGRGGAGTVYKGVMP-NGTLVAVKRLKG-EGTQGGDHGF-QAEIQTLGMIRHRNIVRLrgYCSNPTTNLL--VYEYMPNG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTL---TSNYDIPEEWAQFYTaevvLALDAIHSLGF---------IHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG 229
Cdd:cd14664     76 SLGELlhsRPESQPPLDWETRQR----IALGSARGLAYlhhdcspliIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKD 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  230 mVRCDTAV-GTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14664    152 -SHVMSSVaGSYGYIAPEYAY----TGKVSEKSDVYSYGVVLLELITGKRPF 198
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
81-280 1.58e-12

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 69.63  E-value: 1.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQL---SKfEMVKRSdsaffweERDIMAFS--QSPWIVQLC--CAFQDE---KY 150
Cdd:cd13986      5 QRLLGEGGFSFVYLVEDLSTGRLYALKKIlchSK-EDVKEA-------MREIENYRlfNHPNILRLLdsQIVKEAggkKE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGG---DLVTLTS--NYDIPEEWAQFYTAEVVLALDAIHSL---GFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd13986     77 VYLLLPYYKRGslqDEIERRLvkGTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSM 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  223 MKMD------STGMVRCDTAV--GTPDYISPEVLMSQGGTGYYGReCDWWSVGVFIYELLVGDTPF 280
Cdd:cd13986    157 NPARieiegrREALALQDWAAehCTMPYRAPELFDVKSHCTIDEK-TDIWSLGCTLYALMYGESPF 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
421-952 2.17e-12

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 72.26  E-value: 2.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  421 IEDHGLNHTESNDLEKRLKKLEEKFKHEmQAKEELEnkcrIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQ 500
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLW-FAQRRLE----LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  501 RtqsvrkAGLETDRKRLLENEVSSLKEQLAELKKK-----NQIS--HLSAEKNIH-LERQLEEVSAKLQAELEESERLKK 572
Cdd:COG4913    332 I------RGNGGDRLEQLEREIERLERELEERERRrarleALLAalGLPLPASAEeFAALRAEAAALLEALEEELEALEE 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  573 AQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSL---------------EL------EKRERNAgsetit 631
Cdd:COG4913    406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaealgldeaelpfvgELievrpeEERWRGA------ 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  632 dlqgriygLEGELKHIKSSLSkaeVEKRQLQEDLTTLEKEKNKQEIDLsFKLKAVQQSLEQEEAEH---------KTTKA 702
Cdd:COG4913    480 --------IERVLGGFALTLL---VPPEHYAAALRWVNRLHLRGRLVY-ERVRTGLPDPERPRLDPdslagkldfKPHPF 547
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  703 RLADNNKINQ--------SIEA-----KSETL------------KDMEHKLLEER----SAKQQLEnrlmQLEKensvld 753
Cdd:COG4913    548 RAWLEAELGRrfdyvcvdSPEElrrhpRAITRagqvkgngtrheKDDRRRIRSRYvlgfDNRAKLA----ALEA------ 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  754 cdykqakhELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEIN--SLRSSEQQLKQELnhllelkltlek 831
Cdd:COG4913    618 --------ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAEL------------ 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  832 qnQELskerEESEKQLKEMKDQLEAeqyftklYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKAD 911
Cdd:COG4913    678 --ERL----DASSDDLAALEEQLEE-------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  912 SEQLARItvEEQYSDLEKEKIMKelEIKDMIARHRQDLAEK 952
Cdd:COG4913    745 LELRALL--EERFAAALGDAVER--ELRENLEERIDALRAR 781
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
418-904 2.91e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.61  E-value: 2.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVnarqeAEDNLRSLEKEKVLL 497
Cdd:PRK02224   240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL-----AEAGLDDADAEAVEA 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  498 kHQRTQSVRKAGLETD--RKRL----LENEVSSLKEQLAELKKKNQISHLSAEKnihLERQLEEVSAKLQAELEESERLK 571
Cdd:PRK02224   315 -RREELEDRDEELRDRleECRVaaqaHNEEAESLREDADDLEERAEELREEAAE---LESELEEAREAVEDRREEIEELE 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  572 KaQIEAFR--------QSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGS--------------ET 629
Cdd:PRK02224   391 E-EIEELRerfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvET 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  630 ITDLQGRIYGLEGELKHIKSSLSKAEvEKRQLQEDLTTLEKEKNKqeidLSFKLKAVQQSLEQEEAEHKTTKARLADNNK 709
Cdd:PRK02224   470 IEEDRERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIER----LEERREDLEELIAERRETIEEKRERAEELRE 544
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  710 INQSIEAKSETLKDMEHKLLEERSAKQQlenRLMQLEKENSVLDcDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQ 789
Cdd:PRK02224   545 RAAELEAEAEEKREAAAEAEEEAEEARE---EVAELNSKLAELK-ERIESLERIRTLLAAIADAEDEIERLREKREALAE 620
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  790 RKTLcqgdlkvQRQEINSLRSSEQQLKQELNhllelkltlekqnqelsKEREESEKQLKEmkdqlEAEQYFTKLyKTQIR 869
Cdd:PRK02224   621 LNDE-------RRERLAEKRERKRELEAEFD-----------------EARIEEAREDKE-----RAEEYLEQV-EEKLD 670
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1207153289  870 ELKEESDE---KVKLYKDAQQRIEDLQEERDSLASQLE 904
Cdd:PRK02224   671 ELREERDDlqaEIGAVENELEELEELRERREALENRVE 708
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
72-292 2.96e-12

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 68.91  E-value: 2.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYL 151
Cdd:cd05072      3 EIPRESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTMSVQA----FLEEANLMKTLQHDKLVRLYAVVTKEEPI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLVTLT-----SNYDIPEEWAqfYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:cd05072     78 YIITEYMAKGSLLDFLksdegGKVLLPKLID--FSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLvgdtpfyseslvgTYGKI 292
Cdd:cd05072    156 DNEYTAREGAKFPIKWTAPEAI----NFGSFTIKSDVWSFGILLYEIV-------------TYGKI 204
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
72-294 3.01e-12

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 68.91  E-value: 3.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQ--LVRHKVSQQVY---AMKQLskFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ 146
Cdd:cd05032      2 ELPREKITLIRELGQGSFGMVYegLAKGVVKGEPEtrvAIKTV--NENASMRERIEFLNEASVMKEFNCHHVVRLLGVVS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMPGGDLVT----------LTSNYDIPE-----EWAqfytAEVVLALDAIHSLGFIHRDIKPDNMLLDRN 211
Cdd:cd05032     80 TGQPTLVVMELMAKGDLKSylrsrrpeaeNNPGLGPPTlqkfiQMA----AEIADGMAYLAAKKFVHRDLAARNCMVAED 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  212 GHLKLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMSqggtGYYGRECDWWSVGVFIYELL-VGDTPF--YSESLVG 287
Cdd:cd05032    156 LTVKIGDFGMTRDIYETDYYRKGGKGLLPvRWMAPESLKD----GVFTTKSDVWSFGVVLWEMAtLAEQPYqgLSNEEVL 231
                          250
                   ....*....|
gi 1207153289  288 TY---GKIMD 294
Cdd:cd05032    232 KFvidGGHLD 241
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
75-275 3.39e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 69.06  E-value: 3.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQL---------CCAF 145
Cdd:cd07864      6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLNHRSVVNLkeivtdkqdALDF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEK-YLYLVMEFMpGGDLVTLTSN--YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd07864     85 KKDKgAFYLVFEYM-DHDLMGLLESglVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLA 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  223 MKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLV 275
Cdd:cd07864    164 RLYNSEESRPYTNKVITLWYRPPELLL---GEERYGPAIDVWSCGCILGELFT 213
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
151-321 3.64e-12

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 68.16  E-value: 3.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH---LKLADFGTCMKMD 226
Cdd:cd14012     79 VYLLTEYAPGGSLSELLDSVGsVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLL 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLmsqGGTGYYGRECDWWSVGVFIYELLVG-DTPFYSESLVGtygkimdhknsltFPDDI 305
Cdd:cd14012    159 DMCSRGSLDEFKQTYWLPPELA---QGSKSPTRKTDVWDLGLLFLQMLFGlDVLEKYTSPNP-------------VLVSL 222
                          170
                   ....*....|....*.
gi 1207153289  306 EMSKNAKDLICAFLSS 321
Cdd:cd14012    223 DLSASLQDFLSKCLSL 238
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
81-280 4.29e-12

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 67.86  E-value: 4.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05059      9 LKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSM---SEDDFI-EEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDI-PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFgtcmkmdstGMVR------ 232
Cdd:cd05059     84 GCLLNyLRERRGKfQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDF---------GLARyvldde 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  233 --CDTAVGTP-DYISPEVLMSqggtGYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05059    155 ytSSVGTKFPvKWSPPEVFMY----SKFSSKSDVWSFGVLMWEVFSeGKMPY 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
78-273 6.10e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 68.55  E-value: 6.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAFQDEKY----- 150
Cdd:cd07865     14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKV-LMENEKEGFPITALREIKILQLLKHENVVNLieICRTKATPYnrykg 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 -LYLVMEFMPGgDLVTLTSNYDIpeewaQFYTAEV-------VLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-- 220
Cdd:cd07865     93 sIYLVFEFCEH-DLAGLLSNKNV-----KFTLSEIkkvmkmlLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGla 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  221 -TCMKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYEL 273
Cdd:cd07865    167 rAFSLAKNSQPNRYTNRVVTLWYRPPELLL---GERDYGPPIDMWGAGCIMAEM 217
pknD PRK13184
serine/threonine-protein kinase PknD;
78-305 6.24e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 70.57  E-value: 6.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQ----LSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:PRK13184     4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKiredLSENPLLKKR----FLREAKIAADLIHPGIVPVYSICSDGDPVYY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNY----DIPEEWAQ----------FYTaeVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADF 219
Cdd:PRK13184    80 TMPYIEGYTLKSLLKSVwqkeSLSKELAEktsvgaflsiFHK--ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  220 GTC----MKMD-------------STGMVRCDTAVGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPFYS 282
Cdd:PRK13184   158 GAAifkkLEEEdlldidvdernicYSSMTIPGKIVGTPDYMAPERLLGVPAS----ESTDIYALGVILYQMLTLSFPYRR 233
                          250       260
                   ....*....|....*....|...
gi 1207153289  283 ESlvgtyGKIMDHKNSLTFPDDI 305
Cdd:PRK13184   234 KK-----GRKISYRDVILSPIEV 251
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
81-280 6.51e-12

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 68.02  E-value: 6.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd14026      2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTLTSNYDI-PE-EWAQFYTA--EVVLALDAIHSLG--FIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRC 233
Cdd:cd14026     82 GSLNELLHEKDIyPDvAWPLRLRIlyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGlSKWRQLSISQSRS 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 DTAV---GTPDYISPEVlMSQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14026    162 SKSApegGTIIYMPPEE-YEPSQKRRASVKHDIYSYAIIMWEVLSRKIPF 210
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
75-295 6.77e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 68.92  E-value: 6.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYL-- 151
Cdd:cd07875     23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRpFQNQTHAKRAY--RELVLMKCVNHKNIIGLLNVFTPQKSLee 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 ----YLVMEFMPGGDLVTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd07875    101 fqdvYIVMELMDANLCQVIQMELD--HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT 178
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  228 TGMVrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH 295
Cdd:cd07875    179 SFMM--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQ 240
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
75-295 7.09e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 68.96  E-value: 7.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYL-- 151
Cdd:cd07874     16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRpFQNQTHAKRAY--RELVLMKCVNHKNIISLLNVFTPQKSLee 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 ----YLVMEFMPGGDLVTLTSNYDipEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd07874     94 fqdvYLVMELMDANLCQVIQMELD--HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  228 TGMVrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMDH 295
Cdd:cd07874    172 SFMM--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQ 233
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
82-280 1.03e-11

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 66.95  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAV--QLVRHKVSQQVYAMKQLSKFEMVKRsdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd05085      2 ELLGKGNFGEVykGTLKDKTPVAVKTCKEDLPQELKIK-----FLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLtsnydIPEEWAQFYTAEVV-LALDAIHSLGF------IHRDIKPDNMLLDRNGHLKLADFGTCMKMDStGMVR 232
Cdd:cd05085     77 GGDFLSF-----LRKKKDELKTKQLVkFSLDAAAGMAYleskncIHRDLAARNCLVGENNALKISDFGMSRQEDD-GVYS 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTP-DYISPEVLmsqgGTGYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05085    151 SSGLKQIPiKWTAPEAL----NYGRYSSESDVWSFGILLWETFsLGVCPY 196
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
74-286 1.05e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 67.34  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd07871      3 KLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAI-REVSLLKNLKHANIVTLHDIIHTERCLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPG---------GDLVTLTSnydipeewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmK 224
Cdd:cd07871     81 VFEYLDSdlkqyldncGNLMSMHN--------VKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA-R 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  225 MDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGdTPFYSESLV 286
Cdd:cd07871    152 AKSVPTKTYSNEVVTLWYRPPDVLL---GSTEYSTPIDMWGVGCILYEMATG-RPMFPGSTV 209
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
84-303 1.09e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 66.96  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKqLSKFEMVKRSDSaffweerDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd13995     12 IPRGAFGKVYLAQDTKTKKRMACK-LIPVEQFKPSDV-------EIQACFRHENIAELYGALLWEETVHLFMEAGEGGSV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 V-TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLdRNGHLKLADFGTCMKMDSTGMVRCDTAvGTPDY 242
Cdd:cd13995     84 LeKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPKDLR-GTEIY 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  243 ISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPF---YSESLVGTYGKIMdHKNSLTFPD 303
Cdd:cd13995    162 MSPEVILCRG----HNTKADIYSLGATIIHMQTGSPPWvrrYPRSAYPSYLYII-HKQAPPLED 220
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
77-294 1.13e-11

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 68.23  E-value: 1.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfweeRDImafsqspwivQLCCAFQDEKYL---- 151
Cdd:cd07853      1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNvFQNLVSCKRVF----REL----------KMLCFFKHDNVLsald 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 -------------YLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLAD 218
Cdd:cd07853     67 ilqpphidpfeeiYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICD 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  219 FGTCMKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07853    147 FGLARVEEPDESKHMTQEVVTQYYRAPEILM---GSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITD 219
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
407-907 1.15e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 69.76  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  407 QLLTQQNKCSEEDIIEDH-----GLNH------TESNDLEKRLKKLEEKFKHE----MQAKEELENKcrianqrLEKLSK 471
Cdd:pfam15921  259 ELLLQQHQDRIEQLISEHeveitGLTEkassarSQANSIQSQLEIIQEQARNQnsmyMRQLSDLEST-------VSQLRS 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  472 DLEEevnARQEAEDNLRSLEKEKVL----LKHQRTQ----SVRKAGLETDRKRLL------ENEVSSLKEQLAELKKKNQ 537
Cdd:pfam15921  332 ELRE---AKRMYEDKIEELEKQLVLanseLTEARTErdqfSQESGNLDDQLQKLLadlhkrEKELSLEKEQNKRLWDRDT 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  538 -----ISHLSAE---KNIHLER--------------QLEEVSAKLQAELEESERLKK--AQIEAFRQsqQLELSLRELQE 593
Cdd:pfam15921  409 gnsitIDHLRRElddRNMEVQRleallkamksecqgQMERQMAAIQGKNESLEKVSSltAQLESTKE--MLRKVVEELTA 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  594 RLAQLENSrlvlEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSS---------------LSKAEVEK 658
Cdd:pfam15921  487 KKMTLESS----ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrnvqtecealkLQMAEKDK 562
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  659 -----RQLQEDLTTL------------------EKEKNKQEIDLS-FKLKAVQQSLEQEEAEHKTTKARLADNNKINQSI 714
Cdd:pfam15921  563 vieilRQQIENMTQLvgqhgrtagamqvekaqlEKEINDRRLELQeFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS 642
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  715 EaKSETLKDMEH---KLLEERSA---------------KQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLtEQ 776
Cdd:pfam15921  643 E-RLRAVKDIKQerdQLLNEVKTsrnelnslsedyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM-EG 720
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  777 VEVLNVRVQQETQRKtlcqgdLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEa 856
Cdd:pfam15921  721 SDGHAMKVAMGMQKQ------ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE- 793
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  857 eqyftkLYKTQIRELKEE-SDEKVKLYKDAQQRIE--DL--QEERDSLASQLEVSL 907
Cdd:pfam15921  794 ------VLRSQERRLKEKvANMEVALDKASLQFAEcqDIiqRQEQESVRLKLQHTL 843
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
418-781 1.23e-11

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 69.66  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLE-----K 492
Cdd:TIGR04523  373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsvK 452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  493 EKVLLKHQRTQSVRKAGLETdRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKK 572
Cdd:TIGR04523  453 ELIIKNLDNTRESLETQLKV-LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  573 AQIEAFRQSQQLELSLRELQERLaqlenSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLS 652
Cdd:TIGR04523  532 EKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  653 KAEVEKRQLQEDLTTLEKEKNKQEI---DLSFKLKAVQQSLEQEEAEHKTTKARLAD-NNKINQSIEAKSETLKDMEhKL 728
Cdd:TIGR04523  607 EKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKETIKEIRNKWPEiIKKIKESKTKIDDIIELMK-DW 685
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  729 LEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLN 781
Cdd:TIGR04523  686 LKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
81-279 1.51e-11

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 66.51  E-value: 1.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKqlskFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMpG 160
Cdd:cd14017      5 VKKIGGGGFGEIYKVRDVVDGEEVAMK----VESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL-G 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTLTSNYdiPEewaQFYTAEVVL--------ALDAIHSLGFIHRDIKPDNMLLDRNGH----LKLADFGTCMK-MDS 227
Cdd:cd14017     80 PNLAELRRSQ--PR---GKFSVSTTLrlgiqilkAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQyTNK 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  228 TGMV-RCDTAV----GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTP 279
Cdd:cd14017    155 DGEVeRPPRNAagfrGTVRYASVNAHRNKE----QGRRDDLWSWFYMLIEFVTGQLP 207
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
87-280 1.63e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 66.37  E-value: 1.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   87 GAFGAVQLVRHKvSQQVYAMKQLSKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTL 166
Cdd:cd14027      4 GGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHNEALL-EEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  167 TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--------------TCMKMDSTGMvr 232
Cdd:cd14027     82 LKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskltkeeHNEQREVDGT-- 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  233 CDTAVGTPDYISPEVLMSQGGTGyyGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14027    160 AKKNAGTLYYMAPEHLNDVNAKP--TEKSDVYSFAIVLWAIFANKEPY 205
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
75-294 1.65e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 67.75  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   75 LDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSK-FEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYL-- 151
Cdd:cd07876     20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRpFQNQTHAKRAY--RELVLLKCVNHKNIISLLNVFTPQKSLee 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 ----YLVMEFMPGGdlVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd07876     98 fqdvYLVMELMDAN--LCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACT 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  228 TGMVrcDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07876    176 NFMM--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIE 236
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
71-280 1.90e-11

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 67.20  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   71 LQVKLDDF--DR---VKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEmvKRSDSAFFweERDIMAFSQS------PWIV 139
Cdd:cd14134      2 LIYKPGDLltNRykiLRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVE--KYREAAKI--EIDVLETLAEkdpngkSHCV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  140 QLCCAFQDEKYLYLVMEFM-PggdlvtltSNYDI---------PEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLD 209
Cdd:cd14134     78 QLRDWFDYRGHMCIVFELLgP--------SLYDFlkknnygpfPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  210 -------------------RNGHLKLADFGTCM--KMDSTgmvrcdTAVGTPDYISPEVLMsqgGTGYYgRECDWWSVGV 268
Cdd:cd14134    150 dsdyvkvynpkkkrqirvpKSTDIKLIDFGSATfdDEYHS------SIVSTRHYRAPEVIL---GLGWS-YPCDVWSIGC 219
                          250
                   ....*....|..
gi 1207153289  269 FIYELLVGDTPF 280
Cdd:cd14134    220 ILVELYTGELLF 231
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
81-294 1.97e-11

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 66.14  E-value: 1.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFG-AVQLVRHKVSQQV-------------YAMKQLSKFEMVKRSDSAffweerdimafsQSPWIVQLCCAFQ 146
Cdd:cd14133      4 LEVLGKGTFGqVVKCYDLLTGEEValkiiknnkdyldQSLDEIRLLELLNKKDKA------------DKYHIVRLKDVFY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEfMPGGDLV-----TLTSNYDIPEewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNG--HLKLADF 219
Cdd:cd14133     72 FKNHLCIVFE-LLSQNLYeflkqNKFQYLSLPR--IRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDF 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  220 GTCmkmdSTGMVRCDTAVGTPDYISPEVLMsqggtGY-YGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd14133    149 GSS----CFLTQRLYSYIQSRYYRAPEVIL-----GLpYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIG 215
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
85-280 1.97e-11

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 65.75  E-value: 1.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   85 GRGAFGAVQLVrHKVSQ-QVYAMKQLSKFEmvkrsdsaffwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14060      2 GGGSFGSVYRA-IWVSQdKEVAVKKLLKIE-----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDIPE-EWAQFYT--AEVVLALDAIHS---LGFIHRDIKPDNMLLDRNGHLKLADFGTC-MKMDSTGMvrcdTA 236
Cdd:cd14060     70 FDYLNSNESEEmDMDQIMTwaTDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASrFHSHTTHM----SL 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  237 VGTPDYISPEVLMSQGGTgyygRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14060    146 VGTFPWMAPEVIQSLPVS----ETCDTYSYGVVLWEMLTREVPF 185
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
172-311 2.73e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 66.21  E-value: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  172 IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVgTPDYISPEVLMSQ 251
Cdd:cd07862    107 VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA-RIYSFQMALTSVVV-TLWYRAPEVLLQS 184
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  252 GgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD---HKNSLTFPDDIEMSKNA 311
Cdd:cd07862    185 S----YATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDvigLPGEEDWPRDVALPRQA 243
PTZ00121 PTZ00121
MAEBL; Provisional
393-958 2.98e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 2.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  393 NQLPFVGFTYFREDQLLTQQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFK-HEMQAKEELENKCRIANQRLEKLSK 471
Cdd:PTZ00121  1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAKK 1329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  472 DLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQishlsaeknihLER 551
Cdd:PTZ00121  1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-----------AKK 1398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  552 QLEEVSAKLQaELEESERLKKAQIEAFRQSQQlelsLRELQERLAQLENSRLVLEQDKLSlqtslELEKRERNAGSETIT 631
Cdd:PTZ00121  1399 KAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADEAKKKA-----EEAKKAEEAKKKAEE 1468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  632 DLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN 711
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  712 QSIEAKSETLKDMEHKLLEErsAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQV---EVLNVRVQQ-- 786
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEElk 1626
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  787 --ETQRKTLCQGDLKV--QRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTK 862
Cdd:PTZ00121  1627 kaEEEKKKVEQLKKKEaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  863 LYKTQIRELKE----ESDEKVKLYKDAQQRIEDLQEERDslASQLEVSLTKADSEQLARITVEEQYSDLEKEK---IMKE 935
Cdd:PTZ00121  1707 LKKKEAEEKKKaeelKKAEEENKIKAEEAKKEAEEDKKK--AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavIEEE 1784
                          570       580
                   ....*....|....*....|...
gi 1207153289  936 LEIKDMIARHRQDLAEKDGTINS 958
Cdd:PTZ00121  1785 LDEEDEKRRMEVDKKIKDIFDNF 1807
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
153-295 3.04e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 66.45  E-value: 3.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMpGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHS-LGFIHRDIKPDNMLLD-RNGHLKLADFGTCMKMDS 227
Cdd:cd14136     95 MVFEVL-GPNLLKLIKRYNyrgIPLPLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLCiSKIEVKIADLGNACWTDK 173
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  228 tgmvRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESlvG-TYGKIMDH 295
Cdd:cd14136    174 ----HFTEDIQTRQYRSPEVILGAG----YGTPADIWSTACMAFELATGDYLFDPHS--GeDYSRDEDH 232
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
84-274 3.33e-11

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 65.19  E-value: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKqlskfeMVK-RSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGD 162
Cdd:cd14155      1 IGSGFFSEVYKVRHRTSGQVMALK------MNTlSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTLTSNyDIPEEWaqfyTAEVVLALDA------IHSLGFIHRDIKPDNMLL--DRNGHLKL-ADFGTCMKMDSTGMVRC 233
Cdd:cd14155     75 LEQLLDS-NEPLSW----TVRVKLALDIarglsyLHSKGIFHRDLTSKNCLIkrDENGYTAVvGDFGLAEKIPDYSDGKE 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  234 DTA-VGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELL 274
Cdd:cd14155    150 KLAvVGSPYWMAPEVLRGE----PYNEKADVFSYGIILCEII 187
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
551-1097 3.75e-11

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 68.28  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  551 RQLEEVSAKlqaeleeSERLKKAQieafRQSQQLELSLRELQERLAQLENSRLVLeQDKLSLQTSLELEKRERNAgseti 630
Cdd:pfam01576    2 RQEEEMQAK-------EEELQKVK----ERQQKAESELKELEKKHQQLCEEKNAL-QEQLQAETELCAEAEEMRA----- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  631 tDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEdlttlEKEKNKQEIdlsfklKAVQQSLEQEEA-------EHKTTKAR 703
Cdd:pfam01576   65 -RLAARKQELEEILHELESRLEEEEERSQQLQN-----EKKKMQQHI------QDLEEQLDEEEAarqklqlEKVTTEAK 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  704 LadnnkinQSIEAKSETLKDMEHKLLEERSakqQLENRLMQL-----EKENSVLDCDYKQAKHE-----LQELRSLKENL 773
Cdd:pfam01576  133 I-------KKLEEDILLLEDQNSKLSKERK---LLEERISEFtsnlaEEEEKAKSLSKLKNKHEamisdLEERLKKEEKG 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  774 TEQVEVLNVRVQQETqrkTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQ 853
Cdd:pfam01576  203 RQELEKAKRKLEGES---TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  854 LEAEqyftKLYKTQirelkeesdekvklykdAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEK---- 929
Cdd:pfam01576  280 LESE----RAARNK-----------------AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKalee 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  930 EKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKI----KEEEKQMKSLT 1005
Cdd:pfam01576  339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSehkrKKLEGQLQELQ 418
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1006 VSY-----EKQIQVEKTLKIQA-INKLAEVMKKTDGRPHQINNtDIRRKEKEIRQLQLQLRTE---KEKLNHSIIKYQRE 1076
Cdd:pfam01576  419 ARLseserQRAELAEKLSKLQSeLESVSSLLNEAEGKNIKLSK-DVSSLESQLQDTQELLQEEtrqKLNLSTRLRQLEDE 497
                          570       580
                   ....*....|....*....|...
gi 1207153289 1077 INDMQAMIAEESQVR--LEMQMS 1097
Cdd:pfam01576  498 RNSLQEQLEEEEEAKrnVERQLS 520
PTZ00121 PTZ00121
MAEBL; Provisional
438-1033 4.01e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  438 LKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAE-----DNLRSLEKEKVLLKHQRTQSVRKAGlET 512
Cdd:PTZ00121  1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkaDELKKAEEKKKADEAKKAEEKKKAD-EA 1307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQ 592
Cdd:PTZ00121  1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  593 ERLAQLENSRLVLEQDKlslQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEK 672
Cdd:PTZ00121  1388 EEKKKADEAKKKAEEDK---KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  673 NKQEIDLSFKL-KAVQQSLEQEEAEHKTTKA-RLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENS 750
Cdd:PTZ00121  1465 KAEEAKKADEAkKKAEEAKKADEAKKKAEEAkKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  751 VLDCDYKQAKHELQELRSLKEnlTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQElnhLLELKLTLE 830
Cdd:PTZ00121  1545 KKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKKAEEAK 1619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  831 KQNQELSKEREESEK----QLKEMKDQLEAEQYFTKLYKTQIR--ELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLE 904
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKveqlKKKEAEEKKKAEELKKAEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  905 vslTKADSEQLARITVEEQYsdlEKEKIMKELEIKDMIARHRQDLAEKDGTinsleesnrtltvdVANLASEKEELNNKL 984
Cdd:PTZ00121  1700 ---EAKKAEELKKKEAEEKK---KAEELKKAEEENKIKAEEAKKEAEEDKK--------------KAEEAKKDEEEKKKI 1759
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  985 KHIQQklekikeeEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKT 1033
Cdd:PTZ00121  1760 AHLKK--------EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
70-292 4.30e-11

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 65.29  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   70 ELQVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEK 149
Cdd:cd05067      1 EWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM---SPDAFL-AEANLMKQLQHQRLVRLYAVVTQEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 yLYLVMEFMPGGDLVTL---TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:cd05067     76 -IYIITEYMENGSLVDFlktPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIE 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLvgdtpfyseslvgTYGKI 292
Cdd:cd05067    155 DNEYTAREGAKFPIKWTAPEAI----NYGTFTIKSDVWSFGILLTEIV-------------THGRI 203
PTZ00121 PTZ00121
MAEBL; Provisional
439-1102 5.25e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 5.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  439 KKLEEKFKHEMQAKEELENKCRiANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAgleTDRKRLL 518
Cdd:PTZ00121  1206 RKAEEERKAEEARKAEDAKKAE-AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA---EEARKAD 1281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  519 ENEVSSLKEQLAELKKKNQISHL-SAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSqqlELSLRELQERLAQ 597
Cdd:PTZ00121  1282 ELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADE 1358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  598 LENSRLVLEQDKlsLQTSLELEKRErnagsetitdlqgriyglegELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEI 677
Cdd:PTZ00121  1359 AEAAEEKAEAAE--KKKEEAKKKAD--------------------AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  678 dlsfKLKAvqqsleqEEAEHKTTKARLADNNKINQSIEAKSETLKDM--EHKLLEERSAKQQLENRLMQLEKEnsvldcd 755
Cdd:PTZ00121  1417 ----KKKA-------DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEAKKK------- 1478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  756 yKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEinsLRSSEQQLKQElnhllelkltlekqnqE 835
Cdd:PTZ00121  1479 -AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE---AKKAEEAKKAD----------------E 1538
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  836 LSKEREESE-KQLKEMKDQLEAEQyftklyKTQIRELKEESDEKVKLYKDAQQrIEDLQEERDSLASQLEVSLTKADSEQ 914
Cdd:PTZ00121  1539 AKKAEEKKKaDELKKAEELKKAEE------KKKAEEAKKAEEDKNMALRKAEE-AKKAEEARIEEVMKLYEEEKKMKAEE 1611
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  915 LARitveEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKI 994
Cdd:PTZ00121  1612 AKK----AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  995 KEEEKQMKSLTVSYEKQIQVEKtlKIQAINKLAEVMKKTDgRPHQINNTDIRRKEKEIRQLQLQLRTEKEKLNhSIIKYQ 1074
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEELKK--KEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLK 1763
                          650       660
                   ....*....|....*....|....*...
gi 1207153289 1075 REINDMQAMIAEESQVRLEMQmsLDSKD 1102
Cdd:PTZ00121  1764 KEEEKKAEEIRKEKEAVIEEE--LDEED 1789
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
70-286 6.49e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 65.02  E-value: 6.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   70 ELQVKLDDfdrvklIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEK 149
Cdd:cd07873      2 ETYIKLDK------LGEGTYATVYKGRSKLTDNLVALKEI-RLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIIHTEK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPG---------GDLVTLTSnydipeewAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG 220
Cdd:cd07873     74 SLTLVFEYLDKdlkqylddcGNSINMHN--------VKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  221 TCmKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGdTPFYSESLV 286
Cdd:cd07873    146 LA-RAKSIPTKTYSNEVVTLWYRPPDILL---GSTDYSTQIDMWGVGCIFYEMSTG-RPLFPGSTV 206
PH_MRCK cd01243
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ...
1213-1288 6.86e-11

MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269949  Cd Length: 135  Bit Score: 61.54  E-value: 6.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1213 EGWLSMPAKNTKRFGWDKKYVVVSSKKILFYDSEQDREQS---SPFMILDI-DKLFHVRPVTQTDVYRADPREIPRIFQI 1288
Cdd:cd01243     15 EGYVRVPKPGGVKKGWQRQFAVVCDFKLFLFDISEDKASQpsqVASQVLDMrDEEFSVSSVLASDVIHANKKDIPCIFRV 94
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
238-340 7.03e-11

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 64.30  E-value: 7.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGGtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemSKNAKDLICA 317
Cdd:cd14023    148 GCPAYVSPEILNTTGT--YSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPDHV--SPKARCLIRS 221
                           90       100
                   ....*....|....*....|...
gi 1207153289  318 FLssREVRLGRTGVDEIKCHPFF 340
Cdd:cd14023    222 LL--RREPSERLTAPEILLHPWF 242
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
81-274 7.28e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 64.91  E-value: 7.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKV----SQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQL--CCAFQDEKYLYLV 154
Cdd:cd05081      9 ISQLGKGNFGSVELCRYDPlgdnTGALVAVKQLQHSGPDQQRD---FQREIQILKALHSDFIVKYrgVSYGPGRRSLRLV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVT-LTSNYDIPEEWAQF-YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC--MKMDSTGM 230
Cdd:cd05081     86 MEYLPSGCLRDfLQRHRARLDASRLLlYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAklLPLDKDYY 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  231 VRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELL 274
Cdd:cd05081    166 VVREPGQSPIFWYAPESL----SDNIFSRQSDVWSFGVVLYELF 205
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1320-1374 7.82e-11

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 58.63  E-value: 7.82e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  1320 HEFVLTLYHFPSSCEVCPRPLWHVFRPppALECRRCRVKCHKDHIDRkeeVLAPC 1374
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQ--GLRCSECKVKCHKKCADK---VPKAC 50
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
81-316 8.06e-11

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 64.61  E-value: 8.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMKQL-----SKFEMVKRsdsaffweERDIMA-FSQSPWIVQLC-----CAFQDEK 149
Cdd:cd14037      8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVyvndeHDLNVCKR--------EIEIMKrLSGHKNIVGYIdssanRSGNGVY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTLT----SNYDIPEEWAQFYTaEVVLALDAIHSLG--FIHRDIKPDNMLLDRNGHLKLADFG-TC 222
Cdd:cd14037     80 EVLLLMEYCKGGGVIDLMnqrlQTGLTESEILKIFC-DVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGsAT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  223 MKM----DSTGMvrcdTAV-------GTPDYISPEVLMSQGGTGyYGRECDWWSVGVFIYELLVGDTPFySESlvGTYGk 291
Cdd:cd14037    159 TKIlppqTKQGV----TYVeedikkyTTLQYRAPEMIDLYRGKP-ITEKSDIWALGCLLYKLCFYTTPF-EES--GQLA- 229
                          250       260
                   ....*....|....*....|....*
gi 1207153289  292 IMDHKnsLTFPDdieMSKNAKDLIC 316
Cdd:cd14037    230 ILNGN--FTFPD---NSRYSKRLHK 249
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
78-281 8.31e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 65.12  E-value: 8.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVS--QQVYAMKQL----SKFEMVKRSDSA-----FFWEERDIMafsqspWIVQLCCAFQ 146
Cdd:cd07857      2 YELIKELGQGAYGIVCSARNAETseEETVAIKKItnvfSKKILAKRALRElkllrHFRGHKNIT------CLYDMDIVFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DE-KYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd07857     76 GNfNELYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGF 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  226 dSTGMVRCD----TAVGTPDYISPEVLMSQGGtgyYGRECDWWSVGVFIYELLvGDTPFY 281
Cdd:cd07857    156 -SENPGENAgfmtEYVATRWYRAPEIMLSFQS---YTKAIDVWSVGCILAELL-GRKPVF 210
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
82-211 1.10e-10

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 64.30  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVyamkqlSKFEMVKRSDSAFFWE------ERDIMAFSQSPWIVQLCCA---FQDEKYLy 152
Cdd:cd13981      6 KELGEGGYASVYLAKDDDEQSD------GSLVALKVEKPPSIWEfyicdqLHSRLKNSRLRESISGAHSahlFQDESIL- 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  153 lVMEFMPGGDL------VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN 211
Cdd:cd13981     79 -VMDYSSQGTLldvvnkMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLE 142
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
78-294 1.11e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 64.21  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQL------SKFEMVKRSDSAFFweeRDIMAFSQsPWIVQL--CCA---FQ 146
Cdd:cd07863      2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVrvqtneDGLPLSTVREVALL---KRLEAFDH-PNIVRLmdVCAtsrTD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMpGGDLVTLTSNY---DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCm 223
Cdd:cd07863     78 RETKVTLVFEHV-DQDLRTYLDKVpppGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA- 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  224 KMDSTGMVrCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIMD 294
Cdd:cd07863    156 RIYSCQMA-LTPVVVTLWYRAPEVLLQST----YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFD 221
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
151-280 1.41e-10

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 64.80  E-value: 1.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGgDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH-LKLADFGTCMKMD--- 226
Cdd:cd07854     91 VYIVQEYMET-DLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLvLKIGDFGLARIVDphy 169
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  227 ------STGMVrcdtavgTPDYISPEVLMSqggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07854    170 shkgylSEGLV-------TKWYRSPRLLLS---PNNYTKAIDMWAAGCIFAEMLTGKPLF 219
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
429-947 1.76e-10

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 65.93  E-value: 1.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQeaedNLRSLEKEKVLlkhqrtQSVRKA 508
Cdd:pfam07111  169 SKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVE----SLRKYVGEQVP------PEVHSQ 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 GLETDRKRLLENeVSSLKEQLAELKKKNQISHLSAEKNIH-LERQLEEVSAKLQ-AELEESERLKKAQIEAFRQSQQLEL 586
Cdd:pfam07111  239 TWELERQELLDT-MQHLQEDRADLQATVELLQVRVQSLTHmLALQEEELTRKIQpSDSLEPEFPKKCRSLLNRWREKVFA 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  587 SLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLT 666
Cdd:pfam07111  318 LMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTA 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  667 TLEKEknkqeidLSFKLKAV---QQSLEQEEAEHKTTKARLAD-NNKINQSIEaKSETLKDmehkLLEERSAKQQLENRL 742
Cdd:pfam07111  398 SAEEQ-------LKFVVNAMsstQIWLETTMTRVEQAVARIPSlSNRLSYAVR-KVHTIKG----LMARKVALAQLRQES 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  743 MQLEKENSVLDCDYKQakhELQELRSLKENLTEQVEVLNVRVQQETQRKTLcQGDlkVQRQEINSLrssEQQLKQELNHL 822
Cdd:pfam07111  466 CPPPPPAPPVDADLSL---ELEQLREERNRLDAELQLSAHLIQQEVGRARE-QGE--AERQQLSEV---AQQLEQELQRA 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  823 LELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYF------TKLYKTQIRELKEESDEKVKLYKDAQ---------- 886
Cdd:pfam07111  537 QESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIygqalqEKVAEVETRLREQLSDTKRRLNEARReqakavvslr 616
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  887 --QRIEDLQEERDSLASQLEVSLTKADSEQLARitveeQYSDLEKEK--IMKELEIKDMIARHRQ 947
Cdd:pfam07111  617 qiQHRATQEKERNQELRRLQDEARKEEGQRLAR-----RVQELERDKnlMLATLQQEGLLSRYKQ 676
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
471-1115 2.61e-10

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 65.52  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  471 KDLEEEVNARQEAEDNLRSLEKEKVL---LKHQRTQSVRKAGLETDRKRLLENEvsSLKEQLaelkkKNQISHLSAEKNI 547
Cdd:pfam15921   88 KDLQRRLNESNELHEKQKFYLRQSVIdlqTKLQEMQMERDAMADIRRRESQSQE--DLRNQL-----QNTVHELEAAKCL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  548 HlERQLEEVSAKLqaeleesERLKKAQIEAfrqsqqlELSLRELQERLAQLENS--RLVLEQDKLS------LQTSLELE 619
Cdd:pfam15921  161 K-EDMLEDSNTQI-------EQLRKMMLSH-------EGVLQEIRSILVDFEEAsgKKIYEHDSMStmhfrsLGSAISKI 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  620 KRERNAgseTITDLQGRIYGLEGELKHIKS-SLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAV--QQSLEQEEAE 696
Cdd:pfam15921  226 LRELDT---EISYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSArsQANSIQSQLE 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  697 HKTTKARLADNNKINQSIEAKSeTLKDMEHKLleeRSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQ 776
Cdd:pfam15921  303 IIQEQARNQNSMYMRQLSDLES-TVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  777 VEVLNVRVQ--------QETQRKTLCQGDLKVQ------RQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREE 842
Cdd:pfam15921  379 LQKLLADLHkrekelslEKEQNKRLWDRDTGNSitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNE 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  843 SEKQLKEMKDQLEAEqyftklyKTQIRELKEESDEKVKLYKDAQQRIEDL-----QEERDSLASQLEVSLTKA----DSE 913
Cdd:pfam15921  459 SLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDLtaslqEKERAIEATNAEITKLRSrvdlKLQ 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  914 QLARITVEE---QYSDLEKEKIMKELEIKD-MIARHRQDLAEKDGTINSLEESNRTLTVDVANLaseKEELNNKLKHIQQ 989
Cdd:pfam15921  532 ELQHLKNEGdhlRNVQTECEALKLQMAEKDkVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL---EKEINDRRLELQE 608
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  990 KLEKIKEEEKQMKSLtvsyEKQIQVEKTLKIQAINKLAEVMKKtdgrphqinntdIRRKEKEIRQLQLQLRTEKEKLNHS 1069
Cdd:pfam15921  609 FKILKDKKDAKIREL----EARVSDLELEKVKLVNAGSERLRA------------VKDIKQERDQLLNEVKTSRNELNSL 672
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289 1070 IIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:pfam15921  673 SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
81-284 2.69e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 62.57  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05114      9 MKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEED----FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVtltsNYdIPEEWAQFyTAEVVL--------ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVR 232
Cdd:cd05114     84 GCLL----NY-LRQRRGKL-SRDMLLsmcqdvceGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTS 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  233 CDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELLV-GDTPFYSES 284
Cdd:cd05114    158 SSGAKFPVKWSPPEVFNYS----KFSSKSDVWSFGVLMWEVFTeGKMPFESKS 206
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
84-274 2.81e-10

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 63.04  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd14222      1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKT---FLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYDiPEEWAQ--FYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--------------------- 220
Cdd:cd14222     78 KDFLRADD-PFPWQQkvSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGlsrliveekkkpppdkpttkk 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  221 -TCMKMDSTGMVrcdTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL 274
Cdd:cd14222    157 rTLRKNDRKKRY---TVVGNPYWMAPEMLNGKS----YDEKVDIFSFGIVLCEII 204
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1320-1374 2.83e-10

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 57.14  E-value: 2.83e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289 1320 HEFVLTLYHFPSSCEVCPRPLWHVFRppPALECRRCRVKCHKDHIDRkeeVLAPC 1374
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWGLFK--QGLKCSDCGLVCHKKCLDK---APSPC 50
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
558-1106 3.33e-10

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 64.99  E-value: 3.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  558 AKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLEnsrLVLEQDKLSLQTSLE-LEKRERNagsetITDLQGR 636
Cdd:TIGR00618  166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLT---LCTPCMPDTYHERKQvLEKELKH-----LREALQQ 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  637 IYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEK--------EKNKQEIDLSFK-------LKAVQQSLEQEEAEHKTTK 701
Cdd:TIGR00618  238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElraqeavlEETQERINRARKaaplaahIKAVTQIEQQAQRIHTELQ 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  702 ARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDcDYKQAKHELQELRSLKENLTEQVEVLN 781
Cdd:TIGR00618  318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  782 VrVQQETQRKTLCQGDLKVQRQEINSLR------SSEQQLKQELNHLLELKLTLEKQNQELSK-EREESEKQLKEMKDQL 854
Cdd:TIGR00618  397 S-LCKELDILQREQATIDTRTSAFRDLQgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQL 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  855 EAEQYFTKLY---KTQIRELKEESDEKVKLYKdaQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEK 931
Cdd:TIGR00618  476 QTKEQIHLQEtrkKAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  932 IMKEL-EIKDMIARHRQDLAEKDGTINSLEES---NRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVs 1007
Cdd:TIGR00618  554 ERKQRaSLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL- 632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1008 YEKQIQVEKTLKIQAINKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQL--------QLRTEKEKLNHSIIKYQREind 1079
Cdd:TIGR00618  633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALqkmqsekeQLTYWKEMLAQCQTLLREL--- 709
                          570       580
                   ....*....|....*....|....*..
gi 1207153289 1080 mQAMIAEESQVRLEMQMSLDSKDSDIE 1106
Cdd:TIGR00618  710 -ETHIEEYDREFNEIENASSSLGSDLA 735
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
418-899 3.39e-10

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 65.20  E-value: 3.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHTESNDLEKRLKKLEEKFKHE-------MQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSL 490
Cdd:pfam01576  583 DDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEkaisaryAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQL 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  491 EKEKVLLKHQRtQSVRKAGLETDR-KRLLENEVSSLKEQLAELKKKNQISHlsaEKNIHLERQLEEVSAK----LQAELE 565
Cdd:pfam01576  663 RAEMEDLVSSK-DDVGKNVHELERsKRALEQQVEEMKTQLEELEDELQATE---DAKLRLEVNMQALKAQferdLQARDE 738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  566 ESERLKKAQIeafRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELK 645
Cdd:pfam01576  739 QGEEKRRQLV---KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  646 HIKSS--------------LSKAEVEKRQLQEDLTTLEKEKNKQEIDlsfklkavQQSLEQEEAEHKTTKARLADNNKin 711
Cdd:pfam01576  816 EARASrdeilaqskesekkLKNLEAELLQLQEDLAASERARRQAQQE--------RDELADEIASGASGKSALQDEKR-- 885
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  712 qSIEAKsetLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQ-ETQR 790
Cdd:pfam01576  886 -RLEAR---IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTV 961
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  791 KTLCQGDLKVQRQEINSLrssEQQLKQElnhllelkltlEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQ--- 867
Cdd:pfam01576  962 KSKFKSSIAALEAKIAQL---EEQLEQE-----------SRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQaek 1027
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  868 ----IRELK---EESDEKVKLYKDA----QQRIEDLQEERDSL 899
Cdd:pfam01576 1028 gnsrMKQLKrqlEEAEEEASRANAArrklQRELDDATESNESM 1070
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
409-896 3.80e-10

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 64.74  E-value: 3.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  409 LTQQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLR 488
Cdd:pfam05483  329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  489 SL-----EKEKVLLKHQRTQSVRK--AGLETDRKRLL---ENEVSSLKEQLAELKKKNQishlsaekniHLERQLEEVSA 558
Cdd:pfam05483  409 ELkkilaEDEKLLDEKKQFEKIAEelKGKEQELIFLLqarEKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKT 478
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  559 KLqaeleESERLKKAQIEAfrQSQQLELSLRELQErlaqlENSRLVLEQDKlsLQTSLELEKRERNAGSETITDLQGRIY 638
Cdd:pfam05483  479 EL-----EKEKLKNIELTA--HCDKLLLENKELTQ-----EASDMTLELKK--HQEDIINCKKQEERMLKQIENLEEKEM 544
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  639 GLEGELKHIKSSLSKAEVEKR----QLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSI 714
Cdd:pfam05483  545 NLRDELESVREEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  715 EAKSETLKDMEHKL----LEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQR 790
Cdd:pfam05483  625 SAENKQLNAYEIKVnkleLELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  791 KTLCQGDLKVQRQEINSLRSSEQQLKQElnhllelkltlekQNQELSKEREESEKQLKEMKDQLEAEQyftklyktqiRE 870
Cdd:pfam05483  705 MVALMEKHKHQYDKIIEERDSELGLYKN-------------KEQEQSSAKAALEIELSNIKAELLSLK----------KQ 761
                          490       500
                   ....*....|....*....|....*.
gi 1207153289  871 LKEESDEKVKLYKDAQQRIEDLQEER 896
Cdd:pfam05483  762 LEIEKEEKEKLKMEAKENTAILKDKK 787
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
428-894 4.07e-10

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  428 HTESNDLEKRLKKLEEKFKHEMQAKEELENKCRianqRLEKLsKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRK 507
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELE----KLEKL-LQLLPLYQELEALEAELAELPERLEELEERLEELREL 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  508 AgletDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKniHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELS 587
Cdd:COG4717    162 E----EELEELEAELAELQEELEELLEQLSLATEEELQ--DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  588 LR--ELQERLAQLENSRLVleqdkLSLQTSLELEKRERNAGSETITDLQGRIYGL---------------EGELKHIKSS 650
Cdd:COG4717    236 LEaaALEERLKEARLLLLI-----AAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllarekaslGKEAEELQAL 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  651 LSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQ-EEAEHKTTKARLADNNKINQSI--EAKSETLKDMEHK 727
Cdd:COG4717    311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlREAEELEEELQLEELEQEIAALlaEAGVEDEEELRAA 390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  728 lLEERSAKQQLENRLMQLE---------KENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQ-ETQRKTLCQGD 797
Cdd:COG4717    391 -LEQAEEYQELKEELEELEeqleellgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAElEAELEQLEEDG 469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  798 lkvqrqEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREE-SEKQLKEMKDQleAEQYFTKLYKTQIRELKEESD 876
Cdd:COG4717    470 ------ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEyREERLPPVLER--ASEYFSRLTDGRYRLIRIDED 541
                          490
                   ....*....|....*...
gi 1207153289  877 EKVKLyKDAQQRIEDLQE 894
Cdd:COG4717    542 LSLKV-DTEDGRTRPVEE 558
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
433-655 4.72e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 63.24  E-value: 4.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQsvrkagLET 512
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------LRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLLENevssLKEQLAELKKKNQISH----LSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSL 588
Cdd:COG4942     98 ELEAQKEE----LAELLRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  589 RELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAE 655
Cdd:COG4942    174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
83-292 4.76e-10

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 61.98  E-value: 4.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAV--QLVRHKVSQQVYAMKQLSKFemVKRSDSAFFWEERDIMA-FSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd05047      2 VIGEGNFGQVlkARIKKDGLRMDAAIKRMKEY--ASKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTSNYDIPEEWAQF-----------------YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTC 222
Cdd:cd05047     80 HGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  223 MKMDstgmVRCDTAVGTpdyiSPEVLMSQGGTGY--YGRECDWWSVGVFIYELL-VGDTPFYSESLVGTYGKI 292
Cdd:cd05047    160 RGQE----VYVKKTMGR----LPVRWMAIESLNYsvYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 224
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
65-273 5.32e-10

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 61.60  E-value: 5.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   65 VCNLKELQVKlddfdrvKLIGRGAFGAVQLVRHKvSQQVyAMKQLskfemvKRSDSAF--FWEERDIMAFSQSPWIVQLC 142
Cdd:cd05039      2 AINKKDLKLG-------ELIGKGEFGDVMLGDYR-GQKV-AVKCL------KDDSTAAqaFLAEASVMTTLRHPNLVQLL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  143 CAFQDEKYLYLVMEFMPGGDLVT-LTS--NYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADF 219
Cdd:cd05039     67 GVVLEGNGLYIVTEYMAKGSLVDyLRSrgRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDF 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  220 GTCMKMDSTgmvrcdTAVGT-P-DYISPEVLMSqggtGYYGRECDWWSVGVFIYEL 273
Cdd:cd05039    147 GLAKEASSN------QDGGKlPiKWTAPEALRE----KKFSTKSDVWSFGILLWEI 192
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
73-280 5.56e-10

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 61.54  E-value: 5.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   73 VKLDDFDRVKLIGRGAFGAVQLVRHKVSQqvYAMKqlskfeMVKRSDSA-FFWEERDIMAFSQSPWIVQLCCAFQDEK-Y 150
Cdd:cd05082      3 LNMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVK------CIKNDATAqAFLAEASVMTQLRHSNLVQLLGVIVEEKgG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDS 227
Cdd:cd05082     75 LYIVTEYMAKGSLVDYLRSRGrsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASS 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  228 TGmvrcDTAVGTPDYISPEVLMSQggtgYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05082    155 TQ----DTGKLPVKWTAPEALREK----KFSTKSDVWSFGILLWEIYsFGRVPY 200
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
77-275 6.15e-10

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 62.30  E-value: 6.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKL-----IGRGAFGAVQLVRHKVSQQ--------------VYAMKQL-SKFEMVKRSDsafFWEERDIMAFSQSP 136
Cdd:cd05097      1 EFPRQQLrlkekLGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLrADVTKTARND---FLKEIKIMSRLKNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  137 WIVQLCCAFQDEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQ-------------FYTAEVVLALDAIHSLGFIHRDIKP 203
Cdd:cd05097     78 NIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTFTHannipsvsianllYMAVQIASGMKYLASLNFVHRDLAT 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  204 DNMLLDRNGHLKLADFGTCMKMDSTGMVRCD-TAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELLV 275
Cdd:cd05097    158 RNCLVGNHYTIKIADFGMSRNLYSGDYYRIQgRAVLPIRWMAWESIL----LGKFTTASDVWAFGVTLWEMFT 226
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
76-340 6.20e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 62.38  E-value: 6.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMK--QLSK--FEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ-DEKY 150
Cdd:cd14041      6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihQLNKnwRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLLDRN---GHLKLADFGTCMK 224
Cdd:cd14041     86 FCTVLEYCEGNDLdFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGLSKI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  225 MDST------GMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPF---YSESLVGTYGKIMdH 295
Cdd:cd14041    166 MDDDsynsvdGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFghnQSQQDILQENTIL-K 244
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289  296 KNSLTFPDDIEMSKNAKDLICAFLSSRevRLGRTGVDEIKCHPFF 340
Cdd:cd14041    245 ATEVQFPPKPVVTPEAKAFIRRCLAYR--KEDRIDVQQLACDPYL 287
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
501-989 6.33e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.91  E-value: 6.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  501 RTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKK-----NQISHLSAEKNIHLER--QLEEVSAKLQAELEESERLKkA 573
Cdd:PRK02224   180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESElaeldEEIERYEEQREQARETrdEADEVLEEHEERREELETLE-A 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  574 QIEAFRQSQQLELSLRE-LQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLS 652
Cdd:PRK02224   259 EIEDLRETIAETEREREeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  653 KAEVEKRQLQEDLTTLEkeknkqeidlsfklkavqqsleqEEAEHKTTKARLADnnkinqsieaksETLKDMEHKLLEER 732
Cdd:PRK02224   339 AHNEEAESLREDADDLE-----------------------ERAEELREEAAELE------------SELEEAREAVEDRR 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  733 SAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVevlnvrvqqetqrktlcqGDLKVQRQEINSLRSSE 812
Cdd:PRK02224   384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE------------------AELEATLRTARERVEEA 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEqyftklyktqiRELKEESDEKVKLYKDAQQRIEDL 892
Cdd:PRK02224   446 EALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE-----------VEEVEERLERAEDLVEAEDRIERL 514
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  893 QEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKEL----------EIKDMIARHRQDLAEKDGTINSLEES 962
Cdd:PRK02224   515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaeaeeeaeEAREEVAELNSKLAELKERIESLERI 594
                          490       500
                   ....*....|....*....|....*..
gi 1207153289  963 nRTLTVDVANLASEKEELNNKLKHIQQ 989
Cdd:PRK02224   595 -RTLLAAIADAEDEIERLREKREALAE 620
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
78-276 6.50e-10

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 61.73  E-value: 6.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd07836      2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEI-HLDAEEGTPSTAI-REISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGgDLV----TLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFgtcmkmdstGMVRc 233
Cdd:cd07836     80 MDK-DLKkymdTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADF---------GLAR- 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  234 dtAVGTPD-----------YISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd07836    149 --AFGIPVntfsnevvtlwYRAPDVLL---GSRTYSTSIDIWSVGCIMAEMITG 197
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
83-280 6.57e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 62.13  E-value: 6.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVqlVRHKVSQQVYAMKQLskFEMVKRSDSAF---FWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd14158     22 KLGEGGFGVV--FKGYINDKNVAVKKL--AAMVDISTEDLtkqFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  160 GGDLVTLTS--NYDIPEEWAQFYTAEVVLA--LDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK--MDSTGMVrC 233
Cdd:cd14158     98 NGSLLDRLAclNDTPPLSWHMRCKIAQGTAngINYLHENNHIHRDIKSANILLDETFVPKISDFGLARAseKFSQTIM-T 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  234 DTAVGTPDYISPEVLmsqggTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14158    177 ERIVGTTAYMAPEAL-----RGEITPKSDIFSFGVVLLEIITGLPPV 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
403-748 6.83e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 6.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  403 FREDQLLTQQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEevnarqe 482
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE------- 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  483 aednlrsLEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQishlsaekniHLERQLEEVSAKLQA 562
Cdd:TIGR02168  780 -------AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE----------SLERRIAATERRLED 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  563 ELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEG 642
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  643 ELKHIKSSLSKAEVEKRQLQEDLTtlEKEKNKQEIDLSFKLKAV--QQSLEQEEAEHKTTKARLADnnkIN----QSIEA 716
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEALENKIEddEEEARRRLKRLENKIKELGP---VNlaaiEEYEE 997
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1207153289  717 KSETLKDMEHKLLEERSAKQQLENRLMQLEKE 748
Cdd:TIGR02168  998 LKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
542-790 8.09e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 62.47  E-value: 8.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  542 SAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDklslqtslelekr 621
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  622 ernagsetITDLQGRIYGLEGELKHIKSSLSK--AEVEKRQLQEDLTTLEKEKNKQEIDLSFK-LKAVQQSLEQEEAEHK 698
Cdd:COG4942     85 --------LAELEKEIAELRAELEAQKEELAEllRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  699 TTKARLADnnkINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKEnsvLDCDYKQAKHELQELRSLKENLTEQVE 778
Cdd:COG4942    157 ADLAELAA---LRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIA 230
                          250
                   ....*....|..
gi 1207153289  779 VLNVRVQQETQR 790
Cdd:COG4942    231 RLEAEAAAAAER 242
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
187-282 8.23e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 62.55  E-value: 8.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  187 ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD-STGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWS 265
Cdd:PHA03207   197 ALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDaHPDTPQCYGWSGTLETNSPELL----ALDPYCAKTDIWS 272
                           90
                   ....*....|....*..
gi 1207153289  266 VGVFIYELLVGDTPFYS 282
Cdd:PHA03207   273 AGLVLFEMSVKNVTLFG 289
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
84-220 8.55e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 58.22  E-value: 8.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKQLSKfemvkRSDSAFFWEERDI----MAFSQSPWIVQLCCAFQDEKYLYLVMEFMP 159
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVKIGDD-----VNNEEGEDLESEMdilrRLKGLELNIPKVLVTEDVDGPNILLMELVK 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  160 GGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG 220
Cdd:cd13968     76 GGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
76-284 9.02e-10

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 61.12  E-value: 9.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05112      4 SELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEED----FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVtltsnyDIPEEWAQFYTAEVVLA--LDA------IHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMD 226
Cdd:cd05112     79 EFMEHGCLS------DYLRTQRGLFSAETLLGmcLDVcegmayLEEASVIHRDLAARNCLVGENQVVKVSDFGmTRFVLD 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  227 StgmvRCDTAVGTP---DYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLV-GDTPFYSES 284
Cdd:cd05112    153 D----QYTSSTGTKfpvKWSSPEVF----SFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRS 206
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
174-340 9.69e-10

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 60.82  E-value: 9.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  174 EEWAQ-FYtaEVVLALDAIHSLGFIHRDIKPDNMLL--DRNGHLKLADFGTCMKMDSTGMVRCDTAvGTPDYISPEVLMS 250
Cdd:cd14022     84 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFVFkdEERTRVKLESLEDAYILRGHDDSLSDKH-GCPAYVSPEILNT 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  251 QGGtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDdiEMSKNAKDLICAFLssREVRLGRTG 330
Cdd:cd14022    161 SGS--YSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRSIL--RREPSERLT 232
                          170
                   ....*....|
gi 1207153289  331 VDEIKCHPFF 340
Cdd:cd14022    233 SQEILDHPWF 242
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
74-286 1.08e-09

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 61.55  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd07872      4 KMETYIKLEKLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDKSLTL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGG------DLVTLTSNYDIpeewaQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDS 227
Cdd:cd07872     82 VFEYLDKDlkqymdDCGNIMSMHNV-----KIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKS 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  228 TGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGdTPFYSESLV 286
Cdd:cd07872    156 VPTKTYSNEVVTLWYRPPDVLL---GSSEYSTQIDMWGVGCIFFEMASG-RPLFPGSTV 210
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
1317-1361 1.12e-09

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 55.38  E-value: 1.12e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289 1317 HKGHEFVLTLYHFPSSCEVCPRPLWHVFRpppALECRRCRVKCHK 1361
Cdd:cd20818      1 HNGHKFATVQFNIPTYCEVCNSFIWLMEK---GLVCQVCKFTCHK 42
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
82-280 1.28e-09

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 60.32  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrSDSAFFwEERDIMAFSQSPWIVQLCcAFQDEKYLYLVMEFMPGG 161
Cdd:cd14203      1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTM---SPEAFL-EEAQIMKKLRHDKLVQLY-AVVSEEPIYIVTEFMSKG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYD-----IPEEWAQfyTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTA 236
Cdd:cd14203     75 SLLDFLKDGEgkylkLPQLVDM--AAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGA 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  237 VGTPDYISPEVLMsqggtgyYGR---ECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd14203    153 KFPIKWTAPEAAL-------YGRftiKSDVWSFGILLTELVTkGRVPY 193
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
79-341 1.37e-09

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 61.50  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   79 DRVKLIGRG--AFGAVQLVRHKVSQQVYAMKQLSkFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVME 156
Cdd:cd08227      1 ELLTVIGRGfeDLMTVNLARYKPTGEYVTVRRIN-LEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  157 FMPGG---DLVTlTSNYDIPEEWAQFYTAEVVL-ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMvR 232
Cdd:cd08227     80 FMAYGsakDLIC-THFMDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQ-R 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  233 CDTAVGTPDY-------ISPEVLmSQGGTGYYGREcDWWSVGVFIYELLVGDTPF--------YSESLVGTYGKIMDhkN 297
Cdd:cd08227    158 LRVVHDFPKYsvkvlpwLSPEVL-QQNLQGYDAKS-DIYSVGITACELANGHVPFkdmpatqmLLEKLNGTVPCLLD--T 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  298 SLTFPDDIEMSKNAKDLICAFLSSREVRLGRTGVDEIKCHPFFK 341
Cdd:cd08227    234 TTIPAEELTMKPSRSGANSGLGESTTVSTPRPSNGESSSHPYNR 277
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
73-280 1.40e-09

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 60.66  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   73 VKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrSDSAFFWEERDIMAFSQsPWIVQLCCAFQDEKYLY 152
Cdd:cd05113      1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSM---SEDEFIEEAKVMMNLSH-EKLVQLYGVCTKQRPIF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd05113     76 IITEYMANGCLLNYLREMRKRFQTQQLleMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEY 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  231 VrcdTAVGTP---DYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05113    156 T---SSVGSKfpvRWSPPEVLMYSK----FSSKSDVWAFGVLMWEVYsLGKMPY 202
HR1_ROCK cd11626
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
496-560 1.46e-09

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase; ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It is a serine/threonine protein kinase that is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. ROCKs are the best-described effectors of RhoA. There are two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. ROCK contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212016 [Multi-domain]  Cd Length: 66  Bit Score: 55.44  E-value: 1.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  496 LLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKL 560
Cdd:cd11626      2 LLQHRQQEYQRKADMEAEKRRNVENDVAALKDQLEDLKKQKQESQKAEEKARQLQKQLEEANRLL 66
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
439-778 1.58e-09

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 62.45  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  439 KKLEEKFKHEMQAK--EELENKCRIANQRleklsKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLEtDRKR 516
Cdd:pfam17380  287 RQQQEKFEKMEQERlrQEKEEKAREVERR-----RKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE-ERKR 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  517 llENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQqlelsLRELQERLA 596
Cdd:pfam17380  361 --ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ-----IRAEQEEAR 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  597 QLENSRlvLEQDKLSLQTSLELEKRERNAGSEtitdlqgRIYGLEGELKHIKSSLSKAEVEKRQLQED-LTTLEKEknkq 675
Cdd:pfam17380  434 QREVRR--LEEERAREMERVRLEEQERQQQVE-------RLRQQEEERKRKKLELEKEKRDRKRAEEQrRKILEKE---- 500
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  676 eidlsfkLKAVQQSLEQEEAEHKTTKARLADNNKI----NQSIEAKSETLKDMEhklLEERsakQQLENRLMQLEKENSV 751
Cdd:pfam17380  501 -------LEERKQAMIEEERKRKLLEKEMEERQKAiyeeERRREAEEERRKQQE---MEER---RRIQEQMRKATEERSR 567
                          330       340
                   ....*....|....*....|....*..
gi 1207153289  752 LDCdykqAKHELQELRSLKENLTEQVE 778
Cdd:pfam17380  568 LEA----MEREREMMRQIVESEKARAE 590
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
84-280 1.74e-09

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 60.33  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVYAMKqlSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL 163
Cdd:cd05084      4 IGRGNFGEVFSGRLRADNTPVAVK--SCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNydipeEWAQFYTAEVV-LALDAIHSLGF------IHRDIKPDNMLLDRNGHLKLADFGTCMKMD-----STGMV 231
Cdd:cd05084     82 LTFLRT-----EGPRLKVKELIrMVENAAAGMEYleskhcIHRDLAARNCLVTEKNVLKISDFGMSREEEdgvyaATGGM 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  232 RcdtavGTP-DYISPEVLmsqgGTGYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05084    157 K-----QIPvKWTAPEAL----NYGRYSSESDVWSFGILLWETFsLGAVPY 198
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
549-784 1.75e-09

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 62.34  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  549 LERQLEEvsakLQAELEESErlkkAQIEAFRQSQQ---LELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNA 625
Cdd:COG3206    180 LEEQLPE----LRKELEEAE----AALEEFRQKNGlvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  626 GSETITDLQGriyglEGELKHIKSSLSKAEVEKRQLQEDLTtlekEKNKQEIDLSFKLKAVQQSLEQEeaehktTKARLA 705
Cdd:COG3206    252 GPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYT----PNHPDVIALRAQIAALRAQLQQE------AQRILA 316
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  706 DNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRslkenLTEQVEVLNVRV 784
Cdd:COG3206    317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR-----LAEALTVGNVRV 390
PRK11281 PRK11281
mechanosensitive channel MscK;
507-907 2.51e-09

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 62.24  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  507 KAGLETDRKRLLeneVSSLKEQLAELKKKNQishlSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQlEL 586
Cdd:PRK11281    50 KQKLLEAEDKLV---QQDLEQTLALLDKIDR----QKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  587 SLRELQERLAQLE-------------NSRLVleqdklSLQTSLElekRERNAGSETITDLQgRIYGLEGELKHIKSSLSK 653
Cdd:PRK11281   122 SLRQLESRLAQTLdqlqnaqndlaeyNSQLV------SLQTQPE---RAQAALYANSQRLQ-QIRNLLKGGKVGGKALRP 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  654 AEVEKRQLQEDLTTLEKEKNKQEIDLSFKLkavqQSLEQEEAEHKTTK-ARLADNNKINQS-IEAKSETlkdmehklLEE 731
Cdd:PRK11281   192 SQRVLLQAEQALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTARiQRLEHQLQLLQEaINSKRLT--------LSE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  732 RSAKQQLENRLMQLEKENSVLdcdykqaKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQR---QEINSL 808
Cdd:PRK11281   260 KTVQEAQSQDEAARIQANPLV-------AQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERnikEQISVL 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  809 RSSE------QQLKQELNHLLElkltlekqNQELSKE----REEsEKQLKEMKDQL-EAEQYFTKLYKTQirelKEESDE 877
Cdd:PRK11281   333 KGSLllsrilYQQQQALPSADL--------IEGLADRiadlRLE-QFEINQQRDALfQPDAYIDKLEAGH----KSEVTD 399
                          410       420       430
                   ....*....|....*....|....*....|
gi 1207153289  878 KVKlykdaqQRIEDLQEERDSLASQLEVSL 907
Cdd:PRK11281   400 EVR------DALLQLLDERRELLDQLNKQL 423
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
80-274 3.25e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 59.91  E-value: 3.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRHKVSQ----QVYAMKQLsKFEMVKRSDSAFFwEERDIMAFSQSPWIVQL--CCAFQDEKYLYL 153
Cdd:cd05080      8 KIRDLGEGHFGKVSLYCYDPTNdgtgEMVAVKAL-KADCGPQHRSGWK-QEIDILKTLYHENIVKYkgCCSEQGGKSLQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTG--MV 231
Cdd:cd05080     86 IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLA-KAVPEGheYY 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  232 RCDTAVGTPDY-ISPEVLmsqggtgyygREC------DWWSVGVFIYELL 274
Cdd:cd05080    165 RVREDGDSPVFwYAPECL----------KEYkfyyasDVWSFGVTLYELL 204
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
84-289 3.98e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 59.84  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVqlVRHKVSQQVYAMKQLSK-----FEMVKRSdsafFWEERDIMAFSQSPWIVQLC-CAFQDEKYLyLVMEF 157
Cdd:cd14159      1 IGEGGFGCV--YQAVMRNTEYAVKRLKEdseldWSVVKNS----FLTEVEKLSRFRHPNIVDLAgYSAQQGNYC-LIYVY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVT-LTSNYDIPE-EWAQfyTAEVVL----ALDAIH--SLGFIHRDIKPDNMLLDRNGHLKLADFG-------TC 222
Cdd:cd14159     74 LPNGSLEDrLHCQVSCPClSWSQ--RLHVLLgtarAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGlarfsrrPK 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  223 MKMDSTGMVRCDTAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTY 289
Cdd:cd14159    152 QPGMSSTLARTQTVRGTLAYLPEEYVK----TGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTK 214
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
80-274 4.00e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 59.56  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   80 RVKLIGRGAFGAVQLVRH-----KVSQQVyAMKQLSKFEmvKRSDSAFFWEERDIMAFSQSPWIVQL--CCAFQDEKYLY 152
Cdd:cd05079      8 RIRDLGEGHFGKVELCRYdpegdNTGEQV-AVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYkgICTEDGGNGIK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVT-LTSNYD-IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDST 228
Cdd:cd05079     85 LIMEFLPSGSLKEyLPRNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGltKAIETDKE 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  229 GMVRCDTAVGTPDYISPEVLMSqggTGYYgRECDWWSVGVFIYELL 274
Cdd:cd05079    165 YYTVKDDLDSPVFWYAPECLIQ---SKFY-IASDVWSFGVTLYELL 206
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
428-603 4.25e-09

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 61.02  E-value: 4.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  428 HTESNDLEKRLKKLEEKFKHEMQAKEEL-----ENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKekvLLKHQRT 502
Cdd:pfam06160  229 ALEHLNVDKEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIED---YLEHAEE 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  503 QSvRKAGLETDR----KRLLENEVS---SLKEQLAELKKKNQ-ISHLSAEKNI----------HLERQLEEVSAKlQAEL 564
Cdd:pfam06160  306 QN-KELKEELERvqqsYTLNENELErvrGLEKQLEELEKRYDeIVERLEEKEVayselqeeleEILEQLEEIEEE-QEEF 383
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1207153289  565 EES-ERLKKAQIEAFRQSQQLELSLRELqERLaqLENSRL 603
Cdd:pfam06160  384 KESlQSLRKDELEAREKLDEFKLELREI-KRL--VEKSNL 420
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
84-284 4.76e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 59.21  E-value: 4.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVR-HKVS----QQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd05092     13 LGEGAFGKVFLAEcHNLLpeqdKMLVAVKALKEATESARQD---FQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL------------------------VTLTSNYDIPeewAQFYTAEVVLAldaihSLGFIHRDIKPDNMLLDRNGHL 214
Cdd:cd05092     90 RHGDLnrflrshgpdakildggegqapgqLTLGQMLQIA---SQIASGMVYLA-----SLHFVHRDLATRNCLVGQGLVV 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  215 KLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMSQGGTgyygRECDWWSVGVFIYELLV-GDTPFYSES 284
Cdd:cd05092    162 KIGDFGMSRDIYSTDYYRVGGRTMLPiRWMPPESILYRKFT----TESDIWSFGVVLWEIFTyGKQPWYQLS 229
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
592-819 4.89e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.16  E-value: 4.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  592 QERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKE 671
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  672 KNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLleeRSAKQQLENRLMQLEKENSV 751
Cdd:COG4942     99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL---RADLAELAALRAELEAERAE 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  752 LDCDYKQAKHELQELRSLKENLTEQVEVLnvrvqqetqrktlcQGDLKVQRQEINSLRSSEQQLKQEL 819
Cdd:COG4942    176 LEALLAELEEERAALEALKAERQKLLARL--------------EKELAELAAELAELQQEAEELEALI 229
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
74-280 4.95e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 59.32  E-value: 4.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   74 KLDDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFfwEERDIMAFSQSPWIVQLCCAFQDEKYLYL 153
Cdd:cd07869      3 KADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI--REASLLKGLKHANIVLLHDIIHTKETLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  154 VMEFMpGGDLVTLTSNY--DIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMV 231
Cdd:cd07869     81 VFEYV-HTDLCQYMDKHpgGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA-RAKSVPSH 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  232 RCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07869    159 TYSNEVVTLWYRPPDVLL---GSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
184-342 5.03e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 59.26  E-value: 5.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  184 VVLALDAIH-SLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTG----MVRCDT------AVGTPDYISPEVLMSQG 252
Cdd:cd14011    123 ISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATdqfpYFREYDpnlpplAQPNLNYLAPEYILSKT 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  253 gtgyYGRECDWWSVGVFIYELLV-GDTPFYSESLVGTYGKIMDHKNSLTFPDDIEMSKNAKDLICAFLSSREVRlgRTGV 331
Cdd:cd14011    203 ----CDPASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEV--RPDA 276
                          170
                   ....*....|.
gi 1207153289  332 DEIKCHPFFKN 342
Cdd:cd14011    277 EQLSKIPFFDD 287
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
84-280 5.47e-09

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 58.90  E-value: 5.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQ--LVRHKVSQQV-YAMKQLSKFEMVkrSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLyLVMEFMPG 160
Cdd:cd05060      3 LGHGNFGSVRkgVYLMKSGKEVeVAVKTLKQEHEK--AGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVT-LTSNYDIPE----EWAQfytaEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFgtcmkmdstGMVRcdt 235
Cdd:cd05060     80 GPLLKyLKKRREIPVsdlkELAH----QVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDF---------GMSR--- 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  236 AVGT-PDYISPEvlmsQGG---TGYYGREC----------DWWSVGVFIYELL-VGDTPF 280
Cdd:cd05060    144 ALGAgSDYYRAT----TAGrwpLKWYAPECinygkfssksDVWSYGVTLWEAFsYGAKPY 199
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
183-276 5.92e-09

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 58.66  E-value: 5.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  183 EVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmkmdSTGMVRCDTAVGTPDYISPEVLmsqggTGYYGRECD 262
Cdd:cd13975    110 DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC----KPEAMMSGSIVGTPIHMAPELF-----SGKYDNSVD 180
                           90
                   ....*....|....
gi 1207153289  263 WWSVGVFIYELLVG 276
Cdd:cd13975    181 VYAFGILFWYLCAG 194
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
418-988 6.14e-09

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 61.22  E-value: 6.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHT-ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEeVNARQEAEDNLRSLEKEkvl 496
Cdd:TIGR01612 1099 DDFGKEENIKYAdEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED-VADKAISNDDPEEIEKK--- 1174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  497 LKHQRTQSVRKAGLETDRKRLLeNEVSSLK-------------------------EQLAELKKKNQISHLSAEKNIHLER 551
Cdd:TIGR01612 1175 IENIVTKIDKKKNIYDEIKKLL-NEIAEIEkdktsleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLD 1253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  552 QLEEVSAKLQAELEeSERLKKAQIEAFRQS----QQLELSLRELQERLAQLENSRLVLEQD----------KLSLQTSLe 617
Cdd:TIGR01612 1254 EIKEKSPEIENEMG-IEMDIKAEMETFNIShdddKDHHIISKKHDENISDIREKSLKIIEDfseesdindiKKELQKNL- 1331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  618 LEKRERNAGSETITDLQGRIYGLEgELKHIKSSLSKAEVEKRQLQEDlttlekEKN-KQEIDLSFKL-KAVQQSLEQEEA 695
Cdd:TIGR01612 1332 LDAQKHNSDINLYLNEIANIYNIL-KLNKIKKIIDEVKEYTKEIEEN------NKNiKDELDKSEKLiKKIKDDINLEEC 1404
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  696 EHKTTKArlADNNKINQSIEakseTLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQE-LRSLKENLT 774
Cdd:TIGR01612 1405 KSKIEST--LDDKDIDECIK----KIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNAT 1478
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  775 EQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQeLSKEREESEKQLKEMKDQl 854
Cdd:TIGR01612 1479 NDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNK-FAKTKKDSEIIIKEIKDA- 1556
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  855 eaeqyftklyKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDS---LASQLEVSLTKADSEQLARITVEEQYSDLEKEK 931
Cdd:TIGR01612 1557 ----------HKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkAAIDIQLSLENFENKFLKISDIKKKINDCLKET 1626
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  932 IMKELEIKDM-IARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNN---KLKHIQ 988
Cdd:TIGR01612 1627 ESIEKKISSFsIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDEldsEIEKIE 1687
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
404-748 6.19e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  404 REDQLLTQQNKCSEEdiIEDhglNHTESNDLEKRLKKLEEKFKHEMQAKEELENkcRIANQRLEKLSKDLEEEVNARQEA 483
Cdd:TIGR02169  738 RLEELEEDLSSLEQE--IEN---VKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRI 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  484 EDNLRSLEkekvllkhqrtqsvRKAGLETDRKRLLENEVSSLKEQLAELkkKNQIShlsaekniHLERQLEEVSAKLQAE 563
Cdd:TIGR02169  811 EARLREIE--------------QKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIK--------SIEKEIENLNGKKEEL 866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  564 LEESERLKKAqieafrqsqqlelsLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGE 643
Cdd:TIGR02169  867 EEELEELEAA--------------LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  644 LKHIKSSLsKAEVEKRQLQEDLTTLEKEKNKQEIDLSfKLKAVQQSLEQEEAEhktTKARLADnnkinqsieaksetLKD 723
Cdd:TIGR02169  933 LSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEE---VLKRLDE--------------LKE 993
                          330       340
                   ....*....|....*....|....*
gi 1207153289  724 MEHKLLEERSAKQQLENRLMQLEKE 748
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKRE 1018
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
423-778 6.56e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 61.01  E-value: 6.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  423 DHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRT 502
Cdd:pfam12128  591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  503 QSVrkagleTDRKRLLENEVSSLKEQLAELKKKNQishlsaEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAfrqsq 582
Cdd:pfam12128  671 KAL------AERKDSANERLNSLEAQLKQLDKKHQ------AWLEEQKEQKREARTEKQAYWQVVEGALDAQLAL----- 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  583 qlelslreLQERLAQLENSRLVlEQDKLSLQTSLELEKreRNAGSETITDLQGRIYGLEGELKHIKSSLSKAeVEKRQLQ 662
Cdd:pfam12128  734 --------LKAAIAARRSGAKA-ELKALETWYKRDLAS--LGVDPDVIAKLKREIRTLERKIERIAVRRQEV-LRYFDWY 801
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  663 EDLTTLEKEKNKQEI-DLSFKLKAVQQSLEQEEAEHKTTkarladnnkiNQSIEAKSETLKDMEHKLLEERSAKQQLENR 741
Cdd:pfam12128  802 QETWLQRRPRLATQLsNIERAISELQQQLARLIADTKLR----------RAKLEMERKASEKQQVRLSENLRGLRCEMSK 871
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1207153289  742 LMQLEkensvLDCDYKQAKHE-------LQELRSLKENLTEQVE 778
Cdd:pfam12128  872 LATLK-----EDANSEQAQGSigerlaqLEDLKLKRDYLSESVK 910
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
647-1002 6.58e-09

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 60.76  E-value: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  647 IKSSLSKAEVEKRQLQEDL-TTLEKEKNKQEidlSFKLKAVQQSLEQEEAEHKTTKA---RLADNNKINQSIEAKSETLK 722
Cdd:pfam02463  144 IEIIAMMKPERRLEIEEEAaGSRLKRKKKEA---LKKLIEETENLAELIIDLEELKLqelKLKEQAKKALEYYQLKEKLE 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  723 DMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKtLCQGDLKVQR 802
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK-LLAKEEEELK 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  803 QEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLY 882
Cdd:pfam02463  300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  883 KDAQQRIEDLQEERDSLASQLEVSLTKADSEqlarITVEEQYSDLEKEKIMKELEIKDMIaRHRQDLAEKDGTINSLEES 962
Cdd:pfam02463  380 KLESERLSSAAKLKEEELELKSEEEKEAQLL----LELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELE 454
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1207153289  963 NRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMK 1002
Cdd:pfam02463  455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
146-339 6.66e-09

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 58.35  E-value: 6.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEKYLYLVMEFmpgGDLVTLT-SNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTcmk 224
Cdd:cd14024     57 QDRAYAFFSRHY---GDMHSHVrRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNL--- 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  225 MDSTGMVRCDTAV----GTPDYISPEVLMSqgGTGYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLT 300
Cdd:cd14024    131 EDSCPLNGDDDSLtdkhGCPAYVGPEILSS--RRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI--RRGAFS 206
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207153289  301 FPDdiEMSKNAKDLICAFLssREVRLGRTGVDEIKCHPF 339
Cdd:cd14024    207 LPA--WLSPGARCLVSCML--RRSPAERLKASEILLHPW 241
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
581-1113 7.57e-09

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 60.54  E-value: 7.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  581 SQQLELSLRELQERLAQLENSRLVLE---QDKLSLQT-SLELE--KRERNAGSETITDLQGRIYGLEGELKHIKSSLSKA 654
Cdd:pfam07111   62 SQQAELISRQLQELRRLEEEVRLLREtslQQKMRLEAqAMELDalAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRE 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  655 EVEKRQL-QEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAK-SETLKDMEHKLLEER 732
Cdd:pfam07111  142 LEEIQRLhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQlSKTQEELEAQVTLVE 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  733 SAKQQLENRLMQlEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSE 812
Cdd:pfam07111  222 SLRKYVGEQVPP-EVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELnhllelkltlekqnqeLSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKE----ESDEKVKLYKDAQQR 888
Cdd:pfam07111  301 PKKCRSL----------------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsQSQEQAILQRALQDK 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  889 IEDLQEERDSLASqLEVSLTKAdseQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTV 968
Cdd:pfam07111  365 AAEVEVERMSAKG-LQMELSRA---QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  969 DVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLT-VSYEKQIQVEKTLKIQAINKL-AEVMKKTDGRPHQINNTDIR 1046
Cdd:pfam07111  441 AVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDAdLSLELEQLREERNRLDAELQLsAHLIQQEVGRAREQGEAERQ 520
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289 1047 RKEKEIRQLQLQLRTEKEKLNHSIIKYQREINDMQAMIAEESQVRLEMQ-------MSLDSKDSDIE-RLRSQLT 1113
Cdd:pfam07111  521 QLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTqqqeiygQALQEKVAEVEtRLREQLS 595
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
495-560 8.91e-09

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 53.09  E-value: 8.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  495 VLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKL 560
Cdd:cd11639      1 MMLQHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
441-964 1.14e-08

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 59.84  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  441 LEEKFKHEMQAKEELE--NKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKH-------QRTQSVRKAGLE 511
Cdd:pfam10174  201 LDQKEKENIHLREELHrrNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTngllhteDREEEIKQMEVY 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  512 TDRKRLLENEVSSLKEqlaELKKKnqishlsaeknihlERQLEEVSAKLQAeLEESERLKKAQIEAfrqsqqlelslreL 591
Cdd:pfam10174  281 KSHSKFMKNKIDQLKQ---ELSKK--------------ESELLALQTKLET-LTNQNSDCKQHIEV-------------L 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  592 QERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQ---EDLTTL 668
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQkkiENLQEQ 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 EKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKInqsIEAksetLKdmEHKLLEERSAKQQLEnrlmQLEKE 748
Cdd:pfam10174  410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERI---IER----LK--EQREREDRERLEELE----SLKKE 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  749 NSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQ-ELNHLLELKL 827
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNaEEAVRTNPEI 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  828 TLEKQN--QELSKEREESEKQ----------LKEMK-DQLEAEQYFTKLYKTQIRELKEESDEKVKLyKDAQQriedlqE 894
Cdd:pfam10174  557 NDRIRLleQEVARYKEESGKAqaeverllgiLREVEnEKNDKDKKIAELESLTLRQMKEQNKKVANI-KHGQQ------E 629
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  895 ERDSLASQLEVSLTKADSeqLARITVEEQYSDL--EKEKIMKELE-IKDMIARHRQDLAEKDGTINSLEESNR 964
Cdd:pfam10174  630 MKKKGAQLLEEARRREDN--LADNSQQLQLEELmgALEKTRQELDaTKARLSSTQQSLAEKDGHLTNLRAERR 700
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
516-1108 1.18e-08

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 59.85  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  516 RLLENEVSSLKEQLaelkKKNQISHLSAEknIHLERQLEEVSAKLQAELEESERLKKAQIEAfrqsQQLELSLRELQERL 595
Cdd:pfam12128  205 ILEDDGVVPPKSRL----NRQQVEHWIRD--IQAIAGIMKIRPEFTKLQQEFNTLESAELRL----SHLHFGYKSDETLI 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  596 AQLENSRLVLEQDKLSLQTSLELEKRERNAgsetitDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDltTLEKEKNKQ 675
Cdd:pfam12128  275 ASRQEERQETSAELNQLLRTLDDQWKEKRD------ELNGELSAADAAVAKDRSELEALEDQHGAFLDA--DIETAAADQ 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  676 EidlsfKLKAVQQSLEQEEAEHK--TTKArladnnkinQSIEAKSETLKdmehklleeRSAKQQLENRLMQLEKE-NSVL 752
Cdd:pfam12128  347 E-----QLPSWQSELENLEERLKalTGKH---------QDVTAKYNRRR---------SKIKEQNNRDIAGIKDKlAKIR 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  753 DCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQrqeINSLRSSEQQLKQELNhllelkltlekQ 832
Cdd:pfam12128  404 EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLR---LNQATATPELLLQLEN-----------F 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  833 NQELSKEREESEKQLKEMKDQLEAEqyftklykTQIRELKEESDEKVklyKDAQQRIEDLQEERDSLASQL--------- 903
Cdd:pfam12128  470 DERIERAREEQEAANAEVERLQSEL--------RQARKRRDQASEAL---RQASRRLEERQSALDELELQLfpqagtllh 538
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  904 ---------EVSLTK-ADSEQLAR-----ITVEEQYSD--------LEKEKI------MKELEIKDMIARHRQDLAEKDG 954
Cdd:pfam12128  539 flrkeapdwEQSIGKvISPELLHRtdldpEVWDGSVGGelnlygvkLDLKRIdvpewaASEEELRERLDKAEEALQSARE 618
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  955 TINSLEESNRTLTVDVANLaseKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLaEVMKKTD 1034
Cdd:pfam12128  619 KQAAAEEQLVQANGELEKA---SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-EAQLKQL 694
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1035 GRPHQINNTDIRRKEKEIR-QLQLQLRTEKEKLNHSIIKYQREINDMQ-AMIAEESQVRLEMQMSLDSKDSDIERL 1108
Cdd:pfam12128  695 DKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLALLKAAIAARRsGAKAELKALETWYKRDLASLGVDPDVI 770
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
516-1124 1.48e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  516 RLLEN--EVSSLKEQLAELKKknQISHLSAEKNIHLERQleevsaKLQAELEESERLKkAQIEAFRQSQQLELS---LRE 590
Cdd:COG4913    229 ALVEHfdDLERAHEALEDARE--QIELLEPIRELAERYA------AARERLAELEYLR-AALRLWFAQRRLELLeaeLEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  591 LQERLAQLENSRLVLEQDKLSLQTSL-ELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSkaevekrQLQEDLTTLE 669
Cdd:COG4913    300 LRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRA-------RLEALLAALG 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  670 KEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADnnkinqsIEAKSETLKDmehklleersAKQQLENRLMQLEKEN 749
Cdd:COG4913    373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAE-------AEAALRDLRR----------ELRELEAEIASLERRK 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  750 SVLDCDYKQAKHELQELRSLKEnltEQV----EVLNVRVQQE-----------TQRKTLC--QGDLKVQRQEINSLRsse 812
Cdd:COG4913    436 SNIPARLLALRDALAEALGLDE---AELpfvgELIEVRPEEErwrgaiervlgGFALTLLvpPEHYAAALRWVNRLH--- 509
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 qqLKQELNHLLELKLTLEKQNQELSK------------------ERE----------ESEKQLK---------------- 848
Cdd:COG4913    510 --LRGRLVYERVRTGLPDPERPRLDPdslagkldfkphpfrawlEAElgrrfdyvcvDSPEELRrhpraitragqvkgng 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  849 ---EMKDQ-LEAEQYFT--------KLYKTQIRELKEESDEkvklykdAQQRIEDLQEERDSLASQLEV--SLTKADSEQ 914
Cdd:COG4913    588 trhEKDDRrRIRSRYVLgfdnraklAALEAELAELEEELAE-------AEERLEALEAELDALQERREAlqRLAEYSWDE 660
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  915 LARITVEEQYSDLEKEKimKELE--------IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKH 986
Cdd:COG4913    661 IDVASAEREIAELEAEL--ERLDassddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  987 IQQKLEKIKEEE-----------KQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKK---------TDGRP--------- 1037
Cdd:COG4913    739 AEDLARLELRALleerfaaalgdAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetADLDAdleslpeyl 818
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1038 ---HQINNTDIRRKEKEIRQLQLQL-RTEKEKLNHSI------IKYQ-REINDMQAMIA--EESQVRLEMQmslDSKDSD 1104
Cdd:COG4913    819 allDRLEEDGLPEYEERFKELLNENsIEFVADLLSKLrraireIKERiDPLNDSLKRIPfgPGRYLRLEAR---PRPDPE 895
                          730       740
                   ....*....|....*....|
gi 1207153289 1105 IERLRSQLTSLSIHSLDTTS 1124
Cdd:COG4913    896 VREFRQELRAVTSGASLFDE 915
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
625-916 1.51e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.62  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  625 AGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKeknkqeidlsfKLKAVQQSLEQEEAEHKTTKARL 704
Cdd:COG4942     17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------RIAALARRIRALEQELAALEAEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  705 ADNNKINQSIEAKSETLKDMEHKLLeeRSA-KQQLENRLMQLEKENSVLdcdykQAKHELQELRSLKENLTEQVEVLNVR 783
Cdd:COG4942     86 AELEKEIAELRAELEAQKEELAELL--RALyRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYLAPARREQAEELRAD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  784 VQQetqrktlcqgdLKVQRQEINSLRSSEQQLKQELnhllelkltlEKQNQELSKEREESEKQLKEMKDQLEAEQyftkl 863
Cdd:COG4942    159 LAE-----------LAALRAELEAERAELEALLAEL----------EEERAALEALKAERQKLLARLEKELAELA----- 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  864 ykTQIRELKEESdekvklyKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLA 916
Cdd:COG4942    213 --AELAELQQEA-------EELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
148-277 1.69e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 58.94  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKYLYLVMEFMPGGDLvtltSNYDIPEEW-AQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:PHA03210   243 QKYDFDLYSFMYDEAF----DWKDRPLLKqTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFE 318
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGD 277
Cdd:PHA03210   319 KEREAFDYGWVGTVATNSPEILAGDG----YCEITDIWSCGLILLDMLSHD 365
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
82-280 1.80e-08

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 57.43  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFG------AVQLVRHKVSQQVYAMKQLSKfeMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVM 155
Cdd:cd05044      1 KFLGSGAFGevfegtAKDILGDGSGETKVAVKTLRK--GATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDLVT-LTSNYDIPEEWAQFYTAEVV-LALDA------IHSLGFIHRDIKPDNMLLDRNGH----LKLADFGTCM 223
Cdd:cd05044     79 ELMEGGDLLSyLRAARPTAFTPPLLTLKDLLsICVDVakgcvyLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLAR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  224 KMDSTGMVRCDTAVGTP-DYISPEVLMSqggtGYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05044    159 DIYKNDYYRKEGEGLLPvRWMAPESLVD----GVFTTQSDVWAFGVLMWEILtLGQQPY 213
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
138-280 1.82e-08

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 57.66  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  138 IVQLCCAFQDEKYLYLVMEFM-----------PGGdlvtlTSNYDIpeewaQFYTAEVVLALDAIHSLGFIHRDIKPDNM 206
Cdd:cd07870     60 IVLLHDIIHTKETLTFVFEYMhtdlaqymiqhPGG-----LHPYNV-----RLFMFQLLRGLAYIHGQHILHRDLKPQNL 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  207 LLDRNGHLKLADFGtcmkMDSTGMVRCDT---AVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd07870    130 LISYLGELKLADFG----LARAKSIPSQTyssEVVTLWYRPPDVLL---GATDYSSALDIWGAGCIFIEMLQGQPAF 199
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
582-919 1.93e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 58.98  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  582 QQLELSLRELQERLAQLENSRLVLEQDKLSLqtslELEKRERNAGSETI----TDLQGRIYG--------LEGELKHIKS 649
Cdd:pfam17380  280 HQKAVSERQQQEKFEKMEQERLRQEKEEKAR----EVERRRKLEEAEKArqaeMDRQAAIYAeqermameRERELERIRQ 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  650 SLSKAEVEKRQLQE---------DLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKInqsiEAKSET 720
Cdd:pfam17380  356 EERKRELERIRQEEiameisrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI----RAEQEE 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  721 LKDMEHKLLEERSAKQQLENRLMQLEKEnsvldcdykqakhelqelrslkenltEQVEVLNvrvQQETQRKtlcQGDLKV 800
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQERQ--------------------------QQVERLR---QQEEERK---RKKLEL 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  801 QRQEINSLRSSEQQ---LKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQyftKLYKTQIRELKEESDE 877
Cdd:pfam17380  480 EKEKRDRKRAEEQRrkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE---ERRKQQEMEERRRIQE 556
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  878 KVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARIT 919
Cdd:pfam17380  557 QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPIT 598
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
108-340 2.20e-08

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 56.85  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  108 QLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDE--KYLYLVMEFMPGGDLVTLTSNYDIPEE-----WAQfy 180
Cdd:cd13983     35 KLRKLPKAERQR---FKQEIEILKSLKHPNIIKFYDSWESKskKEVIFITELMTSGTLKQYLKRFKRLKLkviksWCR-- 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  181 taEVVLALDAIHSLG--FIHRDIKPDNMLLDRN-GHLKLADFGTCMKMDSTGMVRCdtaVGTPDYISPEvlMSQGGtgyY 257
Cdd:cd13983    110 --QILEGLNYLHTRDppIIHRDLKCDNIFINGNtGEVKIGDLGLATLLRQSFAKSV---IGTPEFMAPE--MYEEH---Y 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  258 GRECDWWSVGVFIYELLVGDTPfYSE--SLVGTYGKIMdhknSLTFPDDIE--MSKNAKDLICAFLSSREVRLgrTGVDE 333
Cdd:cd13983    180 DEKVDIYAFGMCLLEMATGEYP-YSEctNAAQIYKKVT----SGIKPESLSkvKDPELKDFIEKCLKPPDERP--SAREL 252

                   ....*..
gi 1207153289  334 IKcHPFF 340
Cdd:cd13983    253 LE-HPFF 258
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
431-787 2.25e-08

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 58.82  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  431 SNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAG- 509
Cdd:COG5185    217 SESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKe 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 --LETDRKRLLENEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSaKLQAELEESERLKKAQIEAFRQSQQLELS 587
Cdd:COG5185    297 kiAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIE-QGQESLTENLEAIKEEIENIVGEVELSKS 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  588 LRELQERLAQLENSRLVLEQDKlslQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTT 667
Cdd:COG5185    376 SEELDSFKDTIESTKESLDEIP---QNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNK 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  668 LEKE-KNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNnkiNQSIEAKSETLKD-MEHKLLEERSAKQQLENRLMQL 745
Cdd:COG5185    453 VMREaDEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR---VSTLKATLEKLRAkLERQLEGVRSKLDQVAESLKDF 529
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  746 EKENsvlDCDYKQAKHELQELRSLKENL----TEQVEVLNVRVQQE 787
Cdd:COG5185    530 MRAR---GYAHILALENLIPASELIQASnaktDGQAANLRTAVIDE 572
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
61-280 2.30e-08

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 56.96  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   61 YEKAVCNLKELQVKLDdfdrvKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrSDSAFFwEERDIMAFSQSPWIVQ 140
Cdd:cd05073      1 WEKDAWEIPRESLKLE-----KKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM---SVEAFL-AEANVMKTLQHDKLVK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  141 LCCAFQDEKyLYLVMEFMPGGDLVTLTSNYD---IPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLA 217
Cdd:cd05073     71 LHAVVTKEP-IYIITEFMAKGSLLDFLKSDEgskQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  218 DFGTCMKMDSTGMVRCDTAVGTPDYISPEVLmsqgGTGYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05073    150 DFGLARVIEDNEYTAREGAKFPIKWTAPEAI----NFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
188-276 2.34e-08

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 57.01  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  188 LDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCmKMDSTGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVG 267
Cdd:cd07844    111 LAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA-RAKSVPSKTYSNEVVTLWYRPPDVLL---GSTEYSTSLDMWGVG 186

                   ....*....
gi 1207153289  268 VFIYELLVG 276
Cdd:cd07844    187 CIFYEMATG 195
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
447-874 2.37e-08

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 58.83  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  447 HEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRT---QSVRKAGLETDRKRLLENEVS 523
Cdd:TIGR00618  425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVVLARLLELQEEPC 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  524 SLKEQLAELKKKNQISHLSA----------EKNIHLERQLEEVSAKLQAELEESERLKkAQIEAFRQSQQLELSLRelQE 593
Cdd:TIGR00618  505 PLCGSCIHPNPARQDIDNPGpltrrmqrgeQTYAQLETSEEDVYHQLTSERKQRASLK-EQMQEIQQSFSILTQCD--NR 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  594 RLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRI--YGLEGELKHIKSSLSKAEVEKRQLQEDLTtleke 671
Cdd:TIGR00618  582 SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlQDVRLHLQQCSQELALKLTALHALQLTLT----- 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  672 KNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLEN----RLMQLEK 747
Cdd:TIGR00618  657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAA 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  748 ENSVLDCDYKQAKHE----LQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLL 823
Cdd:TIGR00618  737 REDALNQSLKELMHQartvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  824 ELKLTLEKQNQE---------------------LSKEREESEKQLKE-MKDQLEAEQYFTKL-YKTQIRELKEE 874
Cdd:TIGR00618  817 DILNLQCETLVQeeeqflsrleeksatlgeithQLLKYEECSKQLAQlTQEQAKIIQLSDKLnGINQIKIQFDG 890
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
82-284 2.53e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 56.80  E-value: 2.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVQLVRHKVSQQ---VYAMKQLSKFEMVK-RSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05066     10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKqRRD---FLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDipeewAQFYTAEVVLALDAIHS-------LGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGM 230
Cdd:cd05066     87 MENGSLDAFLRKHD-----GQFTVIQLVGMLRGIASgmkylsdMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPE 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  231 VRCDTAVGT-P-DYISPEVLMSQGgtgyYGRECDWWSVGVFIYELL-VGDTPFYSES 284
Cdd:cd05066    162 AAYTTRGGKiPiRWTAPEAIAYRK----FTSASDVWSYGIVMWEVMsYGERPYWEMS 214
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
68-280 2.65e-08

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 56.85  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   68 LKELQVKLDDFDRVKLIGRGAFGAV---QLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCC- 143
Cdd:cd05074      1 LKDVLIQEQQFTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVIKLIGv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  144 -----AFQDEKYLYLVMEFMPGGDLVT--LTSN-----YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRN 211
Cdd:cd05074     80 slrsrAKGRLPIPMVILPFMKHGDLHTflLMSRigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  212 GHLKLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMSQggtgYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05074    160 MTVCVADFGLSKKIYSGDYYRQGCASKLPvKWLALESLADN----VYTTHSDVWAFGVTMWEIMTrGQTPY 226
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
81-289 2.73e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 56.92  E-value: 2.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQL--VRHKVSQQVYAMKQLSKFEMVKrsDSAFFWEERDIMAFSQSPWIVQlCCAFQDEKYLYL-VMEF 157
Cdd:cd05087      2 LKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASVQ--DQMQFLEEAQPYRALQHTNLLQ-CLAQCAEVTPYLlVMEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVTLTSNYDIPEEWA------QFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGM 230
Cdd:cd05087     79 CPLGDLKGYLRSCRAAESMApdpltlQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGlSHCKYKEDYF 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  231 VRCDTAVGTPDYISPEVLMSQGGTGYY---GRECDWWSVGVFIYELL-VGDTPF--YSESLVGTY 289
Cdd:cd05087    159 VTADQLWVPLRWIAPELVDEVHGNLLVvdqTKQSNVWSLGVTIWELFeLGNQPYrhYSDRQVLTY 223
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
81-280 2.88e-08

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 56.99  E-value: 2.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVYAMK--QLSKF--EMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQ-DEKYLYLVM 155
Cdd:cd14040     11 LHLLGRGGFSEVYKAFDLYEQRYAAVKihQLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  156 EFMPGGDL-VTLTSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLL---DRNGHLKLADFGTCMKMDST- 228
Cdd:cd14040     91 EYCEGNDLdFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDs 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  229 ----GMVRCDTAVGTPDYISPEVLMSQGGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14040    171 ygvdGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF 226
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
81-283 3.07e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 56.95  E-value: 3.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQ----QVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQL--CCAFQDEKYLYLV 154
Cdd:cd14205      9 LQQLGKGNFGSVEMCRYDPLQdntgEVVAVKKLQHSTEEHLRD---FEREIEILKSLQHDNIVKYkgVCYSAGRRNLRLI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  155 MEFMPGGDLVTLTSNYDIPEEWAQF--YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG--TCMKMDSTGM 230
Cdd:cd14205     86 MEYLPYGSLRDYLQKHKERIDHIKLlqYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGltKVLPQDKEYY 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  231 VRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVgdtpfYSE 283
Cdd:cd14205    166 KVKEPGESPIFWYAPESLTESK----FSVASDVWSFGVVLYELFT-----YIE 209
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
347-404 3.44e-08

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 51.59  E-value: 3.44e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289   347 FDTI--RDTMAPVVPELSSDIDTSNFDDD-IKDDPIGTEtFPPPRAFAGNQLPFVGFTYFR 404
Cdd:smart00133    5 WDKLenKEIEPPFVPKIKSPTDTSNFDPEfTEETPVLTP-VDSPLSGGIQQEPFRGFSYVF 64
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
81-280 3.83e-08

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 56.18  E-value: 3.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVR-H--------KVSQQVYAMKQLSKFEM-----VKRSDSAFFweerdiMAFSQSP---WIVQLCC 143
Cdd:cd14150      5 LKRIGTGSFGTVFRGKwHgdvavkilKVTEPTPEQLQAFKNEMqvlrkTRHVNILLF------MGFMTRPnfaIITQWCE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  144 AFQDEKYLYLV-MEFmpggDLVTLTsnyDIPEEWAQfytaevvlALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-T 221
Cdd:cd14150     79 GSSLYRHLHVTeTRF----DTMQLI---DVARQTAQ--------GMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGlA 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  222 CMKMDSTGMVRCDTAVGTPDYISPEVLMSQgGTGYYGRECDWWSVGVFIYELLVGDTPF 280
Cdd:cd14150    144 TVKTRWSGSQQVEQPSGSILWMAPEVIRMQ-DTNPYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
84-274 3.84e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 56.54  E-value: 3.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVR----HKVSQQVYAMKQ------LSKFEMVK-------RSDsafFWEERDIMAFSQSPWIVQLCCAFQ 146
Cdd:cd05095     13 LGEGQFGEVHLCEaegmEKFMDKDFALEVsenqpvLVAVKMLRadanknaRND---FLKEIKIMSRLKDPNIIRLLAVCI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMPGGDLVTLTSNYDIPEEWA-------------QFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH 213
Cdd:cd05095     90 TDDPLCMITEYMENGDLNQFLSRQQPEGQLAlpsnaltvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  214 LKLADFGTCMKMDSTGMVRCD-TAVGTPDYISPEVLMsqggTGYYGRECDWWSVGVFIYELL 274
Cdd:cd05095    170 IKIADFGMSRNLYSGDYYRIQgRAVLPIRWMSWESIL----LGKFTTASDVWAFGVTLWETL 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
659-1115 3.99e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  659 RQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKL--LEERSAKQ 736
Cdd:COG4717     49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  737 QLENRLMQLEKENSVLDCDYKQAKHELQELRSL---KENLTEQVEVLNVRVQQETQRKTL-CQGDLKVQRQEINSLRSSE 812
Cdd:COG4717    129 PLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRL 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  813 QQLKQELnhllelkltlekqnQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQ--------IRELkeesdekVKLYKD 884
Cdd:COG4717    209 AELEEEL--------------EEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaaLLAL-------LGLGGS 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  885 AQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNR 964
Cdd:COG4717    268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  965 TLTVDVANLASEKEELnnKLKHIQQkLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAE--VMKKTDGRPHQINN 1042
Cdd:COG4717    348 ELQELLREAEELEEEL--QLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEeqLEELLGELEELLEA 424
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1043 TDIRRKEKEIRQLQLQLRTEKEKLNhsiiKYQREINDMQAMIAEesqvrLEMQMSLDSKDSDIERLRSQLTSL 1115
Cdd:COG4717    425 LDEEELEEELEELEEELEELEEELE----ELREELAELEAELEQ-----LEEDGELAELLQELEELKAELREL 488
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
183-280 4.01e-08

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 55.86  E-value: 4.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  183 EVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGYYGREc 261
Cdd:cd14062     97 QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGlATVKTRWSGSQQFEQPTGSILWMAPEVIRMQDENPYSFQS- 175
                           90
                   ....*....|....*....
gi 1207153289  262 DWWSVGVFIYELLVGDTPF 280
Cdd:cd14062    176 DVYAFGIVLYELLTGQLPY 194
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
643-981 4.16e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 4.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  643 ELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLK 722
Cdd:COG4372     32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  723 DMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTlcQGDLKVQR 802
Cdd:COG4372    112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA--EQALDELL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  803 QEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEkQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLY 882
Cdd:COG4372    190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL-GLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  883 KDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDGTINSLEES 962
Cdd:COG4372    269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
                          330
                   ....*....|....*....
gi 1207153289  963 NRTLTVDVANLASEKEELN 981
Cdd:COG4372    349 GLLDNDVLELLSKGAEAGV 367
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
552-1115 5.00e-08

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 58.06  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  552 QLEEVSAKLQAELEESERLKKaQIEAFRQSQQLELSLRELQERLAQLENSRLVlEQDKLSLQTSLELEKRERnagsetit 631
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKK-LIEETENLAELIIDLEELKLQELKLKEQAKK-ALEYYQLKEKLELEEEYL-------- 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  632 dLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEiDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN 711
Cdd:pfam02463  227 -LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV-LKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  712 --QSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQ 789
Cdd:pfam02463  305 leRRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  790 RktlcQGDLKVQRQEINSLRSSEQQLKQELNHllelklTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIR 869
Cdd:pfam02463  385 R----LSSAAKLKEEELELKSEEEKEAQLLLE------LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  870 ELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIARHRQDL 949
Cdd:pfam02463  455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  950 AEKDGTINSLEESNRtlTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEV 1029
Cdd:pfam02463  535 GVAVENYKVAISTAV--IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1030 MKKTDGRPHQINNTDIRRKEKEIRQLQLQLRTEkeklnhsiikyQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLR 1109
Cdd:pfam02463  613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKE-----------SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681

                   ....*.
gi 1207153289 1110 SQLTSL 1115
Cdd:pfam02463  682 QEKAES 687
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
417-725 5.54e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 5.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  417 EEDIIEDHglnHTESNDLEKRLKKLEEKfkhEMQAKEELEnkcrianqRLEKLSKDlEEEVNARQEAEDNLRSLEKEkvl 496
Cdd:PRK03918   450 RKELLEEY---TAELKRIEKELKEIEEK---ERKLRKELR--------ELEKVLKK-ESELIKLKELAEQLKELEEK--- 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  497 lkhqrTQSVRKAGLETDRKrllenEVSSLKEQLAELKKKNQISHLSAEKNIHLERQLEEVSAKLQ-AELEESERLKKAQI 575
Cdd:PRK03918   512 -----LKKYNLEELEKKAE-----EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDeLEEELAELLKELEE 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  576 EAFRQSQQLELSLRELQE---RLAQLENSrlvlEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLS 652
Cdd:PRK03918   582 LGFESVEELEERLKELEPfynEYLELKDA----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  653 KAEVEKrqLQEDLTTLEKEKNKqeidLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDME 725
Cdd:PRK03918   658 EEEYEE--LREEYLELSRELAG----LRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
76-292 5.69e-08

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 56.16  E-value: 5.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAV--QLVRHKVSQQVYAMKQLSKFemVKRSDSAFFWEERDIMA-FSQSPWIVQLCCAFQDEKYLY 152
Cdd:cd05089      2 EDIKFEDVIGEGNFGQVikAMIKKDGLKMNAAIKMLKEF--ASENDHRDFAGELEVLCkLGHHPNIINLLGACENRGYLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLTSNYDIPEEWAQF-----------------YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLK 215
Cdd:cd05089     80 IAIEYAPYGNLLDFLRKSRVLETDPAFakehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  216 LADFGtcmkMDSTGMVRCDTAVGTpdyiSPEVLMSQGGTGY--YGRECDWWSVGVFIYELL-VGDTPFYSESLVGTYGKI 292
Cdd:cd05089    160 IADFG----LSRGEEVYVKKTMGR----LPVRWMAIESLNYsvYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKL 231
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
180-276 6.05e-08

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 56.08  E-value: 6.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  180 YTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGH-LKLADFGTCMKMDSTGMvrcdtavgTPD-----YISPEVLMsqgg 253
Cdd:cd14135    110 YAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSASDIGENEI--------TPYlvsrfYRAPEIIL---- 177
                           90       100
                   ....*....|....*....|....
gi 1207153289  254 tGY-YGRECDWWSVGVFIYELLVG 276
Cdd:cd14135    178 -GLpYDYPIDMWSVGCTLYELYTG 200
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
83-276 6.11e-08

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 55.34  E-value: 6.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   83 LIGRGAFGAVqlVRHKVSQQVYAMKQLSKfemvkRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLylVMEFMPGGD 162
Cdd:cd14068      1 LLGDGGFGSV--YRAVYRGEDVAVKIFNK-----HTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  163 LVTL--TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-----DRNGHLKLADFGTCMKMDSTGMVRCDt 235
Cdd:cd14068     72 LDALlqQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKTSE- 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207153289  236 avGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLVG 276
Cdd:cd14068    151 --GTPGFRAPEVAR---GNVIYNQQADVYSFGLLLYDILTC 186
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
434-938 6.23e-08

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 57.44  E-value: 6.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  434 LEKRLKKLEEKFKHEMQakeELENKCrianqrlEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLK---HQRTQSVRKAGL 510
Cdd:pfam05557   14 LQNEKKQMELEHKRARI---ELEKKA-------SALKRQLDRESDRNQELQKRIRLLEKREAEAEealREQAELNRLKKK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  511 ETDRKRLLENEVSSLKEQLAELK--KKNQISHL--SAEKNihlERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLEL 586
Cdd:pfam05557   84 YLEALNKKLNEKESQLADAREVIscLKNELSELrrQIQRA---ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  587 SLRELQERLAQLENsrlvLEQdKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLT 666
Cdd:pfam05557  161 QQSSLAEAEQRIKE----LEF-EIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  667 TLEKEKNKQEidlsfKLKAVQQSLEQEEAEHKTTKaRLADNNKIN-QSIEAKSETLKdmehklleersakqQLENRLMQL 745
Cdd:pfam05557  236 KLEREEKYRE-----EAATLELEKEKLEQELQSWV-KLAQDTGLNlRSPEDLSRRIE--------------QLQQREIVL 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  746 EKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNhllel 825
Cdd:pfam05557  296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELT----- 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  826 kltLEKQNQELSKEREESEKQLKEMKDQLEAEQYftklyktQIRELKEEsdekVKLYKDAQQRIEDLQEERDSLASQLEV 905
Cdd:pfam05557  371 ---MSNYSPQLLERIEEAEDMTQKMQAHNEEMEA-------QLSVAEEE----LGGYKQQAQTLERELQALRQQESLADP 436
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1207153289  906 SLTKADSEQLARI--TVEEQYSDLEKEKIMKELEI 938
Cdd:pfam05557  437 SYSKEEVDSLRRKleTLELERQRLREQKNELEMEL 471
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
78-285 6.53e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 56.19  E-value: 6.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffweERDIMAF-----SQSPWIVQLCCAFQDEKYLY 152
Cdd:cd14229      2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI----EVGILARlsnenADEFNFVRAYECFQHRNHTC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGG--DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLD---RNGHLKLADFGTCMKMD 226
Cdd:cd14229     78 LVFEMLEQNlyDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENiMLVDpvrQPYRVKVIDFGSASHVS 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  227 STgmvRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGdTPFYSESL 285
Cdd:cd14229    158 KT---VCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLYPGAL 208
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
656-933 6.62e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.44  E-value: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  656 VEKRQLQEDLTTLEKEKNKQEIDLsfKLKAVQQSLEQEEAEhkttKARLADNNKiNQSIEAKSETL-----KDMEHKLLE 730
Cdd:pfam17380  284 VSERQQQEKFEKMEQERLRQEKEE--KAREVERRRKLEEAE----KARQAEMDR-QAAIYAEQERMamereRELERIRQE 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  731 ER----------------SAKQQLENRLMQLEKENSVLDCDYKQA-KHELQELRSLKENLTEQVEVLNVRVQQETQRKTL 793
Cdd:pfam17380  357 ERkrelerirqeeiameiSRMRELERLQMERQQKNERVRQELEAArKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  794 CQGDLKVQRQEINSLRSSEQQLKQELnhLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRE--- 870
Cdd:pfam17380  437 VRRLEEERAREMERVRLEEQERQQQV--ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerk 514
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  871 ---LKEESDEKVKLYKDAQQRIEDLQEERdslaSQLEVSLTKADSEQLARITVEEQYSD-LEKEKIM 933
Cdd:pfam17380  515 rklLEKEMEERQKAIYEEERRREAEEERR----KQQEMEERRRIQEQMRKATEERSRLEaMEREREM 577
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
82-280 6.63e-08

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 55.78  E-value: 6.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVqlVRHKVSQQVYAMK---QLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQL--CCAFQDEKYLY---- 152
Cdd:cd05075      6 KTLGEGEFGSV--MEGQLNQDDSVLKvavKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLigVCLQNTESEGYpspv 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTL-------TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd05075     84 VILPFMKHGDLHSFllysrlgDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  226 DSTGMVRCDTAVGTP-DYISPEVLMSQggtgYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05075    164 YNGDYYRQGRISKMPvKWIAIESLADR----VYTTKSDVWSFGVTMWEIATrGQTPY 216
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
79-280 7.38e-08

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 55.47  E-value: 7.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   79 DRVKLI---GRGAFGAVQ--LVRH----KVSQQVyAMKQLSkfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQDEK 149
Cdd:cd05036      6 KNLTLIralGQGAFGEVYegTVSGmpgdPSPLQV-AVKTLP--ELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVV-LALDA------IHSLGFIHRDIKPDNMLLDRNGH---LKLAD 218
Cdd:cd05036     83 PRFILLELMAGGDLKSfLRENRPRPEQPSSLTMLDLLqLAQDVakgcryLEENHFIHRDIAARNCLLTCKGPgrvAKIGD 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  219 FGtcMKMDstgMVRCD------TAVGTPDYISPEVLMSqggtGYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05036    163 FG--MARD---IYRADyyrkggKAMLPVKWMPPEAFLD----GIFTSKTDVWSFGVLLWEIFsLGYMPY 222
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
759-983 8.67e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.31  E-value: 8.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  759 AKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSK 838
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  839 EREESEKQLKEMKDQLEaeqyftKLYKTQIRELKEESDEKVKLYKDA----------QQRIEDLQEERDSLASQLEVSLT 908
Cdd:COG4942     98 ELEAQKEELAELLRALY------RLGRQPPLALLLSPEDFLDAVRRLqylkylaparREQAEELRADLAELAALRAELEA 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  909 KADSEQLARITVEEQYSDLEKEKIMKEleikDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNK 983
Cdd:COG4942    172 ERAELEALLAELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
238-340 9.16e-08

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 54.74  E-value: 9.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  238 GTPDYISPEVLMSQGGtgYYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKImdHKNSLTFPDDIemSKNAKDLICA 317
Cdd:cd13976    148 GCPAYVSPEILNSGAT--YSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKI--RRGQFAIPETL--SPRARCLIRS 221
                           90       100
                   ....*....|....*....|...
gi 1207153289  318 FLssREVRLGRTGVDEIKCHPFF 340
Cdd:cd13976    222 LL--RREPSERLTAEDILLHPWL 242
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
77-280 9.35e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 55.79  E-value: 9.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKL-----IGRGAFG------AVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAF 145
Cdd:cd05101     20 EFPRDKLtlgkpLGEGCFGqvvmaeAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGAC 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  146 QDEKYLYLVMEFMPGGDL---------VTLTSNYDI---PEEWAQFY-----TAEVVLALDAIHSLGFIHRDIKPDNMLL 208
Cdd:cd05101    100 TQDGPLYVIVEYASKGNLreylrarrpPGMEYSYDInrvPEEQMTFKdlvscTYQLARGMEYLASQKCIHRDLAARNVLV 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  209 DRNGHLKLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMSQggtgYYGRECDWWSVGVFIYELL-VGDTPF 280
Cdd:cd05101    180 TENNVMKIADFGLARDINNIDYYKKTTNGRLPvKWMAPEALFDR----VYTHQSDVWSFGVLMWEIFtLGGSPY 249
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
705-1121 1.01e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  705 ADNN--KINQSIEAKSETLKDmehklleERSAKQQLENRLMQLEKEnsvldcdYKQAKHELQELRSLKENLTEQVEVLNV 782
Cdd:PRK03918   163 AYKNlgEVIKEIKRRIERLEK-------FIKRTENIEELIKEKEKE-------LEEVLREINEISSELPELREELEKLEK 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  783 RVQqetqrktlcqgDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKD-QLEAEQY-- 859
Cdd:PRK03918   229 EVK-----------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEYik 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  860 ---FTKLYKTQIRELKEES----------DEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEE---- 922
Cdd:PRK03918   298 lseFYEEYLDELREIEKRLsrleeeingiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerl 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  923 --QYSDLEKEKIMKELE---------------IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASE-KEELNNK- 983
Cdd:PRK03918   378 kkRLTGLTPEKLEKELEelekakeeieeeiskITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhRKELLEEy 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  984 ---LKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKtlKIQAINKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLR 1060
Cdd:PRK03918   458 taeLKRIEKELKEIEEKERKLRKELRELEKVLKKES--ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289 1061 tekeKLNHSIIKYQREINDMQAMIAEesqvRLEMQMSLDSKDSDIERLRSQLTSLSIHSLD 1121
Cdd:PRK03918   536 ----KLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESVE 588
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
102-284 1.13e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 55.02  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  102 QVYAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDL------------VTLTSN 169
Cdd:cd05090     35 QLVAIKTLKDYNNPQQWNE--FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLheflimrsphsdVGCSSD 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  170 YD----IPEEWAQFY--TAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTP-DY 242
Cdd:cd05090    113 EDgtvkSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPiRW 192
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207153289  243 ISPEVLMsqggTGYYGRECDWWSVGVFIYELL-VGDTPFYSES 284
Cdd:cd05090    193 MPPEAIM----YGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFS 231
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
73-284 1.15e-07

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 55.16  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   73 VKLDDFDRVKLIGRGAFGAVQLVR-HKVSQQ----VYAMKQLSkfEMVKRSDSAFFWEERDIMAFSQSPWIVQLCCAFQD 147
Cdd:cd05049      2 IKRDTIVLKRELGEGAFGKVFLGEcYNLEPEqdkmLVAVKTLK--DASSPDARKDFEREAELLTNLQHENIVKFYGVCTE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKYLYLVMEFMPGGDL-----------VTLTSNYDIPEEWAQFYTAEVVL----ALDAIHSLGFIHRDIKPDNMLLDRNG 212
Cdd:cd05049     80 GDPLLMVFEYMEHGDLnkflrshgpdaAFLASEDSAPGELTLSQLLHIAVqiasGMVYLASQHFVHRDLATRNCLVGTNL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  213 HLKLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMsqggtgyYGR---ECDWWSVGVFIYELLV-GDTPFYSES 284
Cdd:cd05049    160 VVKIGDFGMSRDIYSTDYYRVGGHTMLPiRWMPPESIL-------YRKfttESDVWSFGVVLWEIFTyGKQPWFQLS 229
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
187-293 1.37e-07

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 55.24  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  187 ALDAIHSLGFIHRDIKPDNMLLDRNGH--LKLADFGT-CM---KMDStgmvrcdtavgtpdYI------SPEVLMSQGgt 254
Cdd:cd14210    128 ALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSsCFegeKVYT--------------YIqsrfyrAPEVILGLP-- 191
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1207153289  255 gyYGRECDWWSVGVFIYELLVGDTPFYSESLVGTYGKIM 293
Cdd:cd14210    192 --YDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIM 228
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
78-304 1.53e-07

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 54.98  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   78 FDRVKLIGRGAFGAVQLVRHKVSQ--QVYAMKQL--SKFEMVKRSDSAFfweeRDIMAFS--QSPWIVQLCCAFQD--EK 149
Cdd:cd07842      2 YEIEGCIGRGTYGRVYKAKRKNGKdgKEYAIKKFkgDKEQYTGISQSAC----REIALLRelKHENVVSLVEVFLEhaDK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFmpggdlvtltSNYDIpeeWA--QFYTAEVVLA-------------LDAIHSLG---FIHRDIKPDNMLL--- 208
Cdd:cd07842     78 SVYLLFDY----------AEHDL---WQiiKFHRQAKRVSippsmvksllwqiLNGIHYLHsnwVLHRDLKPANILVmge 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  209 -DRNGHLKLADFGTCMKMDS--TGMVRCDTAVGTPDYISPEVLMsqgGTGYYGRECDWWSVGVFIYELLV------GD-- 277
Cdd:cd07842    145 gPERGVVKIGDLGLARLFNAplKPLADLDPVVVTIWYRAPELLL---GARHYTKAIDIWAIGCIFAELLTlepifkGRea 221
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  278 -----TPFYSESLvgtyGKIMDHknsLTFPDD 304
Cdd:cd07842    222 kikksNPFQRDQL----ERIFEV---LGTPTE 246
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
548-1127 2.00e-07

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.89  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  548 HLERQLEEVSAK---LQAELEESERLKKAQieafrqsqqlelslrelqerlaqlensRLVLEQDKLSLQTSLELEKRERN 624
Cdd:pfam15921   75 HIERVLEEYSHQvkdLQRRLNESNELHEKQ---------------------------KFYLRQSVIDLQTKLQEMQMERD 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  625 AgsetITDLQGRiyglegelkhikSSLSKAEVeKRQLQEDLTTLEKEKNKQE---IDLSFKLKAVQQSLEQEEAEHKTTK 701
Cdd:pfam15921  128 A----MADIRRR------------ESQSQEDL-RNQLQNTVHELEAAKCLKEdmlEDSNTQIEQLRKMMLSHEGVLQEIR 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  702 ARLADNNKINQSIEAKSETLKDMEHklleeRSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENlteQVEVLn 781
Cdd:pfam15921  191 SILVDFEEASGKKIYEHDSMSTMHF-----RSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQN---KIELL- 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  782 VRVQQETQRKTLCQGDLKVQ---------RQEINSLRSSEQQLK-QELNHLLELKLTLEKQNQELSKEREESEKQLKEMK 851
Cdd:pfam15921  262 LQQHQDRIEQLISEHEVEITgltekassaRSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  852 DQLEAEQYFTKLYKTQIRELKEESD----EKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDL 927
Cdd:pfam15921  342 DKIEELEKQLVLANSELTEARTERDqfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  928 EKEKI-MKELE--IKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSL 1004
Cdd:pfam15921  422 DDRNMeVQRLEalLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1005 TVSYEkqiqvEKTLKIQAINklAEVMK-------KTDGRPHQINNTD-IRRKEKEIRQLQLQLrTEKEKLNHsIIKYQRE 1076
Cdd:pfam15921  502 TASLQ-----EKERAIEATN--AEITKlrsrvdlKLQELQHLKNEGDhLRNVQTECEALKLQM-AEKDKVIE-ILRQQIE 572
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289 1077 iNDMQ----------AMIAEESQV-------RLEMQ---MSLDSKDSDIERLRSQLTSLSIHSLDTTSISS 1127
Cdd:pfam15921  573 -NMTQlvgqhgrtagAMQVEKAQLekeindrRLELQefkILKDKKDAKIRELEARVSDLELEKVKLVNAGS 642
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
149-284 2.25e-07

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 54.42  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGGDLVTLTSNydIPEEW-AQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL--DRNG--HLKLADFGTCM 223
Cdd:cd14018    113 RTLFLVMKNYPCTLRQYLWVN--TPSYRlARVMILQLLEGVDHLVRHGIAHRDLKSDNILLelDFDGcpWLVIADFGCCL 190
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207153289  224 KMDSTGMvRCDTavgTPDYIS---------PEVLMSQGGTGY---YGReCDWWSVGVFIYELLVGDTPFYSES 284
Cdd:cd14018    191 ADDSIGL-QLPF---SSWYVDrggnaclmaPEVSTAVPGPGVvinYSK-ADAWAVGAIAYEIFGLSNPFYGLG 258
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
81-221 2.26e-07

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 54.27  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVR-HKVSQQVYAMKQLSKFE------MVK--RSDSAF-----FWEERDIMAFSQSPWIVQLCCAFQ 146
Cdd:cd05051     10 VEKLGEGQFGEVHLCEaNGLSDLTSDDFIGNDNKdepvlvAVKmlRPDASKnaredFLKEVKIMSQLKDPNIVRLLGVCT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  147 DEKYLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIH-------------SLGFIHRDIKPDNMLLDRNGH 213
Cdd:cd05051     90 RDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKTLSYGTLLYmatqiasgmkyleSLNFVHRDLATRNCLVGPNYT 169

                   ....*...
gi 1207153289  214 LKLADFGT 221
Cdd:cd05051    170 IKIADFGM 177
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
82-280 2.36e-07

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 54.08  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAV---QLVRHKVSQQVYAMKQLsKFEMVKRSDSAFFWEERDIMAFSQSPWIVQL---CCAFQDEKYL---Y 152
Cdd:cd05035      5 KILGEGEFGSVmeaQLKQDDGSQLKVAVKTM-KVDIHTYSEIEEFLSEAACMKDFDHPNVMRLigvCFTASDLNKPpspM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTL-------TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd05035     84 VILPFMKHGDLHSYllysrlgGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  226 DSTGMVRCDTAVGTP-DYISPEVLMSQggtgYYGRECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05035    164 YSGDYYRQGRISKMPvKWIALESLADN----VYTSKSDVWSFGVTMWEIATrGQTPY 216
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
736-907 2.37e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 53.39  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  736 QQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSE--Q 813
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  814 QLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEqyftklyKTQIRELKEESDEKVklyKDAQQRIEDLQ 893
Cdd:COG1579     93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELDEEL---AELEAELEELE 162
                          170
                   ....*....|....
gi 1207153289  894 EERDSLASQLEVSL 907
Cdd:COG1579    163 AEREELAAKIPPEL 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
550-780 2.63e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 2.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  550 ERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLElSLRELQERLAQLENSRLVLEQDKLSL-----QTSLELEKRERN 624
Cdd:COG4913    220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  625 AGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQ--------LQEDLTTLEKEKNKQEIdlsfKLKAVQQSLEQEEAE 696
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERER----RRARLEALLAALGLP 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  697 HKTTKARLADNNkinQSIEAKSETLKDMEHKLLEERSakqQLENRLMQLEKEnsvldcdYKQAKHELQELRSLKENLTEQ 776
Cdd:COG4913    375 LPASAEEFAALR---AEAAALLEALEEELEALEEALA---EAEAALRDLRRE-------LRELEAEIASLERRKSNIPAR 441

                   ....
gi 1207153289  777 VEVL 780
Cdd:COG4913    442 LLAL 445
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
433-768 2.69e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 54.90  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEkvllkhQRTQSVRKAGLET 512
Cdd:pfam07888   77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED------IKTLTQRVLERET 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLLENEvsslkEQLAELKKKNQishlsAEKNiHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQ 592
Cdd:pfam07888  151 ELERMKERA-----KKAGAQRKEEE-----AERK-QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  593 ERLAQLENSRLVLEQDKLSLQTSlelekRERNAGSE-TITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLqedlttleke 671
Cdd:pfam07888  220 QKLTTAHRKEAENEALLEELRSL-----QERLNASErKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL---------- 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  672 kNKQEIDLSFKLKAVQQSLEQEeaehKTTKARLADNNKinQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSV 751
Cdd:pfam07888  285 -TLQLADASLALREGRARWAQE----RETLQQSAEADK--DRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRV 357
                          330
                   ....*....|....*..
gi 1207153289  752 LDCdykQAKHELQELRS 768
Cdd:pfam07888  358 QLS---ESRRELQELKA 371
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
150-289 2.80e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 54.10  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  150 YLYLVMEFMPGGDLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL-DRNGH--LKLADFGTCMKMD 226
Cdd:cd13977    109 YLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILIsHKRGEpiLKVADFGLSKVCS 188
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  227 STGMV----------RCDTAVGTPDYISPEVLmsqggTGYYGRECDWWSVGVFIYELLVGDTPFYSES---LVGTY 289
Cdd:cd13977    189 GSGLNpeepanvnkhFLSSACGSDFYMAPEVW-----EGHYTAKADIFALGIIIWAMVERITFRDGETkkeLLGTY 259
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
433-622 2.86e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKhEMQAKE---ELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAG 509
Cdd:COG3206    186 ELRKELEEAEAALE-EFRQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 LETDRKRLLEnevssLKEQLAELKKKNQISHLSAeknIHLERQLEEVSAKLQAELEESERLKKAQIEAFR-QSQQLELSL 588
Cdd:COG3206    265 IQQLRAQLAE-----LEAELAELSARYTPNHPDV---IALRAQIAALRAQLQQEAQRILASLEAELEALQaREASLQAQL 336
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207153289  589 RELQERLAQL---ENSRLVLEQDKLSLQTSLE--LEKRE 622
Cdd:COG3206    337 AQLEARLAELpelEAELRRLEREVEVARELYEslLQRLE 375
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
640-905 3.23e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.02  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  640 LEGELKHIKSSLSKAEVEKRQLQEDlttlekeknKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSE 719
Cdd:COG3206    180 LEEQLPELRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  720 TLKDMEHKLLEErSAKQQLENRLMQLEKENSVLDCDYkQAKH-ELQELRslkenltEQVEVLNVRVQQETQRKtlcqgdL 798
Cdd:COG3206    251 SGPDALPELLQS-PVIQQLRAQLAELEAELAELSARY-TPNHpDVIALR-------AQIAALRAQLQQEAQRI------L 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  799 KVQRQEINSLRSSEQQLKQELnhllelkltlekqnqelskerEESEKQLKEMKdQLEAEqyftklyktqIRELKEESDEK 878
Cdd:COG3206    316 ASLEAELEALQAREASLQAQL---------------------AQLEARLAELP-ELEAE----------LRRLEREVEVA 363
                          250       260
                   ....*....|....*....|....*..
gi 1207153289  879 VKLYKDAQQRIEDLQEERDSLASQLEV 905
Cdd:COG3206    364 RELYESLLQRLEEARLAEALTVGNVRV 390
PRK01156 PRK01156
chromosome segregation protein; Provisional
438-1032 3.62e-07

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 54.91  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  438 LKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEvnarqeaEDNLRSLEKEKvllkhqrtqsvRKAGLETDRKrl 517
Cdd:PRK01156   171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADD-------EKSHSITLKEI-----------ERLSIEYNNA-- 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  518 lENEVSSLKEQLaelkkkNQISHLSAEKNiHLERQLEEVSAKLQAELEE-------SERLKKAQIEAFRQSQQlelSLRE 590
Cdd:PRK01156   231 -MDDYNNLKSAL------NELSSLEDMKN-RYESEIKTAESDLSMELEKnnyykelEERHMKIINDPVYKNRN---YIND 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  591 LQERLAQLENSRLVLEQDKLSLQTSLELEKR--ERNAGSETITDLQGRIygleGELKHIKSSLSKAEVEKRQLQEDLTTL 668
Cdd:PRK01156   300 YFKYKNDIENKKQILSNIDAEINKYHAIIKKlsVLQKDYNDYIKKKSRY----DDLNNQILELEGYEMDYNSYLKSIESL 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  669 EKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLadnNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKE 748
Cdd:PRK01156   376 KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL---NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  749 NSVLDC--------------DYKQAKHELQElrSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQ 814
Cdd:PRK01156   453 SVCPVCgttlgeeksnhiinHYNEKKSRLEE--KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  815 LKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDqlEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQE 894
Cdd:PRK01156   531 LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT--SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEI 608
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  895 ERDSLASQLEVSLTKADSEQLariTVEEQYSDLEKEKIMKElEIKDMIARHRQDLAEKDGTINSLEEsnrtltvdvanLA 974
Cdd:PRK01156   609 GFPDDKSYIDKSIREIENEAN---NLNNKYNEIQENKILIE-KLRGKIDNYKKQIAEIDSIIPDLKE-----------IT 673
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  975 SEKEELNNKLKHIQQKLEKIKEEEKQMKSlTVSYEKQIQVEKTLKIQAINKLAEVMKK 1032
Cdd:PRK01156   674 SRINDIEDNLKKSRKALDDAKANRARLES-TIEILRTRINELSDRINDINETLESMKK 730
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
76-282 3.74e-07

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 53.68  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHK--VSQQVYAMKQLskfEMVKRSDSAF----FWEERDIMAFSQSPWIVQL--CCAFQd 147
Cdd:cd05050      5 NNIEYVRDIGQGAFGRVFQARAPglLPYEPFTMVAV---KMLKEEASADmqadFQREAALMAEFDHPNIVKLlgVCAVG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 eKYLYLVMEFMPGGDLVT-LTSNYDIPEEWAQFYTAEVV------LALDAIHSLG----------------FIHRDIKPD 204
Cdd:cd05050     81 -KPMCLLFEYMAYGDLNEfLRHRSPRAQCSLSHSTSSARkcglnpLPLSCTEQLCiakqvaagmaylserkFVHRDLATR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  205 NMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVGTP-DYISPEVLMsqggTGYYGRECDWWSVGVFIYELL-VGDTPFYS 282
Cdd:cd05050    160 NCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPiRWMPPESIF----YNRYTTESDVWAYGVVLWEIFsYGMQPYYG 235
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
522-1028 3.80e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  522 VSSLKEQLAELKKKNqishlsAEKNIHLERQLEEVSAKLQAELEESERLkkaqieafrqsQQLELSLRELQERLAQLENS 601
Cdd:COG4717     48 LERLEKEADELFKPQ------GRKPELNLKELKELEEELKEAEEKEEEY-----------AELQEELEELEEELEELEAE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  602 RLVLEQDKLSLQTSLELEK--RERNAGSETITDLQGRIYGLEGELKHIKSslskAEVEKRQLQEDLTTLEKEKNKQEIDL 679
Cdd:COG4717    111 LEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQL 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  680 SF-KLKAVQQSLEQeeaehkttkarladnnkinqsIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLdcdykQ 758
Cdd:COG4717    187 SLaTEEELQDLAEE---------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----A 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  759 AKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLcqGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSK 838
Cdd:COG4717    241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTI--AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  839 EREESEKQLKEMKDQLEAEQYFTKLYktQIRELKEESDEKVKLYKDAQqrIEDLQEERDSLASQLEVSltkaDSEQL-AR 917
Cdd:COG4717    319 EELEELLAALGLPPDLSPEELLELLD--RIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE----DEEELrAA 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  918 ITVEEQYSDLEKEkimkeleikdmIARHRQDLAEKDGTINSLEESN--RTLTVDVANLASEKEELNNKLKHIQQKLEKIK 995
Cdd:COG4717    391 LEQAEEYQELKEE-----------LEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELE 459
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1207153289  996 EEEKQMKSlTVSYEKQIQVEKTLKIQaINKLAE 1028
Cdd:COG4717    460 AELEQLEE-DGELAELLQELEELKAE-LRELAE 490
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
430-637 3.95e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVR--- 506
Cdd:COG4942     35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRaly 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  507 KAGLETDRKRLLENE---------------VSSLKEQLAELKKKNQishLSAEKNIHLERQLEEVSAKLQAELEESERLK 571
Cdd:COG4942    115 RLGRQPPLALLLSPEdfldavrrlqylkylAPARREQAEELRADLA---ELAALRAELEAERAELEALLAELEEERAALE 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  572 KAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTslELEKRERNAGSETITDLQGRI 637
Cdd:COG4942    192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA--EAAAAAERTPAAGFAALKGKL 255
Filament pfam00038
Intermediate filament protein;
409-663 4.05e-07

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 53.77  E-value: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  409 LTQQNKCSEEDIIEDHGLNHTESNDL----EKRL----KKLEEKFKHEMQAKEELENkcriANQRLEKLSKDLEEEVNAR 480
Cdd:pfam00038   23 LEQQNKLLETKISELRQKKGAEPSRLyslyEKEIedlrRQLDTLTVERARLQLELDN----LRLAAEDFRQKYEDELNLR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  481 QEAEDNLRSLEKEKVLLKHQRTQsvrkagletdrkrlLENEVSSLKEQLA-----------ELKKKNQISHLSAE----K 545
Cdd:pfam00038   99 TSAENDLVGLRKDLDEATLARVD--------------LEAKIESLKEELAflkknheeevrELQAQVSDTQVNVEmdaaR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  546 NIHL-------ERQLEEVSAKLQAELEE--SERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQ---DKLSLQ 613
Cdd:pfam00038  165 KLDLtsalaeiRAQYEEIAAKNREEAEEwyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSlkkQKASLE 244
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  614 TSL-ELEKRernaGSETITDLQGRIYGLEGELKHIKSSLSkaevekRQLQE 663
Cdd:pfam00038  245 RQLaETEER----YELQLADYQELISELEAELQETRQEMA------RQLRE 285
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
162-284 4.19e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 54.13  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSNYDIPEEWAQFyTA---EVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRCDTAV 237
Cdd:PHA03211   245 DLYTYLGARLRPLGLAQV-TAvarQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaACFARGSWSTPFHYGIA 323
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1207153289  238 GTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGDTPFYSES 284
Cdd:PHA03211   324 GTVDTNAPEVLAGDP----YTPSVDIWSAGLVIFEAAVHTASLFSAS 366
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
76-281 4.69e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 53.94  E-value: 4.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSD-------SAFFWEERDIMAFSQSPWivqlccAFQDE 148
Cdd:cd14228     15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGqievsilSRLSSENADEYNFVRSYE------CFQHK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  149 KYLYLVMEFMPGG--DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLL----DRNGHLKLADFGTC 222
Cdd:cd14228     89 NHTCLVFEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSA 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  223 MKMDSTgmvRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGdTPFY 281
Cdd:cd14228    169 SHVSKA---VCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLY 219
PTZ00121 PTZ00121
MAEBL; Provisional
436-750 5.06e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 5.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  436 KRLKKLEEKFKHEMQAK-EELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDR 514
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  515 KRLLENEVSSLKEQLAELKKKNQISHLSAE-----------------KNIHLERQLEEVSAKLQAELEESERLKKAQIEA 577
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkaeedkkkaeeakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  578 FRQSQQLElslRELQERLAQLENSRLVLEQDKLSLQtSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVE 657
Cdd:PTZ00121  1715 KKKAEELK---KAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  658 KRQLQEDLTTLEKEKN------------------KQEIDLSFKLKAVQQSLEQEEA----EHKTTKARLADNNKINQSIE 715
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNfaniieggkegnlvindsKEMEDSAIKEVADSKNMQLEEAdafeKHKFNKNNENGEDGNKEADF 1870
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1207153289  716 AKSETLKDMEHKLLEERSAKQQLENRLMQLEKENS 750
Cdd:PTZ00121  1871 NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
84-280 5.66e-07

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 52.77  E-value: 5.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKyLYLVMEFMPGGDL 163
Cdd:cd05069     20 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMPEA----FLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  164 VTLTSNYD-----IPEEWAQfyTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCDTAVG 238
Cdd:cd05069     94 LDFLKEGDgkylkLPQLVDM--AAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKF 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207153289  239 TPDYISPEVLMsqggtgyYGR---ECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05069    172 PIKWTAPEAAL-------YGRftiKSDVWSFGILLTELVTkGRVPY 210
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
72-280 5.81e-07

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 52.76  E-value: 5.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   72 QVKLDDFDRVKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCcAFQDEKYL 151
Cdd:cd05070      5 EIPRESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPES----FLEEAQIMKKLKHDKLVQLY-AVVSEEPI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  152 YLVMEFMPGGDLVTLTSNYD-----IPEEWAQfyTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMD 226
Cdd:cd05070     79 YIVTEYMSKGSLLDFLKDGEgralkLPNLVDM--AAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  227 STGMVRCDTAVGTPDYISPEVLMsqggtgyYGR---ECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05070    157 DNEYTARQGAKFPIKWTAPEAAL-------YGRftiKSDVWSFGILLTELVTkGRVPY 207
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
82-285 5.82e-07

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 52.57  E-value: 5.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   82 KLIGRGAFGAVqLVRHKVSQQVyAMKQLsKFEMVKRSdsafFWEERDIMAFSQSPWIVQLCCAFQDEKyLYLVMEFMPGG 161
Cdd:cd05083     12 EIIGEGEFGAV-LQGEYMGQKV-AVKNI-KCDVTAQA----FLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  162 DLVTLTSN---YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGtcmkMDSTGMVRCDTAVG 238
Cdd:cd05083     84 NLVNFLRSrgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG----LAKVGSMGVDNSRL 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207153289  239 TPDYISPEVLMSqggtGYYGRECDWWSVGVFIYELL-VGDTPFYSESL 285
Cdd:cd05083    160 PVKWTAPEALKN----KKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSV 203
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
187-280 6.00e-07

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 52.73  E-value: 6.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  187 ALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFG-TCMKMDSTGMVRCDTAVGTPDYISPEVLMSQGGTGyYGRECDWWS 265
Cdd:cd14149    120 GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDNNP-FSFQSDVYS 198
                           90
                   ....*....|....*
gi 1207153289  266 VGVFIYELLVGDTPF 280
Cdd:cd14149    199 YGIVLYELMTGELPY 213
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
81-292 6.39e-07

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 52.41  E-value: 6.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   81 VKLIGRGAFGAVQLVRHKVSQQVyAMKQLSKFEMvkrsDSAFFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPG 160
Cdd:cd05068     13 LRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPGTM----DPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKH 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  161 GDLVTLTSNYD----IPE--EWAqfytAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKMDSTGMVRCD 234
Cdd:cd05068     88 GSLLEYLQGKGrslqLPQliDMA----AQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAR 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  235 TAVGTP-DYISPEVLMSQGGTgyygRECDWWSVGVFIYELLvgdtpfyseslvgTYGKI 292
Cdd:cd05068    164 EGAKFPiKWTAPEAANYNRFS----IKSDVWSFGILLTEIV-------------TYGRI 205
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
453-821 6.54e-07

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 54.10  E-value: 6.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  453 EELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQ-RTQSVRKAGLETDRKRLlENEVSSLKEQLAE 531
Cdd:pfam09730   37 LELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEiKEYKVREARLLQDYSEL-EEENISLQKQVSV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  532 LKKkNQISHLSAEKNIhleRQLEEVSAKLQAELEESERLKK-------AQIEAFRQSQQLELSLR-ELQERLA---QLEN 600
Cdd:pfam09730  116 LKQ-NQVEFEGLKHEI---TRKEEETELLNSQLEEAIRLREiaerqldEALETLKTEREQKNSLRkELSHYMTlndFDYV 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  601 SRLVLEQDKLSLQTSLElEKRERNAGSETITDLQGRIYGLE-GELKHIKSSLSKAEV------------------EKRQL 661
Cdd:pfam09730  192 SHLSISLDGLKFSEDEG-AGTEPNNDGEAMDGGENGGGGLKnSGLDNRTSTPRKSEVfppapslvsdllselnisEIQKL 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  662 QEDLTTLEKEKnkqeIDLSFKLKAVQQSLEQEE---AEHKTTKARLADNNKINQSIEAKsetlKDMEHKLLEERSAKQQL 738
Cdd:pfam09730  271 KQQLIQVEREK----VSLLSTLQESQKQLEQAKgalSEQQEKVNRLTENLEAMRGLQAS----KERQDALDSEKDRDSHE 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  739 ENRLMQLE-KENSVLDCDYKQAKHELQELRslkENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQ 817
Cdd:pfam09730  343 DGDYYEVDiNGPEILECKYRVAVEEAGELR---EELKALKARYNTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQE 419

                   ....
gi 1207153289  818 ELNH 821
Cdd:pfam09730  420 RIAH 423
mukB PRK04863
chromosome partition protein MukB;
544-989 7.27e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 54.19  E-value: 7.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  544 EKNIHLERQLEevsakLQAELEESERlkkaQIEAfrqSQQLelsLRELQERLAQLENSRLVLEQDklsLQTSLELEKRER 623
Cdd:PRK04863   280 ERRVHLEEALE-----LRRELYTSRR----QLAA---EQYR---LVEMARELAELNEAESDLEQD---YQAASDHLNLVQ 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  624 NAgsetiTDLQGRIYGLEGELKHIKSSLSKAE--VEKRQLQEDLTTLEKEKNKQEID-LSFKLKAVQQSLE--QEEA-EH 697
Cdd:PRK04863   342 TA-----LRQQEKIERYQADLEELEERLEEQNevVEEADEQQEENEARAEAAEEEVDeLKSQLADYQQALDvqQTRAiQY 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  698 KTTKARLAdnnKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLkenlteqV 777
Cdd:PRK04863   417 QQAVQALE---RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI-------A 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  778 EVLNVRVQQETQRKTLCQG-DLKVQRQEINSLRSSEQQLKQELNhllelkltlekQNQELSKEREESEKQLKEM-KDQLE 855
Cdd:PRK04863   487 GEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRLSELEQRLR-----------QQQRAERLLAEFCKRLGKNlDDEDE 555
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  856 AEQYFTKLyKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSeqLARItvEEQYSDlekekimkE 935
Cdd:PRK04863   556 LEQLQEEL-EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA--LARL--REQSGE--------E 622
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  936 LEIKDMIARHRQDLAEKDgtinsleesnRTLTVDVANLASEKEELNNKLKHIQQ 989
Cdd:PRK04863   623 FEDSQDVTEYMQQLLERE----------RELTVERDELAARKQALDEEIERLSQ 666
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
512-748 7.34e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 7.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  512 TDRKRLLENEVSSLKEQLAELKK-----KNQISHLSAEKNIhLERQLEEVSAKLQA---ELEESE-RLKKAQIEAFRQSQ 582
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKelaalKKEEKALLKQLAA-LERRIAALARRIRAleqELAALEaELAELEKEIAELRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  583 QLELSLRELQERLAQLEnsrlvleqdKLSLQTSLELekrerNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQ 662
Cdd:COG4942     98 ELEAQKEELAELLRALY---------RLGRQPPLAL-----LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  663 EDLTTLEKEKNKQEIDLSfKLKAVQQSLEQEEAEHKTTKARLadnnkiNQSIEAKSETLKDMEhklleerSAKQQLENRL 742
Cdd:COG4942    164 ALRAELEAERAELEALLA-ELEEERAALEALKAERQKLLARL------EKELAELAAELAELQ-------QEAEELEALI 229

                   ....*.
gi 1207153289  743 MQLEKE 748
Cdd:COG4942    230 ARLEAE 235
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
76-281 8.45e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 52.78  E-value: 8.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGAVQLVRHKVSQQVYAMKQLSKFEMVKRSDSAffweERDIMAFSQSPW-----IVQLCCAFQDEKY 150
Cdd:cd14227     15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI----EVSILARLSTESaddynFVRAYECFQHKNH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  151 LYLVMEFMPGG--DLVTLTSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDN-MLLDRNGH---LKLADFGTCMK 224
Cdd:cd14227     91 TCLVFEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENiMLVDPSRQpyrVKVIDFGSASH 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  225 MDSTgmvRCDTAVGTPDYISPEVLMSQGgtgyYGRECDWWSVGVFIYELLVGdTPFY 281
Cdd:cd14227    171 VSKA---VCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLY 219
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
84-281 8.59e-07

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 52.38  E-value: 8.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAV------QLVRHKVSQQVyAMKQLSKFEMVKRSDSafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEF 157
Cdd:cd05048     13 LGEGAFGKVykgellGPSSEESAISV-AIKTLKENASPKTQQD--FRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGD----LVTLTSNYDIPEEWAQFYTAEVVLALDAIH-------------SLGFIHRDIKPDNMLLDRNGHLKLADFG 220
Cdd:cd05048     90 MAHGDlhefLVRHSPHSDVGVSSDDDGTASSLDQSDFLHiaiqiaagmeylsSHHYVHRDLAARNCLVGDGLTVKISDFG 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  221 TCMKMDSTGMVRCDTAVGTP-DYISPEVLMsqggtgyYGR---ECDWWSVGVFIYELL-VGDTPFY 281
Cdd:cd05048    170 LSRDIYSSDYYRVQSKSLLPvRWMPPEAIL-------YGKfttESDVWSFGVVLWEIFsYGLQPYY 228
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
123-292 8.70e-07

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 52.04  E-value: 8.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  123 FWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFMPGGDLVTL---TSNYDIPEEWAQFYTAEVVLALDAIHSLGFIHR 199
Cdd:cd05052     49 FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYlreCNREELNAVVLLYMATQIASAMEYLEKKNFIHR 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  200 DIKPDNMLLDRNGHLKLADFGTcmkmdsTGMVRCDTAVGTPDYISPEVLMSQGGTGYY--GRECDWWSVGVFIYELLV-G 276
Cdd:cd05052    129 DLAARNCLVGENHLVKVADFGL------SRLMTGDTYTAHAGAKFPIKWTAPESLAYNkfSIKSDVWAFGVLLWEIATyG 202
                          170
                   ....*....|....*.
gi 1207153289  277 DTPFYSESLVGTYGKI 292
Cdd:cd05052    203 MSPYPGIDLSQVYELL 218
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
553-914 9.53e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 53.36  E-value: 9.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  553 LEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITD 632
Cdd:pfam07888   47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  633 LQGRIYGLEGELKHIKSSLSKAEVEkrqlqedlttLEKEKNKQEidlsfklKAVQQsLEQEEAEHKTTKARLADNNKINQ 712
Cdd:pfam07888  127 HEARIRELEEDIKTLTQRVLERETE----------LERMKERAK-------KAGAQ-RKEEEAERKQLQAKLQQTEEELR 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  713 SIeakSETLKDMEHKLLEERSAKQQLENRLMQLekENSVLDCDYKQAKHE--LQELRSLKE--NLTEQ-VEVLNV----- 782
Cdd:pfam07888  189 SL---SKEFQELRNSLAQRDTQVLQLQDTITTL--TQKLTTAHRKEAENEalLEELRSLQErlNASERkVEGLGEelssm 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  783 -----RVQQETQRKTLCQGDLKVQRQEIN-SLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQ--- 853
Cdd:pfam07888  264 aaqrdRTQAELHQARLQAAQLTLQLADASlALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMErek 343
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289  854 LEAEQYFTK-LYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSL---ASQLEVSLTKADSEQ 914
Cdd:pfam07888  344 LEVELGREKdCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVADAK 408
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
84-283 9.71e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 51.93  E-value: 9.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQ--LVRHKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQD----EKYLYLVMEF 157
Cdd:cd14033      9 IGRGSFKTVYrgLDTETTVEVAWCELQTRKLSKGERQR---FSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCIILVTEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  158 MPGGDLVT-LTSNYDIPEEWAQFYTAEVVLALDAIHSLG--FIHRDIKPDNMLLD-RNGHLKLADFGTCmKMDSTGMVRc 233
Cdd:cd14033     86 MTSGTLKTyLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLA-TLKRASFAK- 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289  234 dTAVGTPDYISPEVLMSQggtgyYGRECDWWSVGVFIYELLVGDTPfYSE 283
Cdd:cd14033    164 -SVIGTPEFMAPEMYEEK-----YDEAVDVYAFGMCILEMATSEYP-YSE 206
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
77-315 1.05e-06

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 51.97  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   77 DFDRVKLIGRGAFGAVQLVR-H-KVSQQVYAMKQLSKfemvkrSDSAFFWEErdIMAFSQSPW--IVQLCCAFQDEKYLY 152
Cdd:cd14063      1 ELEIKEVIGKGRFGRVHRGRwHgDVAIKLLNIDYLNE------EQLEAFKEE--VAAYKNTRHdnLVLFMGACMDPPHLA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  153 LVMEFMPGGDLVTLT----SNYDIpeEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDrNGHLKLADFGTcmkMDST 228
Cdd:cd14063     73 IVTSLCKGRTLYSLIherkEKFDF--NKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGL---FSLS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  229 GMVRCDTAVGT---P----DYISPEVL------MSQGGTGYYGRECDWWSVGVFIYELLVGDTPF---YSESLVGTYGKi 292
Cdd:cd14063    147 GLLQPGRREDTlviPngwlCYLAPEIIralspdLDFEESLPFTKASDVYAFGTVWYELLAGRWPFkeqPAESIIWQVGC- 225
                          250       260
                   ....*....|....*....|...
gi 1207153289  293 mDHKNSLtfpDDIEMSKNAKDLI 315
Cdd:cd14063    226 -GKKQSL---SQLDIGREVKDIL 244
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
76-280 1.10e-06

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 52.04  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   76 DDFDRVKLIGRGAFGavqlvrhKVSQQVYAMKQLSKFEM-VKR-------SDSAFFWEERDIMAFSQSPWIVQLCCAFQD 147
Cdd:cd05056      6 EDITLGRCIGEGQFG-------DVYQGVYMSPENEKIAVaVKTcknctspSVREKFLQEAYIMRQFDHPHIVKLIGVITE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  148 EKyLYLVMEFMPGGDLVT-LTSN-YDIPEEWAQFYTAEVVLALDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMKM 225
Cdd:cd05056     79 NP-VWIVMELAPLGELRSyLQVNkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  226 DSTGMVRCDTAVGTPDYISPEVLMSQGGTGyygrECDWWSVGVFIYELLV-GDTPF 280
Cdd:cd05056    158 EDESYYKASKGKLPIKWMAPESINFRRFTS----ASDVWMFGVCMWEILMlGVKPF 209
PRK01156 PRK01156
chromosome segregation protein; Provisional
418-987 1.11e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 53.37  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQAKEELENKCRIanqrLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLL 497
Cdd:PRK01156   172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI----TLKEIERLSIEYNNAMDDYNNLKSALNELSSL 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  498 ---KHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAEL------KKKNQISHLSAEKN--IHLERQLEEVSAKLQaELEE 566
Cdd:PRK01156   248 edmKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIindpvyKNRNYINDYFKYKNdiENKKQILSNIDAEIN-KYHA 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  567 SERlKKAQIEAFRQsqqlelSLRELQERLAQLENSRLVLEQDKL---SLQTSLELEKRERNAGSETITDLQGRIYGLEG- 642
Cdd:PRK01156   327 IIK-KLSVLQKDYN------DYIKKKSRYDDLNNQILELEGYEMdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKi 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  643 -----------------ELKHIKSSLSKAEVEKRQLQEDLttLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHkTTKARLA 705
Cdd:PRK01156   400 qeidpdaikkelneinvKLQDISSKVSSLNQRIRALRENL--DELSRNMEMLNGQSVCPVCGTTLGEEKSNH-IINHYNE 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  706 DNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENrlmqleKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQ 785
Cdd:PRK01156   477 KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES------EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  786 QETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHllelkltleKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYK 865
Cdd:PRK01156   551 IKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNR---------SRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  866 TQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQlevsLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIArh 945
Cdd:PRK01156   622 REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA-- 695
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1207153289  946 rqDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHI 987
Cdd:PRK01156   696 --NRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
591-992 1.11e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 52.98  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  591 LQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETitdlqgriygLEGELKHIKSSLSKAEVEKRQLQEDLTTLEk 670
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQ----------WERQRRELESRVAELKEELRQSREKHEELE- 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  671 EKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKI----NQSIEAKSETLKDMEHKLL----EERSAKQQLENRL 742
Cdd:pfam07888  101 EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTltqrVLERETELERMKERAKKAGaqrkEEEAERKQLQAKL 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  743 MQLEKENSVLDCDYKQAKHELQELRS----LKENLTEQVEVLNVRVQQETQRKTLCQgDLKVQRQEINSLRSSEQQLKQE 818
Cdd:pfam07888  181 QQTEEELRSLSKEFQELRNSLAQRDTqvlqLQDTITTLTQKLTTAHRKEAENEALLE-ELRSLQERLNASERKVEGLGEE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  819 L-------NHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQyftklyKTQIRELKEESDEKVKLYKDAQQRIED 891
Cdd:pfam07888  260 LssmaaqrDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQER------ETLQQSAEADKDRIEKLSAELQRLEER 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  892 LQEERdslasqlevsltkadseqlaritveeqysdLEKEKIMKELEI-KDMiarHRQDLAEKDGTINSLEESNRTLTVDV 970
Cdd:pfam07888  334 LQEER------------------------------MEREKLEVELGReKDC---NRVQLSESRRELQELKASLRVAQKEK 380
                          410       420
                   ....*....|....*....|..
gi 1207153289  971 ANLASEKEELNNKLKHIQQKLE 992
Cdd:pfam07888  381 EQLQAEKQELLEYIRQLEQRLE 402
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
84-284 1.13e-06

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 51.96  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289   84 IGRGAFGAVQLVR-----HKVSQQVYAMKQLSKFEMVKRSDsafFWEERDIMAFSQSPWIVQLCCAFQDEKYLYLVMEFM 158
Cdd:cd05093     13 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKD---FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  159 PGGDL----------VTLTSNYDIPEEWAQ---FYTAEVVLA-LDAIHSLGFIHRDIKPDNMLLDRNGHLKLADFGTCMK 224
Cdd:cd05093     90 KHGDLnkflrahgpdAVLMAEGNRPAELTQsqmLHIAQQIAAgMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289  225 MDSTGMVRCDTAVGTP-DYISPEVLMSQGGTgyygRECDWWSVGVFIYELLV-GDTPFYSES 284
Cdd:cd05093    170 VYSTDYYRVGGHTMLPiRWMPPESIMYRKFT----TESDVWSLGVVLWEIFTyGKQPWYQLS 227
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
835-1137 1.18e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  835 ELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKlYKDAQQRIEDLqeERDSLASQLEVSLT--KADS 912
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREY--EGYELLKEKEALERqkEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  913 EQLARITVEEQYSDLEKEKIMKELEikdMIARHRQDLAEK-----DGTINSLEESNRTLTVDVANLASEKEELNNKLKHI 987
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLE---EIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  988 QQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKTDGRPHQINNTDirRKEKEIRQLQLQLRTEKEKLN 1067
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD--KEFAETRDELKDYREKLEKLK 398
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289 1068 HSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSLSIH-SLDTTSISSIGNDLDSDEA 1137
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQ 469
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
636-888 1.19e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 52.12  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  636 RIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKeknkQEIDLSfKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIE 715
Cdd:pfam15905   95 RLQALEEELEKVEAKLNAAVREKTSLSASVASLEK----QLLELT-RVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  716 AKSETL----KDMEHKL------LEERSAK-QQLENRLMQLEKENSVLDCDYKQAKHELQELrslkENLTEQVEVLNVRV 784
Cdd:pfam15905  170 AKMKEVmakqEGMEGKLqvtqknLEHSKGKvAQLEEKLVSTEKEKIEEKSETEKLLEYITEL----SCVSEQVEKYKLDI 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  785 QQetqrktlCQGDLKVQRQEINSLRSSEQQLKQELnhlLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEqyftkly 864
Cdd:pfam15905  246 AQ-------LEELLKEKNDEIESLKQSLEEKEQEL---SKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAE------- 308
                          250       260
                   ....*....|....*....|....
gi 1207153289  865 ktqIRELKEESDEKVKLYKDAQQR 888
Cdd:pfam15905  309 ---LEELKEKLTLEEQEHQKLQQK 329
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
780-983 1.23e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  780 LNVRVQQETQRKTLCQGDLKVQRQE-------INSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMkD 852
Cdd:PRK02224   176 LGVERVLSDQRGSLDQLKAQIEEKEekdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-E 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  853 QLEAEqyftklyktqIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKI 932
Cdd:PRK02224   255 TLEAE----------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE 324
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  933 mkelEIKDMIARHRQDLAEKDGTINSLEEsnrtltvDVANLASEKEELNNK 983
Cdd:PRK02224   325 ----ELRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAEELREE 364
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
564-820 1.30e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.10  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  564 LEESERLKKAQIEafRQSQQLELSLRELQERLAQLENsrlvleqdklslqtslELEK-RERNAgsetITDLQGRIYGLEG 642
Cdd:COG3206    162 LEQNLELRREEAR--KALEFLEEQLPELRKELEEAEA----------------ALEEfRQKNG----LVDLSEEAKLLLQ 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  643 ELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLK-AVQQSLEQEEAEHKTTKARLAdnnkinQSIEAKSETL 721
Cdd:COG3206    220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAELS------ARYTPNHPDV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  722 KDMEHKLleeRSAKQQLENRLMQLEKEnsvLDCDYKQAKHELQELRSLKENLTEQVEVLNvrvQQETQRKTLcQGDLKVQ 801
Cdd:COG3206    294 IALRAQI---AALRAQLQQEAQRILAS---LEAELEALQAREASLQAQLAQLEARLAELP---ELEAELRRL-EREVEVA 363
                          250
                   ....*....|....*....
gi 1207153289  802 RQEINSLRSSEQQLKQELN 820
Cdd:COG3206    364 RELYESLLQRLEEARLAEA 382
mukB PRK04863
chromosome partition protein MukB;
434-901 1.35e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.42  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  434 LEKRLKKLEEKFKhemqAKEELENkcriANQRLEKLSKDLEEEVNARQEAEDNLRSLEkekvllkhQRTQSVRKAGLETD 513
Cdd:PRK04863   285 LEEALELRRELYT----SRRQLAA----EQYRLVEMARELAELNEAESDLEQDYQAAS--------DHLNLVQTALRQQE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  514 RKRLLENEVSSLKEQLAElkkKNQISHLSAEknihlerQLEEVSAKLQAELEESERLkKAQIEAFRQsqqlelSLRELQE 593
Cdd:PRK04863   349 KIERYQADLEELEERLEE---QNEVVEEADE-------QQEENEARAEAAEEEVDEL-KSQLADYQQ------ALDVQQT 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  594 RLAQLENSRLVLEQDK-LSLQTSLELEKRErnagsETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTlekek 672
Cdd:PRK04863   412 RAIQYQQAVQALERAKqLCGLPDLTADNAE-----DWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL----- 481
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  673 nkqeidlsfkLKAVQQSLEQEEAEHkttKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQ-LENRLMQLEKENSV 751
Cdd:PRK04863   482 ----------VRKIAGEVSRSEAWD---VARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQrAERLLAEFCKRLGK 548
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  752 LDCDYKQAKHELQELRSLKENLTEQVEvlNVRVQQETQRKTLCQgdLKVQRQEINSLRSSEQQLKQELNhllelkltlek 831
Cdd:PRK04863   549 NLDDEDELEQLQEELEARLESLSESVS--EARERRMALRQQLEQ--LQARIQRLAARAPAWLAAQDALA----------- 613
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289  832 QNQELSKEREESEKQLKE-MKDQLEAEqyftklyktqiRELKEESDEkvklykdAQQRIEDLQEERDSLAS 901
Cdd:PRK04863   614 RLREQSGEEFEDSQDVTEyMQQLLERE-----------RELTVERDE-------LAARKQALDEEIERLSQ 666
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
464-654 1.84e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  464 QRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDRKRL--LENEVSSLKEQLAELKKKNqiSHL 541
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASS--DDL 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  542 SAeknihLERQLEEvsakLQAELEEserLKKAQIEAFRQSQQLELSLRELQERLAQLEnSRLVLEQDKLSLQTSLELEKR 621
Cdd:COG4913    688 AA-----LEEQLEE----LEAELEE---LEEELDELKGEIGRLEKELEQAEEELDELQ-DRLEAAEDLARLELRALLEER 754
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1207153289  622 ERNAGSETITD-----LQGRIYGLEGELKHIKSSLSKA 654
Cdd:COG4913    755 FAAALGDAVERelrenLEERIDALRARLNRAEEELERA 792
PRK01156 PRK01156
chromosome segregation protein; Provisional
553-1136 2.68e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 52.21  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  553 LEEVSAKLQAELEESERLKKAQieafrQSQQLELSlrELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITD 632
Cdd:PRK01156   171 LKDVIDMLRAEISNIDYLEEKL-----KSSNLELE--NIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  633 LQGR---IYGLEGELKHIKSSLSKAE---VEKRQLQEDLTTLEKE---KNKQEIDLSFKLKavqqslEQEEAEHKTTKAR 703
Cdd:PRK01156   244 LSSLedmKNRYESEIKTAESDLSMELeknNYYKELEERHMKIINDpvyKNRNYINDYFKYK------NDIENKKQILSNI 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  704 LADNNKINQSIEaKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSvldcDYKQAKHELQELRSLKENLTEQVEVLNVR 783
Cdd:PRK01156   318 DAEINKYHAIIK-KLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEM----DYNSYLKSIESLKKKIEEYSKNIERMSAF 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  784 VQQETQRKTLCQGDLKVQRQEINSlrsSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLK------EMKDqlEAE 857
Cdd:PRK01156   393 ISEILKIQEIDPDAIKKELNEINV---KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGE--EKS 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  858 QYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLAS-QLEVSLTKADSEQLARITVEEQYSDLE--KEKIMK 934
Cdd:PRK01156   468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIKINelKDKHDK 547
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  935 ELEIKDMI-ARHRQDLAEKDGTINSLEeSNRTLtVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQ 1013
Cdd:PRK01156   548 YEEIKNRYkSLKLEDLDSKRTSWLNAL-AVISL-IDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1014 VEKTLKIQAINKLAEVMKKTDGRPHQINNtdIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQREINDMQAMIAEESQVRle 1093
Cdd:PRK01156   626 NEANNLNNKYNEIQENKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE-- 701
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1207153289 1094 mqmsldskdSDIERLRSQLTSLSIhsldttSISSIGNDLDSDE 1136
Cdd:PRK01156   702 ---------STIEILRTRINELSD------RINDINETLESMK 729
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
648-1111 2.98e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.15  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  648 KSSLSKAEVEkRQLQEDLTTLEKEKNKQEIDlsfKLKAVQQSLEQEEAEHKTTKARL-ADNNKINQSIEAKSETLKDMEH 726
Cdd:pfam12128  215 KSRLNRQQVE-HWIRDIQAIAGIMKIRPEFT---KLQQEFNTLESAELRLSHLHFGYkSDETLIASRQEERQETSAELNQ 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  727 KLleeRSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRS-LKENLTEQVEVLnvrvQQETQRKTLCQGDLKVQRQEI 805
Cdd:pfam12128  291 LL---RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDqHGAFLDADIETA----AADQEQLPSWQSELENLEERL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  806 NSLRSSEQQLKQELNHLLELKLTLEKQ-----NQELSKEREESEKQLKEMKDQLEA-EQYFTKLYKTQIRELKEE----- 874
Cdd:pfam12128  364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagiKDKLAKIREARDRQLAVAEDDLQAlESELREQLEAGKLEFNEEeyrlk 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  875 ---SDEKVKL------------YKDAQQRIEDLQEE-------RDSLASQLEVSLTKADSE----QLARITVEEQYSDLE 928
Cdd:pfam12128  444 srlGELKLRLnqatatpelllqLENFDERIERAREEqeaanaeVERLQSELRQARKRRDQAsealRQASRRLEERQSALD 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  929 KEKIMKELEIKDMIARHRQDLA---EKDGTINSLEESNRTLTVDVANLASEKEELNN-----KLKHIQqkLEKIKEEEKQ 1000
Cdd:pfam12128  524 ELELQLFPQAGTLLHFLRKEAPdweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvklDLKRID--VPEWAASEEE 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1001 MKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKTDG--RPHQINNTDIRRKEKEIRQLQLQLRTEKEKLNHSIIKYQREIN 1078
Cdd:pfam12128  602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKasREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN 681
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1207153289 1079 D-MQAMIAEESQVRLEMQMSLDSKDSDIERLRSQ 1111
Cdd:pfam12128  682 ErLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
673-1116 3.25e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 51.67  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  673 NKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLadnnkinqsiEAKSETLKDmehKLLEERSAKQQLENRLMQLEKENSVL 752
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIEL----------EKKASALKR---QLDRESDRNQELQKRIRLLEKREAEA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  753 DCDYKQakhELQELRSLKENLTEQVEVLNVRVQQETQRKTLcqgdLKVQRQEINSLRSSEQQlkqelnhllelkltlekQ 832
Cdd:pfam05557   68 EEALRE---QAELNRLKKKYLEALNKKLNEKESQLADAREV----ISCLKNELSELRRQIQR-----------------A 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  833 NQELS---KEREESEKQLKEMKDQLeaeqyftklykTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVslTK 909
Cdd:pfam05557  124 ELELQstnSELEELQERLDLLKAKA-----------SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEI--VK 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  910 ADSEQLARItveeqySDLEKEkimkeleikdmIARHRQD---LAEKDGTINSLEEsnrtltvdvanlasEKEELNNKLKH 986
Cdd:pfam05557  191 NSKSELARI------PELEKE-----------LERLREHnkhLNENIENKLLLKE--------------EVEDLKRKLER 239
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  987 IQQklekikeEEKQMKSLTVSYEKQIQvektlKIQAINKLAEVMKKTDGRPHqinntDIRRKEKEIRQLQLQLRTEKEKL 1066
Cdd:pfam05557  240 EEK-------YREEAATLELEKEKLEQ-----ELQSWVKLAQDTGLNLRSPE-----DLSRRIEQLQQREIVLKEENSSL 302
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1067 NHSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSLS 1116
Cdd:pfam05557  303 TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
433-676 3.32e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.66  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELEnkcRIanqRLEKLSKDLEEevnARQE--AEDNLRSLEKEKVLLKHQRTQSVRKAGL 510
Cdd:pfam17380  328 EMDRQAAIYAEQERMAMERERELE---RI---RQEERKRELER---IRQEeiAMEISRMRELERLQMERQQKNERVRQEL 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  511 ETDRK-RLLENEVS-SLKEQLAELKK---------KNQISHLSAEKnihlERQLEEVSAKLQAELEESERLKkaQIEAFR 579
Cdd:pfam17380  399 EAARKvKILEEERQrKIQQQKVEMEQiraeqeearQREVRRLEEER----AREMERVRLEEQERQQQVERLR--QQEEER 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  580 QSQQLELSLRELQERLAQlENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEV-EK 658
Cdd:pfam17380  473 KRKKLELEKEKRDRKRAE-EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeER 551
                          250
                   ....*....|....*...
gi 1207153289  659 RQLQEDLTTLEKEKNKQE 676
Cdd:pfam17380  552 RRIQEQMRKATEERSRLE 569
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
426-633 3.36e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 3.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  426 LNHTES--NDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQ 503
Cdd:TIGR02169  814 LREIEQklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  504 SVRKAGLETDRKRLLENEVSSLKEQLAELK-----KKNQISHLSAEKNIHLERQLEEVSA-KLQAELEE-SERLKKAQIE 576
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKakleaLEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRvEEEIRALEPV 973
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  577 AFRQSQQLElslrELQERLAQLENSRLVLEQDKLSLQTSLE-LEKRERNAGSETITDL 633
Cdd:TIGR02169  974 NMLAIQEYE----EVLKRLDELKEKRAKLEEERKAILERIEeYEKKKREVFMEAFEAI 1027
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
771-1066 3.59e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  771 ENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEM 850
Cdd:COG4372     41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  851 KDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARItVEEQYSDLEKE 930
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKE 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  931 KIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEK 1010
Cdd:COG4372    200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1011 QIQVEKTLKIQAINKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLRTEKEKL 1066
Cdd:COG4372    280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
582-745 6.86e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 6.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  582 QQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSlskaeVEKRQL 661
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-----KEYEAL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  662 QEDLTTLEKEK---NKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADnnkINQSIEAKSETLKDMEHKLLEER-SAKQQ 737
Cdd:COG1579     95 QKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAEReELAAK 171

                   ....*...
gi 1207153289  738 LENRLMQL 745
Cdd:COG1579    172 IPPELLAL 179
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
453-903 8.46e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.59  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  453 EELENKCRIANQRLEKLSKDL---EEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAgleTDRKRLLENEVSSLKEQL 529
Cdd:pfam10174  313 ETLTNQNSDCKQHIEVLKESLtakEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDL---TEEKSTLAGEIRDLKDML 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  530 AELKKKNQISHLSAEkniHLERQLEEVSAKLQaelEESERLKKAQIEafrqSQQLELSLRELQERLAQLENsrlVLEQdk 609
Cdd:pfam10174  390 DVKERKINVLQKKIE---NLQEQLRDKDKQLA---GLKERVKSLQTD----SSNTDTALTTLEEALSEKER---IIER-- 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  610 lsLQTSLELEKRERnagSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQS 689
Cdd:pfam10174  455 --LKEQREREDRER---LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK 529
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  690 LEQ---EEAEHKTTKaRLADNNKINQSIEAKSETLkDMEHKLLEERSAKQQLE-NRLMQL--EKENSVLDCDYKQAKHEL 763
Cdd:pfam10174  530 KEEcskLENQLKKAH-NAEEAVRTNPEINDRIRLL-EQEVARYKEESGKAQAEvERLLGIlrEVENEKNDKDKKIAELES 607
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  764 QELRSLKEnltEQVEVLNVR-VQQETQRKTLCQGDLKVQRQEINSLRSSEQQL----------KQELN----HLLELKLT 828
Cdd:pfam10174  608 LTLRQMKE---QNKKVANIKhGQQEMKKKGAQLLEEARRREDNLADNSQQLQLeelmgalektRQELDatkaRLSSTQQS 684
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  829 LEKQNQELSKEREESEKQLK---EMKDQLEAEQYFTKlyKTQIRELKEESDEKvklyKDAQQRIEDLQEERDSLASQL 903
Cdd:pfam10174  685 LAEKDGHLTNLRAERRKQLEeilEMKQEALLAAISEK--DANIALLELSSSKK----KKTQEEVMALKREKDRLVHQL 756
PRK11281 PRK11281
mechanosensitive channel MscK;
464-860 9.32e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 50.68  E-value: 9.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  464 QRLEKLS--KDLEEEV-NARQEAEDNLRSLEKekvllkhqrTQSVRKAgLETDRKRL--LENEVSSLKEQLAELKKKNQ- 537
Cdd:PRK11281    43 AQLDALNkqKLLEAEDkLVQQDLEQTLALLDK---------IDRQKEE-TEQLKQQLaqAPAKLRQAQAELEALKDDNDe 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  538 --ISHLSAEKNIHLERQLEEVSAKL---QAELEE-----------SERLKKAQIEAFRQSQQLELSLRELQERLAQLENS 601
Cdd:PRK11281   113 etRETLSTLSLRQLESRLAQTLDQLqnaQNDLAEynsqlvslqtqPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  602 RLVL---EQDKLSLQTSLElekRERNAGSETITDLqgriygleGELKHiksSLSKAEVekRQLQEDLTTLEKEKNKQEID 678
Cdd:PRK11281   193 QRVLlqaEQALLNAQNDLQ---RKSLEGNTQLQDL--------LQKQR---DYLTARI--QRLEHQLQLLQEAINSKRLT 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  679 LSfkLKAVQQSLEQEEAEHKTTKARLADNNKINQSIeakSETLKDMEHKL--LEERS--AKQQLENrLMQ----LEKENS 750
Cdd:PRK11281   257 LS--EKTVQEAQSQDEAARIQANPLVAQELEINLQL---SQRLLKATEKLntLTQQNlrVKNWLDR-LTQsernIKEQIS 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  751 VLDCD-------YKQAkhelQELRSLKE--NLTEQVEvlNVRVQQ---ETQRKTLCQGDLKVQR-----------QEINS 807
Cdd:PRK11281   331 VLKGSlllsrilYQQQ----QALPSADLieGLADRIA--DLRLEQfeiNQQRDALFQPDAYIDKleaghksevtdEVRDA 404
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  808 L-------RSSEQQLKQELNhllelkltlekqNQ-ELSKEREESEKQLKEMKDQLEA---EQYF 860
Cdd:PRK11281   405 LlqllderRELLDQLNKQLN------------NQlNLAINLQLNQQQLLSVSDSLQStltQQIF 456
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
793-1037 1.01e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  793 LCQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAeqyftklYKTQIRELK 872
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  873 EESDEKVKLYKDAQQRIEDLQEErdsLASQLEVSLTKADSEQLARITVEEQYSDLEKE-KIMKEL--EIKDMIARHRQDL 949
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLapARREQAEELRADL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  950 AEKDGTINSLEESNRTLTVDVANLASEKEELNNKlkhIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKiQAINKLAEV 1029
Cdd:COG4942    160 AELAALRAELEAERAELEALLAELEEERAALEAL---KAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAE 235

                   ....*...
gi 1207153289 1030 MKKTDGRP 1037
Cdd:COG4942    236 AAAAAERT 243
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
429-696 2.37e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.74  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQrtqsvrka 508
Cdd:pfam07888  150 TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK-------- 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 gLETDRKRLLENEvsSLKEQLAELKKKNQISHLSAEKnihLERQLEEVSA---KLQAELEESeRLKKAQIEAfrQSQQLE 585
Cdd:pfam07888  222 -LTTAHRKEAENE--ALLEELRSLQERLNASERKVEG---LGEELSSMAAqrdRTQAELHQA-RLQAAQLTL--QLADAS 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  586 LSLRELQERLAqlensrlvleQDKLSLQTSLELEKrernagsETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDL 665
Cdd:pfam07888  293 LALREGRARWA----------QERETLQQSAEADK-------DRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCN 355
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207153289  666 TTLEKEKNKQEIDLSFKLKAVQQSLEQEEAE 696
Cdd:pfam07888  356 RVQLSESRRELQELKASLRVAQKEKEQLQAE 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
433-633 2.92e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSK-------------------DLEEEVNARQEAEDNLRSLEKE 493
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaereiaELEAELERLDASSDDLAALEEQ 693
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  494 KVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQLAELKKKNQ--ISHLSAEKNIHLERQLEEVSA-KLQAELEE--SE 568
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaEDLARLELRALLEERFAAALGdAVERELREnlEE 773
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  569 RLKKAQIEAFRQSQQLEL---------------------SLRELQERLAQLENSRLV-------------LEQDKLSLQT 614
Cdd:COG4913    774 RIDALRARLNRAEEELERamrafnrewpaetadldadleSLPEYLALLDRLEEDGLPeyeerfkellnenSIEFVADLLS 853
                          250
                   ....*....|....*....
gi 1207153289  615 SLElekRERNAGSETITDL 633
Cdd:COG4913    854 KLR---RAIREIKERIDPL 869
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
481-737 3.44e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  481 QEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDRkrlLENEVSSLKEQLAELKKK--NQISHLSAEKN--IHLERQLEEV 556
Cdd:COG4372      9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDK---LQEELEQLREELEQAREEleQLEEELEQARSelEQLEEELEEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  557 SAKLQAELEESERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGR 636
Cdd:COG4372     86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  637 IYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEA 716
Cdd:COG4372    166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
                          250       260
                   ....*....|....*....|.
gi 1207153289  717 KSETLKDMEHKLLEERSAKQQ 737
Cdd:COG4372    246 EDKEELLEEVILKEIEELELA 266
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
525-1110 3.52e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 48.28  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  525 LKEQLAELKKKNQIshlsaeknihLERQLEEVSAKLQAELEE-----SERLKKAQieAFRQSQQLELSLRELQERLAQLE 599
Cdd:pfam10174    1 LQAQLRDLQRENEL----------LRRELDIKESKLGSSMNSiktfwSPELKKER--ALRKEEAARISVLKEQYRVTQEE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  600 NSRLVLE----QDKLSLQTSL-ELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNK 674
Cdd:pfam10174   69 NQHLQLTiqalQDELRAQRDLnQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIET 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  675 QEIDLSFKLKAVQQSLE---------QEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQL 745
Cdd:pfam10174  149 QKQTLGARDESIKKLLEmlqskglpkKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  746 EKENSVLDCdyKQAKHELQElRSLKEnLTEQVEVL--NVRVQQETQRKTLCQgdLKVQRQEINSLRSSEQQLKQELNHLL 823
Cdd:pfam10174  229 KALQTVIEM--KDTKISSLE-RNIRD-LEDEVQMLktNGLLHTEDREEEIKQ--MEVYKSHSKFMKNKIDQLKQELSKKE 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  824 ELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQ- 902
Cdd:pfam10174  303 SELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEi 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  903 ------LEVSLTKADSEQLARITVEEQYSDleKEKIMKELeiKDMIARHRQD--------------LAEKDGTINSLEE- 961
Cdd:pfam10174  383 rdlkdmLDVKERKINVLQKKIENLQEQLRD--KDKQLAGL--KERVKSLQTDssntdtalttleeaLSEKERIIERLKEq 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  962 ---SNRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMK----SLTVSYEKQIQVEKTLKIQAINKLAEVMKKTD 1034
Cdd:pfam10174  459 rerEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKehasSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1035 GRPHQINNTDIRRKEKEIrqlQLQLRTekekLNHSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRS 1110
Cdd:pfam10174  539 QLKKAHNAEEAVRTNPEI---NDRIRL----LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELES 607
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
568-897 3.65e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  568 ERLKKAQIEAF--------------RQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDL 633
Cdd:COG4372      6 EKVGKARLSLFglrpktgiliaalsEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  634 QGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKN---KQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKI 710
Cdd:COG4372     86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  711 NQSIEAKSETLKdmEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQR 790
Cdd:COG4372    166 LAALEQELQALS--EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  791 ktlcQGDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTKLYKTQIRE 870
Cdd:COG4372    244 ----LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
                          330       340
                   ....*....|....*....|....*..
gi 1207153289  871 LKEESDEKVKLYKDAQQRIEDLQEERD 897
Cdd:COG4372    320 ALLELAKKLELALAILLAELADLLQLL 346
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
783-1091 3.77e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.20  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  783 RVQQETQRKTLcqgDLKVQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAEQYFTK 862
Cdd:pfam17380  300 RLRQEKEEKAR---EVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISR 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  863 LYKTQIREL-KEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIM-----KEL 936
Cdd:pfam17380  377 MRELERLQMeRQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMervrlEEQ 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  937 EIKDMIARHRQDLAEKDGTINSLEESNRTltvdvanlASEKEELNNKLkhiqqklekikeeekqmksltvsYEKQIQVEK 1016
Cdd:pfam17380  457 ERQQQVERLRQQEEERKRKKLELEKEKRD--------RKRAEEQRRKI-----------------------LEKELEERK 505
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153289 1017 TLKIQAINKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLRtEKEKLNHSIIKYQREINDMQAMIAEESQVR 1091
Cdd:pfam17380  506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME-ERRRIQEQMRKATEERSRLEAMEREREMMR 579
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
643-948 4.38e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.93  E-value: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  643 ELKHIKSSLSKAEVEKRQLQEDLTTLEK--EKNKQEIDlsfKLKAVQQSLEqeeaehkttKARLADNNKINQSIEakset 720
Cdd:pfam06160   87 ALDEIEELLDDIEEDIKQILEELDELLEseEKNREEVE---ELKDKYRELR---------KTLLANRFSYGPAID----- 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  721 lkdmehkLLEERSAkqQLENRLMQLEKENSvlDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQetqrktlCQGDLKV 800
Cdd:pfam06160  150 -------ELEKQLA--EIEEEFSQFEELTE--SGDYLEAREVLEKLEEETDALEELMEDIPPLYEE-------LKTELPD 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  801 QRQEinsLRSSEQQLKQElnHLLELKLTLEKQNQELSKEREESEKQLKE-------------------MKDQLEAE---- 857
Cdd:pfam06160  212 QLEE---LKEGYREMEEE--GYALEHLNVDKEIQQLEEQLEENLALLENleldeaeealeeieeridqLYDLLEKEvdak 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  858 QYFTKLYKT----------QIRELKEESDEKVKLY---KDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQY 924
Cdd:pfam06160  287 KYVEKNLPEiedylehaeeQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEEL 366
                          330       340
                   ....*....|....*....|....*..
gi 1207153289  925 SDLEK--EKIMKEL-EIKDMIARHRQD 948
Cdd:pfam06160  367 EEILEqlEEIEEEQeEFKESLQSLRKD 393
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
852-1116 4.45e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 4.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  852 DQLEAEQYFTKLYKTQIRELKeeSD-------EKVKLYKDAQQRIEDLQEERDSLASQLEVSLTK-----------ADSE 913
Cdd:COG3206     71 SGLSSLSASDSPLETQIEILK--SRpvlervvDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKgsnvieisytsPDPE 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  914 QLARI--TVEEQYSDLEKEKIMKELE-----IKDMIARHRQDLAEKDGTINSLEESNrtltvDVANLASEKEELNNKLKH 986
Cdd:COG3206    149 LAAAVanALAEAYLEQNLELRREEARkalefLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSE 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  987 IQQKLEKIKEEEKQMKSLTVSYEKQIQvektlkiqainklaevmKKTDGRPHQINNTDIRRKEKEIRQLQLQLRTEKEKL 1066
Cdd:COG3206    224 LESQLAEARAELAEAEARLAALRAQLG-----------------SGPDALPELLQSPVIQQLRAQLAELEAELAELSARY 286
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207153289 1067 --NH-SIIKYQREINDMQAMIAEesqvrlEMQMSLDSKDSDIERLRSQLTSLS 1116
Cdd:COG3206    287 tpNHpDVIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQ 333
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
755-989 4.54e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  755 DYKQAKHELQELRSLKENL---TEQVEVLNvRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELnhllelkltlek 831
Cdd:COG4913    226 AADALVEHFDDLERAHEALedaREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL------------ 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  832 qnqeLSKEREESEKQLKEMKDQLEAEQyftklykTQIRELKEESDE-KVKLYKDAQQRIEDLQEERDSLASQLEVSLTKA 910
Cdd:COG4913    293 ----LEAELEELRAELARLEAELERLE-------ARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRR 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  911 DS--EQLARITVEEQYSdlekekimkELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELNNKLKHIQ 988
Cdd:COG4913    362 ARleALLAALGLPLPAS---------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432

                   .
gi 1207153289  989 Q 989
Cdd:COG4913    433 R 433
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
798-1103 6.47e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.20  E-value: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  798 LKVQRQEI--NSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQLEAeqyftklYKTQIRELKEES 875
Cdd:pfam07888   24 LVVPRAELlqNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE-------LKEELRQSREKH 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  876 DEKVKLYKDAQQRIEDLQEERDSLASQlevsltKADSEQLARiTVEEQYSDLEKEKIMKELEIKDMIARHRQDLAEKDgt 955
Cdd:pfam07888   97 EELEEKYKELSASSEELSEEKDALLAQ------RAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRK-- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  956 inslEESnrtltvdvanlaSEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVmkktdg 1035
Cdd:pfam07888  168 ----EEE------------AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA------ 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289 1036 rphqinntdiRRKEKEIRQLQLQLRTEKEKLNHSIIKYQ---REINDMQAM----IAEESQVRLEM-QMSLDSKDS 1103
Cdd:pfam07888  226 ----------HRKEAENEALLEELRSLQERLNASERKVEglgEELSSMAAQrdrtQAELHQARLQAaQLTLQLADA 291
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
450-748 9.93e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 9.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  450 QAKEELENkcriANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDRKRLLENEVSSLKEQL 529
Cdd:COG4372     49 QLREELEQ----AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  530 AELKKKNQishlsaeknihlerQLEEVSAKLQAELEESErlkkaqieafRQSQQLELSLRELQERLAQLENSRLVLEQDK 609
Cdd:COG4372    125 QDLEQQRK--------------QLEAQIAELQSEIAERE----------EELKELEEQLESLQEELAALEQELQALSEAE 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  610 LSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQS 689
Cdd:COG4372    181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  690 LEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLEKE 748
Cdd:COG4372    261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
410-1109 1.13e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 46.97  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  410 TQQNKCSE-EDIIEDHGLNHTES---------NDLEKRLKK-----LEEKFKHEMQAKEELENKCRIANQRLEKL----- 469
Cdd:TIGR01612  971 TLIDKINElDKAFKDASLNDYEAknnelikyfNDLKANLGKnkenmLYHQFDEKEKATNDIEQKIEDANKNIPNIeiaih 1050
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  470 ------SKDLEEEV---------NARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGletdrKRLLENEVSSLKEQLAELKK 534
Cdd:TIGR01612 1051 tsiyniIDEIEKEIgkniellnkEILEEAEINITNFNEIKEKLKHYNFDDFGKEE-----NIKYADEINKIKDDIKNLDQ 1125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  535 KnqishlsAEKNIhleRQLEEVSAKLQAELEESerlkKAQIEafrqsqqlelSLRELQERLAQLENSRlvleqdklslqt 614
Cdd:TIGR01612 1126 K-------IDHHI---KALEEIKKKSENYIDEI----KAQIN----------DLEDVADKAISNDDPE------------ 1169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  615 slELEKRERNagseTITDLQGRiyglegelKHIKSSLSKAEVEKRQLQEDLTTLEKEKNkqeIDLSFKLKAVQQSLEQEE 694
Cdd:TIGR01612 1170 --EIEKKIEN----IVTKIDKK--------KNIYDEIKKLLNEIAEIEKDKTSLEEVKG---INLSYGKNLGKLFLEKID 1232
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  695 AEHKttkarladnnKINQSIEAKSETLKDMEHklLEERSakQQLENRL---MQLEKENSVLDC---DYKQ----AKHELQ 764
Cdd:TIGR01612 1233 EEKK----------KSEHMIKAMEAYIEDLDE--IKEKS--PEIENEMgieMDIKAEMETFNIshdDDKDhhiiSKKHDE 1298
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  765 ELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQ--EINSLRSSEQQL---------KQELNHLLELKLTLEKQN 833
Cdd:TIGR01612 1299 NISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHnsDINLYLNEIANIynilklnkiKKIIDEVKEYTKEIEENN 1378
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  834 QELSKEREESEKQLKEMKDQLEAEQYFTKLYKT-----------QIRELK-----EESDEKVkLYKDAQQRIED------ 891
Cdd:TIGR01612 1379 KNIKDELDKSEKLIKKIKDDINLEECKSKIESTlddkdidecikKIKELKnhilsEESNIDT-YFKNADENNENvlllfk 1457
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  892 ------------LQEERDSLASQLEVSLTK----ADSEQLARITVEEQYSDLEKEKIM---------------KELEIKD 940
Cdd:TIGR01612 1458 niemadnksqhiLKIKKDNATNDHDFNINElkehIDKSKGCKDEADKNAKAIEKNKELfeqykkdvtellnkySALAIKN 1537
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  941 MIARHRQDlaeKDGTINSLEESNRTLTVDvanlASEKEELNNKLKhiQQKLEKIKEEEKQMKSLTVSYEKQIQVE----K 1016
Cdd:TIGR01612 1538 KFAKTKKD---SEIIIKEIKDAHKKFILE----AEKSEQKIKEIK--KEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenK 1608
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289 1017 TLKIQAI-NKLAEVMKKTDGRPHQINNTDIRRKEKEIRQLQLQLRTEKEKLnHSIIKYQREINDMQAmiaeesqvrlemq 1095
Cdd:TIGR01612 1609 FLKISDIkKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFL-ESLKDQKKNIEDKKK------------- 1674
                          810
                   ....*....|....
gi 1207153289 1096 mSLDSKDSDIERLR 1109
Cdd:TIGR01612 1675 -ELDELDSEIEKIE 1687
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
652-986 1.20e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.66  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  652 SKAEVEkrQLQEDLTTLEKEKNKQEIDLsfkLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMehklLEE 731
Cdd:pfam05557    7 SKARLS--QLQNEKKQMELEHKRARIEL---EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ----AEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  732 RSAKQQLENRLMQLEKENSVLDCDYKQAKHEL-QELRSLKENLTEQvevlnvrvQQETQRKTLCQGDLKVQRQEINSLRS 810
Cdd:pfam05557   78 NRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRRQIQRA--------ELELQSTNSELEELQERLDLLKAKAS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  811 SEQQLKQELNHLLELKLTLEKQNQELSKE---REESEKQLKEMKDQL------EAEQYFTKLYKTQIRELKEES---DEK 878
Cdd:pfam05557  150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEiqsQEQDSEIVKNSKSELaripelEKELERLREHNKHLNENIENKlllKEE 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  879 VKLYKDAQQRIEDLQEERDSLASQLEVSLTKADS-EQLARITVEEQYSDLEKEKIMKELEIKDMIarhrqdLAEKDGTIN 957
Cdd:pfam05557  230 VEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDLSRRIEQLQQREIV------LKEENSSLT 303
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1207153289  958 S----LEESNRTLTVDVANLASEKEELNNKLKH 986
Cdd:pfam05557  304 SsarqLEKARRELEQELAQYLKKIEDLNKKLKR 336
mukB PRK04863
chromosome partition protein MukB;
435-794 1.36e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  435 EKRLKKLEEkfkhEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQ----EAEDnlrslEKEKVLLKHQRTQSVRK-AG 509
Cdd:PRK04863   785 EKRIEQLRA----EREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafEADP-----EAELRQLNRRRVELERAlAD 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  510 LETDRKRLlENEVSSLKEQLAELKKKNQISHLSAEKniHLERQLEEVSAKLqAELEESERlkkaqieafrqsqqlelSLR 589
Cdd:PRK04863   856 HESQEQQQ-RSQLEQAKEGLSALNRLLPRLNLLADE--TLADRVEEIREQL-DEAEEAKR-----------------FVQ 914
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  590 ELQERLAQLENSRLVLEQDklslQTSLELEKRERNAGSETITDLQGRIYGLEgELKHIKSSLSKAEVEKRqlqedlttLE 669
Cdd:PRK04863   915 QHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQRRAHFSYEDAAEM--------LA 981
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  670 KEKNKQEiDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQ----SIEAKSETLKDMEHKL----------LEERSA- 734
Cdd:PRK04863   982 KNSDLNE-KLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAslksSYDAKRQMLQELKQELqdlgvpadsgAEERARa 1060
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289  735 -KQQLENRLM-------QLEKENSVLDcdyKQAKHELQELRSLKENLTEQvevlnvRVQQETQRKTLC 794
Cdd:PRK04863  1061 rRDELHARLSanrsrrnQLEKQLTFCE---AEMDNLTKKLRKLERDYHEM------REQVVNAKAGWC 1119
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
647-987 1.38e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  647 IKSSLSKAEVEKRQLQEDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKinqsieaksetlkdmeh 726
Cdd:COG4372      4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE----------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  727 KLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEIN 806
Cdd:COG4372     67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  807 SLRSSEQQLKQELNHLLELKLTLEKQNQELSKerEESEKQLKEMKDQLEAEQYFTKLYKTQIRELKEESDEKVKLYKDAQ 886
Cdd:COG4372    147 EREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  887 QRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLE--KEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNR 964
Cdd:COG4372    225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
                          330       340
                   ....*....|....*....|...
gi 1207153289  965 TLTVDVANLASEKEELNNKLKHI 987
Cdd:COG4372    305 AALSLIGALEDALLAALLELAKK 327
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
411-619 1.88e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  411 QQNKCSEEDIIEDHGLNHTESNDLEKRLKKLEEKFKHEMQA--KEELENKCRI-------ANQRLEKLSKDLEEEVNARQ 481
Cdd:pfam17380  410 ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERvrLEEQERQQQVerlrqqeEERKRKKLELEKEKRDRKRA 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  482 EaEDNLRSLEKEkvllkhqrTQSVRKAGLETDRKR-LLENEVSSLKEQLAELKKKnqishlsaeknihleRQLEEvsakl 560
Cdd:pfam17380  490 E-EQRRKILEKE--------LEERKQAMIEEERKRkLLEKEMEERQKAIYEEERR---------------REAEE----- 540
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207153289  561 qaeleesERLKKAQIEAFRQSQQLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELE 619
Cdd:pfam17380  541 -------ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
429-711 2.02e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  429 TESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEaednlrsLEKEKVLLKHQRTQSVRKA 508
Cdd:COG4372     73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD-------LEQQRKQLEAQIAELQSEI 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  509 GLETDRKRLLENEVSSLKEQLAELKKKNQiSHLSAEKNIHLERQLEEVSAKLQAELEESERLKKAQIEAFRQSQQLELSL 588
Cdd:COG4372    146 AEREEELKELEEQLESLQEELAALEQELQ-ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  589 RELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGS------ETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQ 662
Cdd:COG4372    225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELelailvEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1207153289  663 EDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKIN 711
Cdd:COG4372    305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
452-748 2.17e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  452 KEELENKcrIANQRLE-KLSKDLEEEVNAR-QEAEDNLRSLEKEKVLLKHQRTQSVRKA-GLETDRKRLL------ENEV 522
Cdd:pfam15921  592 KAQLEKE--INDRRLElQEFKILKDKKDAKiRELEARVSDLELEKVKLVNAGSERLRAVkDIKQERDQLLnevktsRNEL 669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  523 SSLKEQLAELKK--KNQISHLSAEKNiHLERQLEEVsaklQAELEESERLKKA-----------------QIEAFR-QSQ 582
Cdd:pfam15921  670 NSLSEDYEVLKRnfRNKSEEMETTTN-KLKMQLKSA----QSELEQTRNTLKSmegsdghamkvamgmqkQITAKRgQID 744
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  583 QLELSLRELQERLAQLENSRLVLEQDKLSLQTSLELEKRERNAGSETITDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQ 662
Cdd:pfam15921  745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQ 824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  663 EDLTTLEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRL 742
Cdd:pfam15921  825 DIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDL 904

                   ....*.
gi 1207153289  743 MQLEKE 748
Cdd:pfam15921  905 KQLLQE 910
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-614 3.03e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  418 EDIIEDHGLNHTESN----DLEKRLKKLEEKFKHEMQAKEELENKCRIANQR--LEKLSKDLEEEVNARQEAEDNLRSLE 491
Cdd:COG4717    322 EELLAALGLPPDLSPeellELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELK 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  492 KEKVLLKHQRTQ--SVRKAGLETDRKRLLENEVSSLKEQLAELKK------------KNQISHLSAEKNI-HLERQLEEV 556
Cdd:COG4717    402 EELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEeleelreelaelEAELEQLEEDGELaELLQELEEL 481
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  557 SAKLQAELEESERLKKAQ------IEAFRQSQQLELsLRELQERLAQLENSR--LVLEQDKLSLQT 614
Cdd:COG4717    482 KAELRELAEEWAALKLALelleeaREEYREERLPPV-LERASEYFSRLTDGRyrLIRIDEDLSLKV 546
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
832-1029 3.29e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  832 QNQELSKEREESEKQLKEMKDQL-EAEQYFTKlYKTQ--IRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEV--S 906
Cdd:COG3206    169 RREEARKALEFLEEQLPELRKELeEAEAALEE-FRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlrA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  907 LTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIAR----H------RQDLAEKDGTINS-LEESNRTLTVDVANLAS 975
Cdd:COG3206    248 QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnHpdvialRAQIAALRAQLQQeAQRILASLEAELEALQA 327
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207153289  976 EKEELNNKLKHIQQKLEKIKEEEKQMKSLtvsyEKQIQVEKTLKIQAINKLAEV 1029
Cdd:COG3206    328 REASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEA 377
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
668-1112 3.67e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.42  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  668 LEKEKNKQEIDLSFKLKAVQQSLEQEEAEHKTTK-ARLADNNKINQSIEAKSETLKDMEHKLLEERSAKQQLENRLMQLE 746
Cdd:TIGR00606  196 QTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKeAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  747 KENSVLDCDYKQAKHELQE-LRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELNhlLEL 825
Cdd:TIGR00606  276 SRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQG--RLQ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  826 KLTLEKQNQELSKEREESEKQLKEMKDQLE----AEQYFTKLYKTQIRELKEESDEKVKLYKD-------AQQRIEDLQE 894
Cdd:TIGR00606  354 LQADRHQEHIRARDSLIQSLATRLELDGFErgpfSERQIKNFHTLVIERQEDEAKTAAQLCADlqskerlKQEQADEIRD 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  895 ERDSLASQLEVSLTKADSEQLARITVEEQYSDLE-KEKIMKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANL 973
Cdd:TIGR00606  434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADL 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  974 ASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEV--MKKTDGRPHQINNtDIRRKEKE 1051
Cdd:TIGR00606  514 DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHSKSK-EINQTRDR 592
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207153289 1052 IRQLQLQLRTEKEKLNHsiikYQREINDMQAMIAEESQVRLEMQMSLDsKDSDIERLRSQL 1112
Cdd:TIGR00606  593 LAKLNKELASLEQNKNH----INNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEEI 648
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
436-704 4.13e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.42  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  436 KRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQSVRKAGLETDRK 515
Cdd:pfam15905   73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQK 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  516 RLlenevSSLKEQLAELKKKnqishlsaeknihLERQLEEVSAKlqaeleeserlkkaQIEAFRQSQQLELSLRELQERL 595
Cdd:pfam15905  153 KM-----SSLSMELMKLRNK-------------LEAKMKEVMAK--------------QEGMEGKLQVTQKNLEHSKGKV 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  596 AQLENSRLVLEQDKLSlqtslelEKRERNAGSETITDLQGRIYGLEG---ELKHIKSSLSKAEVEKRQLQEDLTTLEKEK 672
Cdd:pfam15905  201 AQLEEKLVSTEKEKIE-------EKSETEKLLEYITELSCVSEQVEKyklDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  673 NKQEIDLSFKLKAVQQSLEQEEAEHKTTKARL 704
Cdd:pfam15905  274 SKQIKDLNEKCKLLESEKEELLREYEEKEQTL 305
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
511-772 4.80e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.03  E-value: 4.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  511 ETDRKRLLENEVSSLKEQLAELKKKNQishlsaekniHLERQLEEVSAKLQAELEESERLKKAqieafrqSQQLELSLRE 590
Cdd:pfam15905   71 ESKDQKELEKEIRALVQERGEQDKRLQ----------ALEEELEKVEAKLNAAVREKTSLSAS-------VASLEKQLLE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  591 LQeRLAQLENSRLVLEQDKLSLQT-SLELEK--RERNAGSETITDLQgriYGLEGELKHIKSSLSKAEVEKRQLQEDLTT 667
Cdd:pfam15905  134 LT-RVNELLKAKFSEDGTQKKMSSlSMELMKlrNKLEAKMKEVMAKQ---EGMEGKLQVTQKNLEHSKGKVAQLEEKLVS 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  668 LEKEKNKQEIDLS------FKLKAVQQSLEQEEAEHKTTKARLADNNKINQSIEAKSETLKDMEHKLLEERSAK-QQLEN 740
Cdd:pfam15905  210 TEKEKIEEKSETEklleyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcKLLES 289
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1207153289  741 RLMQLEKENSVLDCDYKQAKHELQELRSLKEN 772
Cdd:pfam15905  290 EKEELLREYEEKEQTLNAELEELKEKLTLEEQ 321
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
433-617 5.24e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEkvllkhqrtqsvrkagLET 512
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------------IKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  513 DRKRLleNEVSSLKEQLAELKkknQISHLSAEKnihleRQLEEVSAKLQAELEE-SERLKKAQIEAFRQSQQLELSLREL 591
Cdd:COG1579     78 YEEQL--GNVRNNKEYEALQK---EIESLKRRI-----SDLEDEILELMERIEElEEELAELEAELAELEAELEEKKAEL 147
                          170       180
                   ....*....|....*....|....*.
gi 1207153289  592 QERLAQLENSRLVLEQDKLSLQTSLE 617
Cdd:COG1579    148 DEELAELEAELEELEAEREELAAKIP 173
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
710-1111 8.25e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.97  E-value: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  710 INQSIEAKSETLKDM-----EHKLLEERSAKQQ--LENRLMQLEkensVLDCDYKQAKHELQELRS-------LKENLTE 775
Cdd:pfam07111   61 LSQQAELISRQLQELrrleeEVRLLRETSLQQKmrLEAQAMELD----ALAVAEKAGQAEAEGLRAalagaemVRKNLEE 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  776 --QVEVLNVRVQQETQRKTLCQGdlkvQRQEINSLRSSEQQLKQELNHLLELKLTLEKQNQELSKEREESEKQLKEMKDQ 853
Cdd:pfam07111  137 gsQRELEEIQRLHQEQLSSLTQA----HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  854 LEAEQYFTKLYKTQIRE--LKEESDEKVKL-YKDAQQRIEDLQEERDSLASQLEV------SLTKADSEQLARITVEEQY 924
Cdd:pfam07111  213 LEAQVTLVESLRKYVGEqvPPEVHSQTWELeRQELLDTMQHLQEDRADLQATVELlqvrvqSLTHMLALQEEELTRKIQP 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  925 SD-LE--------------KEKIM--------KELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVDVANLASEKEELN 981
Cdd:pfam07111  293 SDsLEpefpkkcrsllnrwREKVFalmvqlkaQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  982 NKLKHIQQKLEKIKEEEKQMKSLTVSYEKQIQVEKTLKIQAINKLAEVMKKTDGRPHQINNTDIR-----RKEKEIRQLQ 1056
Cdd:pfam07111  373 MSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRlsyavRKVHTIKGLM 452
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207153289 1057 ------LQLRTEKEKLNHSIIKYQREIN-DMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQ 1111
Cdd:pfam07111  453 arkvalAQLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAELQLSAHLIQQEVGRAREQ 514
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
434-673 1.10e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.30  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  434 LEKRLKKLEEKFKH---------EMQAKEELENkcriANQRLEKLSKDLE------EEVNAR-----QEAEDNLRSLEKE 493
Cdd:pfam06160  151 LEKQLAEIEEEFSQfeeltesgdYLEAREVLEK----LEEETDALEELMEdipplyEELKTElpdqlEELKEGYREMEEE 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  494 KVLLKH----QRTQSVRKAgLETDRKRLLENEVSSLKEQLAELKKknQISHL--------SAEKNIH-----LERQLEEV 556
Cdd:pfam06160  227 GYALEHlnvdKEIQQLEEQ-LEENLALLENLELDEAEEALEEIEE--RIDQLydllekevDAKKYVEknlpeIEDYLEHA 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  557 SAKLQAELEESERLKKaqieAFRQSQQLELSLRELQERLAQLENSRLVLEQ---DKLSLQTSLElekrernagsETITDL 633
Cdd:pfam06160  304 EEQNKELKEELERVQQ----SYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQ----------EELEEI 369
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1207153289  634 QGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEKN 673
Cdd:pfam06160  370 LEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
430-566 1.41e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  430 ESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQeaednLRSLEKEKVLLKHQRTQsvrkag 509
Cdd:COG1579     39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISD------ 107
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  510 LETDRKRLLEnEVSSLKEQLAELKKknQISHLSAEKNiHLERQLEEVSAKLQAELEE 566
Cdd:COG1579    108 LEDEILELME-RIEELEEELAELEA--ELAELEAELE-EKKAELDEELAELEAELEE 160
mukB PRK04863
chromosome partition protein MukB;
445-953 1.48e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  445 FKHEMQAKEELENKCRIANQRLEKLSKDLEEEVNARQEAEDNLRSLEKEKVLLKHQRTQ------SVRKAGLETDRK--- 515
Cdd:PRK04863   416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqLVRKIAGEVSRSeaw 495
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  516 -------------RLLENEVSSLKEQLAELKKK--------------NQISHLSAEKNIHLERQLEEVSAKLQAELEESE 568
Cdd:PRK04863   496 dvarellrrlreqRHLAEQLQQLRMRLSELEQRlrqqqraerllaefCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  569 RLKKAQIEAFRQSQQLELSLREL----------QERLAQL--------ENSRLVLEQdklsLQTSLELEK---RERNAGS 627
Cdd:PRK04863   576 EARERRMALRQQLEQLQARIQRLaarapawlaaQDALARLreqsgeefEDSQDVTEY----MQQLLEREReltVERDELA 651
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  628 ETITDLQGRIYGLEG-------ELKHIKSSLSK---AEV------------------------------EKRQLQ----- 662
Cdd:PRK04863   652 ARKQALDEEIERLSQpggsedpRLNALAERFGGvllSEIyddvsledapyfsalygparhaivvpdlsdAAEQLAgledc 731
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  663 -EDLTTLE----------------------KEKNKQ-------EIDLsFKLKAVQQSLEQEEAEHKTTKARLA----DNN 708
Cdd:PRK04863   732 pEDLYLIEgdpdsfddsvfsveelekavvvKIADRQwrysrfpEVPL-FGRAAREKRIEQLRAEREELAERYAtlsfDVQ 810
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  709 KINQSIEAKSETLK---------DMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSL--------KE 771
Cdd:PRK04863   811 KLQRLHQAFSRFIGshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDE 890
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  772 NLTEQVEVLNVRVQ--QETQRKTLCQGDLKVQ-RQEINSLRSSEQQLKQ-ELNHLLELKLTLEKQNQ-----ELSKER-- 840
Cdd:PRK04863   891 TLADRVEEIREQLDeaEEAKRFVQQHGNALAQlEPIVSVLQSDPEQFEQlKQDYQQAQQTQRDAKQQafaltEVVQRRah 970
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  841 ---EESEKQL---KEMKDQL-----EAEQYFTKLyKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTK 909
Cdd:PRK04863   971 fsyEDAAEMLaknSDLNEKLrqrleQAEQERTRA-REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVP 1049
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207153289  910 ADS--EQLARITVEEQY----------SDLEKEKIMKELEIKDMIARHRQdlAEKD 953
Cdd:PRK04863  1050 ADSgaEERARARRDELHarlsanrsrrNQLEKQLTFCEAEMDNLTKKLRK--LERD 1103
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
762-937 1.76e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  762 ELQELRSLKENLTEQVEVLNVRVQQETQRKTLCQGDLKVQRQEINSLRSSEQQLKQELnhllelkltlekqnQELSKERE 841
Cdd:COG1579     11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  842 ESEKQLKEMKDQ-----LEAEQYFTKLYKT----QIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEvsltkads 912
Cdd:COG1579     77 KYEEQLGNVRNNkeyeaLQKEIESLKRRISdledEILELMERIEELEEELAELEAELAELEAELEEKKAELD-------- 148
                          170       180
                   ....*....|....*....|....*
gi 1207153289  913 EQLARITVEEQYSDLEKEKIMKELE 937
Cdd:COG1579    149 EELAELEAELEELEAEREELAAKIP 173
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
433-781 2.72e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.15  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  433 DLEKRLKKLEE---KFKHeMQAKEELENkcrianqrLEKLSKDLEEEVNARQEAEDNLRSLEK------EKVLLKHqrtQ 503
Cdd:pfam06160   64 DIEELLFEAEElndKYRF-KKAKKALDE--------IEELLDDIEEDIKQILEELDELLESEEknreevEELKDKY---R 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  504 SVRKAgLETDR------KRLLENEVSSLKEQLAELKKKNQIS-HLSAEKniHLErQLEEVSAKLQAELEE-SERLKKAQI 575
Cdd:pfam06160  132 ELRKT-LLANRfsygpaIDELEKQLAEIEEEFSQFEELTESGdYLEARE--VLE-KLEEETDALEELMEDiPPLYEELKT 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  576 EAFRQsqqlelsLRELQERLAQLENSRLVLEQDKLS---------LQTSLE-LEKRERNAGSETITDLQGRI---YG-LE 641
Cdd:pfam06160  208 ELPDQ-------LEELKEGYREMEEEGYALEHLNVDkeiqqleeqLEENLAlLENLELDEAEEALEEIEERIdqlYDlLE 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  642 GELKhiksslSKAEVEKRqlQEDLTTLEKEKNKQEIDLSFKLKAVQQSL---EQEEAEHKTTKARL----ADNNKINQSI 714
Cdd:pfam06160  281 KEVD------AKKYVEKN--LPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLeeleKRYDEIVERL 352
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207153289  715 EAKSETLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLN 781
Cdd:pfam06160  353 EEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKSN 419
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
728-1062 3.74e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  728 LLEERSAKQQLENRLMQLEKENSVLDCDYKQAKhelqELRSLKENLTEQVEVLNVRVQQETQRKTlcqGDLKVQRQEINS 807
Cdd:TIGR00618  158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKK----SLHGKAELLTLRSQLLTLCTPCMPDTYH---ERKQVLEKELKH 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  808 LRSSEQQLKQELNHllelkltlEKQNQELSKEREESEKQLKEMKDQLEAeqyftklYKTQIRELKEESDE-----KVKLY 882
Cdd:TIGR00618  231 LREALQQTQQSHAY--------LTQKREAQEEQLKKQQLLKQLRARIEE-------LRAQEAVLEETQERinrarKAAPL 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  883 KDAQQRIEDLQEERDSLASQLEVSLTKADSEQLARITVEEQYSDLEKEKIMKELEIKDMIarHRQDLAEKDGTINSLEES 962
Cdd:TIGR00618  296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI--HIRDAHEVATSIREISCQ 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  963 NRTLTVDVANLASEKEELNNKLKHIQQKLEKIKEEEKQMKSLTVSY----------EKQIQVEK--------------TL 1018
Cdd:TIGR00618  374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFrdlqgqlahaKKQQELQQryaelcaaaitctaQC 453
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1207153289 1019 KIQAINKLAEVMKKTDGRPHQINNTD-IRRKEKEIRQLQLQLRTE 1062
Cdd:TIGR00618  454 EKLEKIHLQESAQSLKEREQQLQTKEqIHLQETRKKAVVLARLLE 498
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
636-805 3.79e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  636 RIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEknkqeidlsfkLKAVQQSLEQEEAEHKTTKARLA-DNNKINQSI 714
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-----------LEDLEKEIKRLELEIEEVEARIKkYEEQLGNVR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  715 EAKSetLKDMEHKLLEERSAKQQLENRLMQLEKENSVLDCDYKQAKHELQELRSLKENLTEQVEVLNVRVQQETQRktlc 794
Cdd:COG1579     87 NNKE--YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---- 160
                          170
                   ....*....|.
gi 1207153289  795 qgdLKVQRQEI 805
Cdd:COG1579    161 ---LEAEREEL 168
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
420-1122 8.73e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 8.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  420 IIEDHGlnhtESNDLEKRLKKLEEKFKHEMQAKEELENKCRIANQRLEKLSKD----------LEEEVNARQEAED---N 486
Cdd:TIGR01612  329 ILESEG----EQGHIINKLIFLEKEFEDTIHKSDIYKDECLSNHLFMEDYLKDdkispyyyefLEEIKKIAKQRAIffyN 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  487 LRSLEKEKVLLKHQrtQSVRKAGLETDRKRLLE----NEVSSLKEQLAELKKKNQISHLSAeknihLERQLEEVSAklqa 562
Cdd:TIGR01612  405 AKKLKHLEILYKHQ--EDILNNFHKTIERLIFEkpdpNNNNIFKDDFDEFNKPIPKSKLKA-----LEKRFFEIFE---- 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  563 ELEESERLKKAQIEAFRQSQQLELSL---RELQERLAQLEN--SRLVLEQDKLSLQTSLELEK---RERNAG----SETI 630
Cdd:TIGR01612  474 EEWGSYDIKKDIDENSKQDNTVKLILmrmKDFKDIIDFMELykPDEVPSKNIIGFDIDQNIKAklyKEIEAGlkesYELA 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  631 TDLQGRIYGLEGELKHIKSSLSKAEVEKRQLQEDLTTLEKEK---NKQEIDLSFKLKAVqqSLEQEEAEHKTTKARLADN 707
Cdd:TIGR01612  554 KNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIiyiNKLKLELKEKIKNI--SDKNEYIKKAIDLKKIIEN 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  708 NKINQSIEAKSETLKDMEH---------KLLEERSAKQQ-----LENRLMQLEKENSVldcDYKQAKHELQELRSLKENL 773
Cdd:TIGR01612  632 NNAYIDELAKISPYQVPEHlknkdkiysTIKSELSKIYEddidaLYNELSSIVKENAI---DNTEDKAKLDDLKSKIDKE 708
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  774 TEQVEVLNVRVQQ------ETQRKTLCQGDLKVQRQ---EINS--------LRSSEQQLKQELNHLLELKLTLEKQNQEL 836
Cdd:TIGR01612  709 YDKIQNMETATVElhlsniENKKNELLDIIVEIKKHihgEINKdlnkiledFKNKEKELSNKINDYAKEKDELNKYKSKI 788
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  837 SKEREESEKQ--LKEMKDQlEAEQYFTKlYKTQIRELKEESDEKVKLYKDAQQRIEDLQEERDSLASQLEVSLTKADS-- 912
Cdd:TIGR01612  789 SEIKNHYNDQinIDNIKDE-DAKQNYDK-SKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSeh 866
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  913 EQLARIT-------VEEQYSDLEKekimKELEIKDMIARHRQDLAEKDGTINSLEESNRTLTVdVANLASEKEELNNKLK 985
Cdd:TIGR01612  867 EQFAELTnkikaeiSDDKLNDYEK----KFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKI-CENTKESIEKFHNKQN 941
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153289  986 HIQQKLEKIKEEEKQMKSLTVSYEKQIqvEKTLkIQAINKLAEVMKKTDGRPHQINNTDIRrkeKEIRQLQLQLRTEKEK 1065
Cdd:TIGR01612  942 ILKEILNKNIDTIKESNLIEKSYKDKF--DNTL-IDKINELDKAFKDASLNDYEAKNNELI---KYFNDLKANLGKNKEN 1015
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153289 1066 -LNHSIIKYQREINDMQAMIAEESQVRLEMQMSLDSKDSDIERLRSQLTSLSIHSLDT 1122
Cdd:TIGR01612 1016 mLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK 1073
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH