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Conserved domains on  [gi|392899979|ref|NP_001255374|]
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Serine/threonine-protein kinase WNK [Caenorhabditis elegans]

Protein Classification

WNK family serine/threonine-protein kinase( domain architecture ID 12991120)

WNK (With No Lysine) family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0004674|GO:0006468|GO:0005524
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
279-543 7.46e-175

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: 527.95  E-value: 7.46e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcGKRKY 358
Cdd:cd13983     1 RYLKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWES----KSKKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd13983    77 VIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINGNTGEVKIGDLGLATLLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIpaQYPEIRE 518
Cdd:cd13983   157 QSFAKSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESLSKV--KDPELKD 234
                         250       260
                  ....*....|....*....|....*
gi 392899979  519 IIDRCIRvRREERSTVKQLLVDDFF 543
Cdd:cd13983   235 FIEKCLK-PPDERPSARELLEHPFF 258
OSR1_C super family cl12053
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
569-633 5.08e-12

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


The actual alignment was detected with superfamily member pfam12202:

Pssm-ID: 463491  Cd Length: 62  Bit Score: 62.67  E-value: 5.08e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979   569 IQMQLRVYDEKKRKQyrfKENEGLQFAFDIENDSPDEVVQQMIEQQHIPDEDTRMITKLIKDKVD 633
Cdd:pfam12202    1 INLVLRVRDPKKKKH---KELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
 
Name Accession Description Interval E-value
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
279-543 7.46e-175

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: 527.95  E-value: 7.46e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcGKRKY 358
Cdd:cd13983     1 RYLKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWES----KSKKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd13983    77 VIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINGNTGEVKIGDLGLATLLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIpaQYPEIRE 518
Cdd:cd13983   157 QSFAKSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESLSKV--KDPELKD 234
                         250       260
                  ....*....|....*....|....*
gi 392899979  519 IIDRCIRvRREERSTVKQLLVDDFF 543
Cdd:cd13983   235 FIEKCLK-PPDERPSARELLEHPFF 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
282-543 7.38e-71

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 238.20  E-value: 7.38e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVL 361
Cdd:smart00220    2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFED------EDKLYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKS 440
Cdd:smart00220   75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLD-EDGHVKLADFGLARqLDPGE 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    441 FAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGvKPECFSRIPAQYPEIREI 519
Cdd:smart00220  152 KLTTFVGTPEYMAPEVLlGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKP-KPPFPPPEWDISPEAKDL 230
                           250       260
                    ....*....|....*....|....
gi 392899979    520 IDRCIRVRREERSTVKQLLVDDFF 543
Cdd:smart00220  231 IRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
277-540 2.09e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 198.70  E-value: 2.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFlKFDEELGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgk 355
Cdd:COG0515     6 LGRY-RILRLLGRGGMGVVYLARDLRLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 rkYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT 435
Cdd:COG0515    81 --RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTP-DGRVKLIDFGIAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAK---SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:COG0515   156 ALGGATLTqtgTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLREPPPPPSELRPD 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  512 QYPEIREIIDRCIRVRREER-STVKQLLVD 540
Cdd:COG0515   235 LPPALDAIVLRALAKDPEERyQSAAELAAA 264
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
281-540 1.22e-45

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: 165.75  E-value: 1.22e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   281 LKFDEELGRGSFKTVFRG----LDTETGVAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKR 356
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGA-DEEEREDFLEEASIMKKLDHPNIVKLL------GVCTQG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   357 KYIVLVTELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA- 434
Cdd:pfam07714   74 EPLYIVTEYMPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVS-ENLVVKISDFGLSr 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   435 TLKNKSFAKSVIGTPE---FMAPEMYEEM-YDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECfsri 509
Cdd:pfam07714  151 DIYDDDYYRKRGGGKLpikWMAPESLKDGkFTSKSDVWSFGVLLWEIFTlGEQPYPG-MSNEEVLEFLEDGYRLPQ---- 225
                          250       260       270
                   ....*....|....*....|....*....|..
gi 392899979   510 PAQYP-EIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:pfam07714  226 PENCPdELYDLMKQCWAYDPEDRPTFSELVED 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
277-485 5.28e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.57  E-value: 5.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFlKFDEELGRGSFKTVFRGLDTETG--VAVawcelqesKLNKTE-------RQRFREEAEMLKDLQHPNIVRFYDYW 347
Cdd:NF033483    6 GGRY-EIGERIGRGGMAEVYLAKDTRLDrdVAV--------KVLRPDlardpefVARFRREAQSAASLSHPNIVSVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  348 ESADLcgkrKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVK 427
Cdd:NF033483   77 EDGGI----PYIVM--EYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILIT-KDGRVK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  428 IGDLGLA------TLKNKSfakSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:NF033483  148 VTDFGIAralsstTMTQTN---SVLGTVHYLSPEQARgGTVDARSDIYSLGIVLYEMLTGRPPFD 209
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
279-480 8.29e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.90  E-value: 8.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLnKTERQRFRE-------------EAEMLKDLQHPNIVRFYD 345
Cdd:PTZ00024    9 RYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEI-SNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  346 YWESADlcgkrkYIVLVTELMtSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGS 425
Cdd:PTZ00024   88 VYVEGD------FINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWY--FMHRDLSPANIFIN-SKGI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  426 VKIGDLGLA-----------TLKNKSFAKSVIGTPE-----FMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:PTZ00024  158 CKIADFGLArrygyppysdtLSKDETMQRREEMTSKvvtlwYRAPEllMGAEKYHFAVDMWSVGCIFAELLTG 230
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
302-481 8.60e-13

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 74.11  E-value: 8.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   302 ETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrKYIVLVTELMTSGTLKMYLKRFKR 380
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEhQRARFRRETALCARLYHPNIVALLDSGEAPP-----GLLFAVFEYVPGRTLREVLAADGA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   381 INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI--TGTTGSVKIGDLGLATL---------KNKSFAKSVIGTP 449
Cdd:TIGR03903   76 LPAGETGRLMLQVLDALACAHNQG--IVHRDLKPQNIMVsqTGVRPHAKVLDFGIGTLlpgvrdadvATLTRTTEVLGTP 153
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 392899979   450 EFMAPemyEEMYDESV----DVYAFGMCLLEMVTGE 481
Cdd:TIGR03903  154 TYCAP---EQLRGEPVtpnsDLYAWGLIFLECLTGQ 186
OSR1_C pfam12202
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
569-633 5.08e-12

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


Pssm-ID: 463491  Cd Length: 62  Bit Score: 62.67  E-value: 5.08e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979   569 IQMQLRVYDEKKRKQyrfKENEGLQFAFDIENDSPDEVVQQMIEQQHIPDEDTRMITKLIKDKVD 633
Cdd:pfam12202    1 INLVLRVRDPKKKKH---KELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
 
Name Accession Description Interval E-value
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
279-543 7.46e-175

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: 527.95  E-value: 7.46e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcGKRKY 358
Cdd:cd13983     1 RYLKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWES----KSKKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd13983    77 VIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINGNTGEVKIGDLGLATLLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIpaQYPEIRE 518
Cdd:cd13983   157 QSFAKSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESLSKV--KDPELKD 234
                         250       260
                  ....*....|....*....|....*
gi 392899979  519 IIDRCIRvRREERSTVKQLLVDDFF 543
Cdd:cd13983   235 FIEKCLK-PPDERPSARELLEHPFF 258
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
279-543 2.68e-142

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: 440.21  E-value: 2.68e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlCGKRKY 358
Cdd:cd14033     1 RFLKFNIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKST--VRGHKC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd14033    79 IILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFITGPTGSVKIGDLGLATLKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIpaQYPEIRE 518
Cdd:cd14033   159 ASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKPDSFYKV--KVPELKE 236
                         250       260
                  ....*....|....*....|....*
gi 392899979  519 IIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14033   237 IIEGCIRTDKDERFTIQDLLEHRFF 261
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
262-546 2.65e-135

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 422.15  E-value: 2.65e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  262 EDDFDAQEKPIDKSKNGRFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIV 341
Cdd:cd14030     8 DEIEELETKAVG*SPDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  342 RFYDYWESAdlCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITG 421
Cdd:cd14030    88 RFYDSWEST--VKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  422 TTGSVKIGDLGLATLKNKSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGV 501
Cdd:cd14030   166 PTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGV 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  502 KPECFSRIPAqyPEIREIIDRCIRVRREERSTVKQLLVDDFFTPE 546
Cdd:cd14030   246 KPASFDKVAI--PEVKEIIEGCIRQNKDERYAIKDLLNHAFFQEE 288
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
279-546 2.10e-134

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the 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. The WNK2-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: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 418.71  E-value: 2.10e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcGKRkY 358
Cdd:cd14032     1 RFLKFDIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAK-GKR-C 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd14032    79 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIpaQYPEIRE 518
Cdd:cd14032   159 ASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKV--TDPEIKE 236
                         250       260
                  ....*....|....*....|....*...
gi 392899979  519 IIDRCIRVRREERSTVKQLLVDDFFTPE 546
Cdd:cd14032   237 IIGECICKNKEERYEIKDLLSHAFFAED 264
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
270-546 4.47e-134

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 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: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 418.36  E-value: 4.47e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  270 KPIDKSKNGRFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWES 349
Cdd:cd14031     1 KAVATSPGGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  350 AdLCGKrKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIG 429
Cdd:cd14031    81 V-LKGK-KCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLATLKNKSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRI 509
Cdd:cd14031   159 DLGLATLMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKV 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  510 PAqyPEIREIIDRCIRVRREERSTVKQLLVDDFFTPE 546
Cdd:cd14031   239 TD--PEVKEIIEGCIRQNKSERLSIKDLLNHAFFAED 273
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
282-543 7.38e-71

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 238.20  E-value: 7.38e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVL 361
Cdd:smart00220    2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFED------EDKLYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKS 440
Cdd:smart00220   75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLD-EDGHVKLADFGLARqLDPGE 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    441 FAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGvKPECFSRIPAQYPEIREI 519
Cdd:smart00220  152 KLTTFVGTPEYMAPEVLlGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKP-KPPFPPPEWDISPEAKDL 230
                           250       260
                    ....*....|....*....|....
gi 392899979    520 IDRCIRVRREERSTVKQLLVDDFF 543
Cdd:smart00220  231 IRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
285-543 2.53e-61

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: 210.84  E-value: 2.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCgkrkYIVLvtE 364
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTL----NIFL--E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA----TLKNKS 440
Cdd:cd06606    80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNG--IVHRDIKGANILVDS-DGVVKLADFGCAkrlaEIATGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNP-ATIYRkvISGVK-----PECFSripaqy 513
Cdd:cd06606   157 GTKSLRGTPYWMAPEVIrGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPvAALFK--IGSSGepppiPEHLS------ 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06606   229 EEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
287-523 7.38e-59

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: 203.54  E-value: 7.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG--LDTEtgVAVAwcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYIVLVTE 364
Cdd:cd13999     1 IGSGSFGEVYKGkwRGTD--VAIK--KLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGA------CLSPPPLCIVTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYL-KRFKRINIKVLKSWCRQILKGLSFLHTrnPPVIHRDLKCDNIFITGTtGSVKIGDLGLATLKNKSFAK 443
Cdd:cd13999    71 YMPGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHS--PPIIHRDLKSLNILLDEN-FTVKIADFGLSRIKNSTTEK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 --SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPaqyPEIREII 520
Cdd:cd13999   148 mtGVVGTPRWMAPEVLRgEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCP---PELSKLI 224

                  ...
gi 392899979  521 DRC 523
Cdd:cd13999   225 KRC 227
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
284-540 1.23e-54

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: 191.65  E-value: 1.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTE-RQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyIVLV 362
Cdd:cd14014     5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfRERFLREARALARLSHPNIVRVYDVGEDDGR------PYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATLKNKS-- 440
Cdd:cd14014    79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANILLTE-DGRVKLTDFGIARALGDSgl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 -FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfSRIPAQYP-EIR 517
Cdd:cd14014   156 tQTGSVLGTPAYMAPEQARGGpVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPP--SPLNPDVPpALD 233
                         250       260
                  ....*....|....*....|....
gi 392899979  518 EIIDRCIRVRREER-STVKQLLVD 540
Cdd:cd14014   234 AIILRALAKDPEERpQSAAELLAA 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
277-540 2.09e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 198.70  E-value: 2.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFlKFDEELGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgk 355
Cdd:COG0515     6 LGRY-RILRLLGRGGMGVVYLARDLRLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 rkYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT 435
Cdd:COG0515    81 --RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTP-DGRVKLIDFGIAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAK---SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:COG0515   156 ALGGATLTqtgTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLREPPPPPSELRPD 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  512 QYPEIREIIDRCIRVRREER-STVKQLLVD 540
Cdd:COG0515   235 LPPALDAIVLRALAKDPEERyQSAAELAAA 264
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
287-538 1.94e-53

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: 186.71  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELM 366
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK-LLEELLREIEILKKLNHPNIVKLYDVFET------ENFLYLVMEYC 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLK-RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT-LKNKSFAKS 444
Cdd:cd00180    74 EGGSLKDLLKeNKGPLSEEEALSILRQLLSALEYLHSNG--IIHRDLKPENILLDS-DGTVKLADFGLAKdLDSDDSLLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYEEM----YDESVDVYAFGMCLLEMvtgeypysecmnpatiyrkvisgvkpecfsripaqyPEIREII 520
Cdd:cd00180   151 TTGGTTPPYYAPPELLggryYGPKVDIWSLGVILYEL------------------------------------EELKDLI 194
                         250
                  ....*....|....*...
gi 392899979  521 DRCIRVRREERSTVKQLL 538
Cdd:cd00180   195 RRMLQYDPKKRPSAKELL 212
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
285-543 1.96e-53

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: 188.44  E-value: 1.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAD-LCgkrkyIVLvt 363
Cdd:cd08215     6 RVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGkLC-----IVM-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINI-----KVLKsWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd08215    79 EYADGGDLAQKIKKQKKKGQpfpeeQILD-WFVQICLALKYLHSRK--ILHRDLKTQNIFLT-KDGVVKLGDFGISKVLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 --KSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGvkpeCFSRIPAQY-P 514
Cdd:cd08215   155 stTDLAKTVVGTPYYLSPELCENKpYNYKSDIWALGCVLYELCTLKHPF-EANNLPALVYKIVKG----QYPPIPSQYsS 229
                         250       260
                  ....*....|....*....|....*....
gi 392899979  515 EIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd08215   230 ELRDLVNSMLQKDPEKRPSANEILSSPFI 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
285-543 2.03e-52

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: 185.10  E-value: 2.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKlnKTERQRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLvtE 364
Cdd:cd05122     6 EKIGKGGFGVVYKARHKKTGQIVAIKKINLES--KEKKESILNEIAILKKCKHPNIVKYYGSY----LKKDELWIVM--E 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLK-RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA- 442
Cdd:cd05122    78 FCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLT-SDGEVKLIDFGLSAQLSDGKTr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrkvISGVKPECFSRIPAQY-PEIREII 520
Cdd:cd05122   155 NTFVGTPYWMAPEVIQGKpYGFKADIWSLGITAIEMAEGKPPYSELPPMKALF---LIATNGPPGLRNPKKWsKEFKDFL 231
                         250       260
                  ....*....|....*....|...
gi 392899979  521 DRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd05122   232 KKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
287-542 3.80e-50

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: 178.75  E-value: 3.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGvavAWCELQESKL---NKTERQRFRE---EAEMLKDLQHPNIVRFYdyweSADLCGKRKYIV 360
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTG---DFFAVKEVSLvddDKKSRESVKQleqEIALLSKLRHPNIVQYY----GTEREEDNLYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNK 439
Cdd:cd06632    81 L--EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRN--TVHRDIKGANILVD-TNGVVKLADFGMAKhVEAF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEM---YEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrIPAQY-PE 515
Cdd:cd06632   156 SFAKSFKGSPYWMAPEVimqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPP----IPDHLsPD 231
                         250       260
                  ....*....|....*....|....*..
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06632   232 AKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
282-538 5.44e-49

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: 175.36  E-value: 5.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVL 361
Cdd:cd05117     3 ELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFED------DKNLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGLAT-LKN 438
Cdd:cd05117    77 VMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQG--IVHRDLKPENILLASKDpdSPIKIIDFGLAKiFEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYP-YSEcmNPATIYRKVISG---VKPECFSRIpaqY 513
Cdd:cd05117   155 GEKLKTVCGTPYYVAPEVLKGkGYGKKCDIWSLGVILYILLCGYPPfYGE--TEQELFEKILKGkysFDSPEWKNV---S 229
                         250       260
                  ....*....|....*....|....*
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05117   230 EEAKDLIKRLLVVDPKKRLTAAEAL 254
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
295-540 6.15e-48

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 172.34  E-value: 6.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  295 VFRGLDTETGVAVAWCELQ--ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWesADLCGKRKYIVLVTELMTSGTLK 372
Cdd:cd13984    10 AYLAMDTEEGVEVVWNEVQfsERKIFKAQEEKIRAVFDNLIQLDHPNIVKFHRYW--TDVQEEKARVIFITEYMSSGSLK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  373 MYLKR----FKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK-SFAKSVIG 447
Cdd:cd13984    88 QFLKKtkknHKTMNEKSWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQ-HNGLIKIGSVAPDAIHNHvKTCREEHR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  448 TPEFMAPEM-YEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPA---TIYRKVISgvkpecfsripAQYPEIREIIDRC 523
Cdd:cd13984   167 NLHFFAPEYgYLEDVTTAVDIYSFGMCALEMAALEIQSNGEKVSAneeAIIRAIFS-----------LEDPLQKDFIRKC 235
                         250
                  ....*....|....*..
gi 392899979  524 IRVRREERSTVKQLLVD 540
Cdd:cd13984   236 LSVAPQDRPSARDLLFH 252
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
281-538 8.69e-48

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: 171.96  E-value: 8.69e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    281 LKFDEELGRGSFKTVFRG----LDTETGVAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKR 356
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNIVKLLGV------CTEE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    357 KYIVLVTELMTSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLA 434
Cdd:smart00221   74 EPLMIVMEYMPGGDLLDYLRknRPKELSLSDLLSFALQIARGMEYLESKN--FIHRDLAARNCLV-GENLVVKISDFGLS 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    435 TLKNKSFAKSVIGTPE---FMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRI 509
Cdd:smart00221  151 RDLYDDDYYKVKGGKLpirWMAPESLKEgKFTSKSDVWSFGVLLWEIFTlGEEPYPG-MSNAEVLEYLKKGYRLPKPPNC 229
                           250       260
                    ....*....|....*....|....*....
gi 392899979    510 PaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:smart00221  230 P---PELYKLMLQCWAEDPEDRPTFSELV 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
285-538 2.41e-47

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: 171.18  E-value: 2.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYwesaDLCGKRKYIVLVTE 364
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDR----IVDRANTTLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKS--W--CRQILKGLSFLHTRNPP---VIHRDLKCDNIFITGtTGSVKIGDLGLATL- 436
Cdd:cd08217    82 YCEGGDLAQLIKKCKKENQYIPEEfiWkiFTQLLLALYECHNRSVGggkILHRDLKPANIFLDS-DNNVKLGDFGLARVl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQY- 513
Cdd:cd08217   161 sHDSSFAKTYVGTPYYMSPELLNEQsYDEKSDIWSLGCLIYELCALHPPF-QAANQLELAKKIKEGK----FPRIPSRYs 235
                         250       260
                  ....*....|....*....|....*
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd08217   236 SELNEVIKSMLNVDPDKRPSVEELL 260
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
281-538 1.01e-46

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 168.86  E-value: 1.01e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    281 LKFDEELGRGSFKTVFRG----LDTETGVAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKR 356
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGklkgKGGKKKVEVAVKTLKEDASEQ-QIEEFLREARIMRKLDHPNVVKLLGV------CTEE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    357 KYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLAT 435
Cdd:smart00219   74 EPLYIVMEYMEGGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLESKN--FIHRDLAARNCLV-GENLVVKISDFGLSR 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979    436 LKNKSFAKSVIGTPE---FMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIP 510
Cdd:smart00219  151 DLYDDDYYRKRGGKLpirWMAPESLKEgKFTSKSDVWSFGVLLWEIFTlGEQPYPG-MSNEEVLEYLKNGYRLPQPPNCP 229
                           250       260
                    ....*....|....*....|....*...
gi 392899979    511 aqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:smart00219  230 ---PELYDLMLQCWAEDPEDRPTFSELV 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
287-543 4.79e-46

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: 166.63  E-value: 4.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTELM 366
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTED------FIYLVLEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGDLGLA-TLKNKSFAK 443
Cdd:cd14009    75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKN--IIHRDLKPQNLLLStsGDDPVLKIADFGFArSLQPASMAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPAQYPEIREIIDR 522
Cdd:cd14009   153 TLCGSPLYMAPEILQfQKYDAKADLWSVGAILFEMLVGKPPFRG-SNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRR 231
                         250       260
                  ....*....|....*....|.
gi 392899979  523 CIRVRREERstvkqLLVDDFF 543
Cdd:cd14009   232 LLRRDPAER-----ISFEEFF 247
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
280-544 5.02e-46

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: 167.00  E-value: 5.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYI 359
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVA---IKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGD------EL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKR-FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL-- 436
Cdd:cd06614    72 WVVMEYMDGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQN--VIHRDIKSDNILL-SKDGSVKLADFGFAAQlt 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPA-TIYRKVISGV----KPECFSrip 510
Cdd:cd06614   149 KEKSKRNSVVGTPYWMAPEVIKrKDYGPKVDIWSLGIMCIEMAEGEPPYLE-EPPLrALFLITTKGIpplkNPEKWS--- 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  511 aqyPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06614   225 ---PEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
281-540 1.22e-45

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: 165.75  E-value: 1.22e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   281 LKFDEELGRGSFKTVFRG----LDTETGVAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKR 356
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGA-DEEEREDFLEEASIMKKLDHPNIVKLL------GVCTQG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   357 KYIVLVTELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA- 434
Cdd:pfam07714   74 EPLYIVTEYMPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVS-ENLVVKISDFGLSr 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   435 TLKNKSFAKSVIGTPE---FMAPEMYEEM-YDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECfsri 509
Cdd:pfam07714  151 DIYDDDYYRKRGGGKLpikWMAPESLKDGkFTSKSDVWSFGVLLWEIFTlGEQPYPG-MSNEEVLEFLEDGYRLPQ---- 225
                          250       260       270
                   ....*....|....*....|....*....|..
gi 392899979   510 PAQYP-EIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:pfam07714  226 PENCPdELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
285-538 4.68e-45

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: 163.94  E-value: 4.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd06627     6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKD------SLYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LK-NKSFA 442
Cdd:cd06627    80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQG--VIHRDIKGANILTT-KDGLVKLADFGVATkLNeVEKDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNP-ATIYRkvIsgVKPECfSRIPAQY-PEIREI 519
Cdd:cd06627   157 NSVVGTPYWMAPEVIEmSGVTTASDIWSVGCTVIELLTGNPPYYD-LQPmAALFR--I--VQDDH-PPLPENIsPELRDF 230
                         250
                  ....*....|....*....
gi 392899979  520 IDRCIRVRREERSTVKQLL 538
Cdd:cd06627   231 LLQCFQKDPTLRPSAKELL 249
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
285-538 4.35e-44

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: 161.15  E-value: 4.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd14003     6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIET------ENKIYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-KNKSFAK 443
Cdd:cd14003    80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILLDK-NGNLKIIDFGLSNEfRGGSLLK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPEMYE-EMYD-ESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGvKPECFSRIPaqyPEIREIID 521
Cdd:cd14003   157 TFCGTPAYAAPEVLLgRKYDgPKADVWSLGVILYAMLTGYLPFDD-DNDSKLFRKILKG-KYPIPSHLS---PDARDLIR 231
                         250
                  ....*....|....*..
gi 392899979  522 RCIRVRREERSTVKQLL 538
Cdd:cd14003   232 RMLVVDPSKRITIEEIL 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
285-538 1.02e-41

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: 154.49  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYD-YWESADLCgkrkyivLVT 363
Cdd:cd08529     6 NKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDsFVDKGKLN-------IVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSW--CRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKS- 440
Cdd:cd08529    79 EYAENGDLHSLIKSQRGRPLPEDQIWkfFIQTLLGLSHLHSKK--ILHRDIKSMNIFLD-KGDNVKIGDLGVAKILSDTt 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 -FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQY-PEIR 517
Cdd:cd08529   156 nFAQTIVGTPYYLSPELCEDKpYNEKSDVWALGCVLYELCTGKHPF-EAQNQGALILKIVRGK----YPPISASYsQDLS 230
                         250       260
                  ....*....|....*....|.
gi 392899979  518 EIIDRCIRVRREERSTVKQLL 538
Cdd:cd08529   231 QLIDSCLTKDYRQRPDTTELL 251
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
285-543 1.89e-41

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: 153.86  E-value: 1.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTE-RQRFREEAEMLKDLQHPNIVRFYDYWESADLCgkrkYIVLvt 363
Cdd:cd14099     7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKqREKLKSEIKIHRSLKHPNIVKFHDCFEDEENV----YILL-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-----KN 438
Cdd:cd14099    81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFLDE-NMNVKIGDFGLAARleydgER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KsfaKSVIGTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVisgvkPECFSRIPAQY--- 513
Cdd:cd14099   158 K---KTLCGTPNYIAPEVLEKKkgHSFEVDIWSLGVILYTLLVGKPPF-ETSDVKETYKRI-----KKNEYSFPSHLsis 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14099   229 DEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
285-538 2.40e-41

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: 153.46  E-value: 2.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG-----LDTETGVAVAwcELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYI 359
Cdd:cd00192     1 KKLGEGAFGEVYKGklkggDGKTVDVAVK--TLKEDASES-ERKDFLKEARVMKKLGHPNVVRLLGV------CTEEEPL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKR---------FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGD 430
Cdd:cd00192    72 YLVMEYMEGGDLLDFLRKsrpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKK--FVHRDLAARNCLV-GEDLVVKISD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLA-TLKNKSFAKSVIGTPE---FMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPE 504
Cdd:cd00192   149 FGLSrDIYDDDYYRKKTGGKLpirWMAPESLKDgIFTSKSDVWSFGVLLWEIFTlGATPYPG-LSNEEVLEYLRKGYRLP 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  505 CFSRIPaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd00192   228 KPENCP---DELYELMLSCWQLDPEDRPTFSELV 258
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
286-538 1.26e-40

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: 151.59  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQeSKLNKTERQRFREEAEMLKDLQHPNIVRFYD-YWESADLCgkrkyIVLvtE 364
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKIH-VDGDEEFRKQLLRELKTLRSCESPYVVKCYGaFYKEGEIS-----IVL--E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHT-RNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAK 443
Cdd:cd06623    80 YMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRH--IIHRDIKPSNLLIN-SKGEVKIADFGISKVLENTLDQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 --SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYS--ECMNPATIYRKVISGVKPE----CFSripaqyP 514
Cdd:cd06623   157 cnTFVGTVTYMSPERIQgESYSYAADIWSLGLTLLECALGKFPFLppGQPSFFELMQAICDGPPPSlpaeEFS------P 230
                         250       260
                  ....*....|....*....|....
gi 392899979  515 EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd06623   231 EFRDFISACLQKDPKKRPSAAELL 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
287-543 2.58e-40

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: 150.78  E-value: 2.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER------------QRFREEAEMLKDLQHPNIVRFYDYWESAdlcg 354
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREgkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIDDP---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKM--YLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG 432
Cdd:cd14008    77 ESDKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENG--IVHRDIKPENLLLT-ADGTVKISDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATL---KNKSFAKSViGTPEFMAPEMY---EEMYD-ESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVISGVKPEC 505
Cdd:cd14008   154 VSEMfedGNDTLQKTA-GTPAFLAPELCdgdSKTYSgKAADIWALGVTLYCLVFGRLPFN-GDNILELYEAIQNQNDEFP 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  506 FSRIPaqYPEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14008   232 IPPEL--SPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
287-544 4.59e-40

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: 149.55  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT--ERQrFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd14007     8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSglEHQ-LRREIEIQSHLRHPNILRLYGYFED------KKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKNKSFAKS 444
Cdd:cd14007    81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKN--IIHRDIKPENILL-GSNGELKLADFGWSVHAPSNRRKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQYPEIREIIDRC 523
Cdd:cd14007   158 FCGTLDYLPPEMVEgKEYDYKVDIWSLGVLCYELLVGKPPF-ESKSHQETYKRIQNVD----IKFPSSVSPEAKDLISKL 232
                         250       260
                  ....*....|....*....|.
gi 392899979  524 IRVRREERSTVKQLLVDDFFT 544
Cdd:cd14007   233 LQKDPSKRLSLEQVLNHPWIK 253
Pkinase pfam00069
Protein kinase domain;
283-543 4.68e-39

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 145.46  E-value: 4.68e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   283 FDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLV 362
Cdd:pfam00069    3 VLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD------NLYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGlsflhtrnppvihrdlkcdnifitgttgsvkigdlglatLKNKSFA 442
Cdd:pfam00069   77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEG---------------------------------------LESGSSL 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   443 KSVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG--VKPECFSRIPaqyPEIREI 519
Cdd:pfam00069  118 TTFVGTPWYMAPEVLGGnPYGPKVDVWSLGCILYELLTGKPPFPG-INGNEIYELIIDQpyAFPELPSNLS---EEAKDL 193
                          250       260
                   ....*....|....*....|....
gi 392899979   520 IDRCIRVRREERSTVKQLLVDDFF 543
Cdd:pfam00069  194 LKKLLKKDPSKRLTATQALQHPWF 217
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
293-538 1.48e-38

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 145.84  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  293 KTVFRGLDTETGVAVAWCEL--QESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWesADLCGKRKYIVLVTELMTSGT 370
Cdd:cd14035     8 ESTFLAMDTEEGVEVVWNELffQDKKAFKAHEDKIKTMFENLTLVDHPNIVKFHKYW--LDVKDNHARVVFITEYVSSGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  371 LKMYLKRFKR----INIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNkSFAKSVI 446
Cdd:cd14035    86 LKQFLKKTKKnhktMNARAWKRWCTQILSALSYLHSCEPPIIHGNLTSDTIFIQ-HNGLIKIGSVWHRLFVN-VLPEGGV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  447 GTP-----------EFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEypysecmnpatIYRKVISGVKPECFSRI--PAQY 513
Cdd:cd14035   164 RGPlrqereelrnlHFFPPEYGSCEDGTAVDIFSFGMCALEMAVLE-----------IQANGDTRVSEEAIARArhSLED 232
                         250       260
                  ....*....|....*....|....*
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14035   233 PNMREFILSCLRHNPCKRPTAHDLL 257
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
287-544 3.38e-38

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: 144.88  E-value: 3.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER----QRFREEAEMLKDLQHPNIVRFYdywesADLCGKRKYIVLV 362
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevvEAIREEIRMMARLNHPNIVRML-----GATQHKSHFNIFV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT-LKNK-- 439
Cdd:cd06630    83 -EWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQ--IIHRDLKGANLLVDSTGQRLRIADFGAAArLASKgt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 ---SFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECM---NPATIYrKVISGVK----PECFSr 508
Cdd:cd06630   160 gagEFQGQLLGTIAFMAPEVLRgEQYGRSCDVWSVGCVIIEMATAKPPWNAEKisnHLALIF-KIASATTpppiPEHLS- 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  509 ipaqyPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06630   238 -----PGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
277-538 8.48e-38

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: 143.59  E-value: 8.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLK-FDEE--LGRGSFKTVFRGLDTETGV--AVAWCELQESKlnkTERQRFREEAEMLKDLQHPNIVRFYDYW-ESA 350
Cdd:cd13996     1 NSRYLNdFEEIelLGSGGFGSVYKVRNKVDGVtyAIKKIRLTEKS---SASEKVLREVKALAKLNHPNIVRYYTAWvEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  351 DLcgkrkYIVLvtELMTSGTLKMYLKR---FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVK 427
Cdd:cd13996    78 PL-----YIQM--ELCEGGTLRDWIDRrnsSSKNDRKLALELFKQILKGVSYIHSKG--IVHRDLKPSNIFLDNDDLQVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  428 IGDLGLAT--LKNKSFAKSV--------------IGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVtgeYPYSECMNP 490
Cdd:cd13996   149 IGDFGLATsiGNQKRELNNLnnnnngntsnnsvgIGTPLYASPEQLDgENYNEKADIYSLGIILFEML---HPFKTAMER 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  491 ATIYRKVISGVKPECFSripAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd13996   226 STILTDLRNGILPESFK---AKHPKEADLIQSLLSKNPEERPSAEQLL 270
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
274-538 3.32e-37

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 142.19  E-value: 3.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  274 KSKNGRFLKFDEELGRGS---FKTVFRGLDTETGVAVAWCELQ--ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWe 348
Cdd:cd14034     1 ESPCGRWQKRREEVNQRNvpgIDSAYLAMDTEEGVEVVWNEVQfsERKNFKLQEEKVKAVFDNLIQLEHLNIVKFHKYW- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 sADLCGKRKYIVLVTELMTSGTLKMYLKRFKR----INIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTG 424
Cdd:cd14034    80 -ADVKENRARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQ-HNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  425 SVKIGDLGLATLKNK-SFAKSVIGTPEFMAPEmYEEMYD--ESVDVYAFGMCLLEMV------TGEYPYSecmnPATIYR 495
Cdd:cd14034   158 LIKIGSVAPDTINNHvKTCREEQKNLHFFAPE-YGEVANvtTAVDIYSFGMCALEMAvleiqgNGESSYV----PQEAIN 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 392899979  496 KVISGVKPecfsripaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14034   233 SAIQLLED----------PLQREFIQKCLEVDPSKRPTARELL 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
285-543 3.93e-37

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: 142.24  E-value: 3.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTE----RQRFREEAeMLKDLQHPNIVRFYDYwesadLCGKRKyIV 360
Cdd:cd07829     5 EKLGEGTYGVVYKAKDKKTGEIVA---LKKIRLDNEEegipSTALREIS-LLKELKHPNIVKLLDV-----IHTENK-LY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA---TL 436
Cdd:cd07829    75 LVFEYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHR--ILHRDLKPQNLLINR-DGVLKLADFGLArafGI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPY---SE----------------------CMN 489
Cdd:cd07829   151 PLRTYTHEVV-TLWYRAPEilLGSKHYSTAVDIWSVGCIFAELITGKPLFpgdSEidqlfkifqilgtpteeswpgvTKL 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  490 PAtiYRKVISGVKPECF-SRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd07829   230 PD--YKPTFPKWPKNDLeKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
287-531 1.17e-36

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: 139.57  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTEL 365
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRkEVEHTLNERNILERVNHPFIVKLHYAFQT------EEKLYLVLDY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLAT--LKNKSFAK 443
Cdd:cd05123    75 VPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLG--IIYRDLKPENILLDSD-GHIKLTDFGLAKelSSDGDRTY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISG-VK-PECFSripaqyPEIREII 520
Cdd:cd05123   152 TFCGTPEYLAPEVLLgKGYGKAVDWWSLGVLLYEMLTGKPPF-YAENRKEIYEKILKSpLKfPEYVS------PEAKSLI 224
                         250
                  ....*....|.
gi 392899979  521 DRCIRVRREER 531
Cdd:cd05123   225 SGLLQKDPTKR 235
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
285-542 2.30e-36

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: 139.49  E-value: 2.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLdTETG--VAVAWCELQESKLNKTERQ--RFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIV 360
Cdd:cd06631     7 NVLGKGAYGTVYCGL-TSTGqlIAVKQVELDTSDKEKAEKEyeKLQEEVDLLKTLKHVNIVGYL------GTCLEDNVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG-------- 432
Cdd:cd06631    80 IFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNN--VIHRDIKGNNIMLM-PNGVIKLIDFGcakrlcin 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATLKNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNP-ATIYrKVISGVK-----PEC 505
Cdd:cd06631   157 LSSGSQSQLLKSMRGTPYWMAPEVInETGHGRKSDIWSIGCTVFEMATGKPPWAD-MNPmAAIF-AIGSGRKpvprlPDK 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  506 FSripaqyPEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06631   235 FS------PEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
287-538 3.90e-36

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: 138.29  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDywesADLCGKRKYIVlvTELM 366
Cdd:cd08530     8 LGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKE----AFLDGNRLCIV--MEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFK--RINIKVLKSWcR---QILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSF 441
Cdd:cd08530    82 PFGDLSKLISKRKkkRRLFPEDDIW-RifiQMLRGLKALHDQK--ILHRDLKSANILLS-AGDLVKIGDLGISKVLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQYP-EIREI 519
Cdd:cd08530   158 AKTQIGTPLYAAPEVWKGRpYDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRYKVCRGK----FPPIPPVYSqDLQQI 232
                         250
                  ....*....|....*....
gi 392899979  520 IDRCIRVRREERSTVKQLL 538
Cdd:cd08530   233 IRSLLQVNPKKRPSCDKLL 251
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
287-540 2.00e-35

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: 136.37  E-value: 2.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGlDTETGVAVAwcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCgkrkyivLVTELM 366
Cdd:cd14062     1 IGSGSFGTVYKG-RWHGDVAVK--KLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLA-------IVTQWC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYL----KRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd14062    71 EGSSLYKHLhvleTKFEMLQLIDI---ARQTAQGMDYLHAKN--IIHRDLKSNNIFLH-EDLTVKIGDFGLATVKTRWSG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPE----FMAPEMY----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISG-VKPEcFSRIPAQY 513
Cdd:cd14062   145 SQQFEQPTgsilWMAPEVIrmqdENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGyLRPD-LSKVRSDT 223
                         250       260
                  ....*....|....*....|....*...
gi 392899979  514 P-EIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:cd14062   224 PkALRRLMEDCIKFQRDERPLFPQILAS 251
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
282-539 4.79e-35

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: 135.48  E-value: 4.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFYD-YWESADLcgkrkYI 359
Cdd:cd08224     3 EIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMmDAKARQDCLKEIDLLQQLNHPNIIKYLAsFIENNEL-----NI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLvtELMTSGTLKMYLKRFKR----INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA- 434
Cdd:cd08224    78 VL--ELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKR--IMHRDIKPANVFITA-NGVVKLGDLGLGr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLKNKSF-AKSVIGTPEFMAPE-MYEEMYDESVDVYAFGmCLL-EMVTGEYP-YSECMNPATIYRKVISG----VKPECF 506
Cdd:cd08224   153 FFSSKTTaAHSLVGTPYYMSPErIREQGYDFKSDIWSLG-CLLyEMAALQSPfYGEKMNLYSLCKKIEKCeyppLPADLY 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  507 SRipaqypEIREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd08224   232 SQ------ELRDLVAACIQPDPEKRPDISYVLD 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
283-543 5.57e-35

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: 135.09  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAwCELQEsklNKTERQRFREEAEMLKDLQHPNIVRFY-------DYWESADLCGK 355
Cdd:cd06612     7 ILEKLGEGSYGSVYKAIHKETGQVVA-IKVVP---VEEDLQEIIKEISILKQCDSPYIVKYYgsyfkntDLWIVMEYCGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKyivlVTELMtsgtlKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT 435
Cdd:cd06612    83 GS----VSDIM-----KITNKTLTEEEIAAI---LYQTLKGLEYLHSNK--KIHRDIKAGNILLN-EEGQAKLADFGVSG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAK--SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPAtiyrKVISGVK---PECFSrI 509
Cdd:cd06612   148 QLTDTMAKrnTVIGTPFWMAPEVIQEIgYNNKADIWSLGITAIEMAEGKPPYSD-IHPM----RAIFMIPnkpPPTLS-D 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  510 PAQY-PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06612   222 PEKWsPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
287-543 1.23e-34

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: 134.02  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCEL-QESKLNKTERQRFREEAEMLKDLQHPNIVRFYDywesadlCGKR-KYIVLV 362
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGreLAVKQVEIdPINTEASKEVKALECEIQLLKNLQHERIVQYYG-------CLQDeKSLSIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLG----LATLKN 438
Cdd:cd06625    81 MEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANI-LRDSNGNVKLGDFGaskrLQTICS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrIPAQYPEI- 516
Cdd:cd06625   158 STGMKSVTGTPYWMSPEVINgEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQ----LPPHVSEDa 233
                         250       260
                  ....*....|....*....|....*..
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06625   234 RDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
288-542 3.72e-34

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: 132.81  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTerQRFREEAEMLKDLQHPNIVRFYdyweSADLCGKRKYIVLvtEL 365
Cdd:cd06626     9 GEGTFGKVYTAVNLDTGelMAMKEIRFQDNDPKTI--KEIADEMKVLEGLDHPNLVRYY----GVEVHREEVYIFM--EY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLAT-LKNKSFA-- 442
Cdd:cd06626    81 CQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENG--IVHRDIKPANIFLDSN-GLIKLGDFGSAVkLKNNTTTma 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 ----KSVIGTPEFMAPEMY----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrIPAQY- 513
Cdd:cd06626   158 pgevNSLVGTPAYMAPEVItgnkGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHKPP----IPDSLq 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  514 --PEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06626   234 lsPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
287-533 6.78e-34

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: 132.19  E-value: 6.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGkrkyivLVTELM 366
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLG------LVMEYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRfKRINIKvlksW------CRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKS 440
Cdd:cd13978    75 ENGSLKSLLER-EIQDVP----WslrfriIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHF-HVKISDFGLSKLGMKS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 F-------AKSVIGTPEFMAPEMYEEMY---DESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPE----CF 506
Cdd:cd13978   149 IsanrrrgTENLGGTPIYMAPEAFDDFNkkpTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSlddiGR 228
                         250       260
                  ....*....|....*....|....*..
gi 392899979  507 SRIPAQYPEIREIIDRCIRVRREERST 533
Cdd:cd13978   229 LKQIENVQELISLMIRCWDGNPDARPT 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
285-542 6.86e-34

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: 132.43  E-value: 6.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDYWESADLCGKRKYIVLVT 363
Cdd:cd06608    12 EVIGEGTYGKVYKARHKKTGQLAA---IKIMDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGGDDQLWLVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSW----CRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL-ATLKN 438
Cdd:cd06608    89 EYCGGGSVTDLVKGLRKKGKRLKEEWiayiLRETLRGLAYLHENK--VIHRDIKGQNILLT-EEAEVKLVDFGVsAQLDS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAK-SVIGTPEFMAPEM------YEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSriPA 511
Cdd:cd06608   166 TLGRRnTFIGTPYWMAPEViacdqqPDASYDARCDVWSLGITAIELADGKPPLCD-MHPMRALFKIPRNPPPTLKS--PE 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  512 QYP-EIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06608   243 KWSkEFNDFISECLIKNYEQRPFTEELLEHPF 274
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
285-538 7.68e-34

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: 132.23  E-value: 7.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG---LDTETGVavawceLQESKLNKTERQRfreEAEMLKDLQHPNIVRFYDYWESADLC-------- 353
Cdd:cd14047    12 ELIGSGGFGQVFKAkhrIDGKTYA------IKRVKLNNEKAER---EVKALAKLDHPNIVRYNGCWDGFDYDpetsssns 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 --GKRKYIVLVTELMTSGTLKMYLKR---FKRINIKVLKSWcRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKI 428
Cdd:cd14047    83 srSKTKCLFIQMEFCEKGTLESWIEKrngEKLDKVLALEIF-EQITKGVEYIHSKK--LIHRDLKPSNIFLV-DTGKVKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLAT-LKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVtgeYPYSECMNPATIYRKVISGVKPECF 506
Cdd:cd14047   159 GDFGLVTsLKNDGKRTKSKGTLSYMSPEQISsQDYGKEVDIYALGLILFELL---HVCDSAFEKSKFWTDLRNGILPDIF 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  507 SRipaQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14047   236 DK---RYKIEKTIIKKMLSKKPEDRPNASEIL 264
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
285-542 1.24e-33

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: 131.73  E-value: 1.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQESKL-NKTERQR-----FREEAEMLKDLQHPNIVRFYDYWESADlcgkr 356
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGemLAVKQVELPKTSSdRADSRQKtvvdaLKSEIDTLKDLDHPNIVQYLGFEETED----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL--- 433
Cdd:cd06629    82 -YFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKG--ILHRDLKADNILVD-LEGICKISDFGIskk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 -ATLKNKSFAKSVIGTPEFMAPEM---YEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrI 509
Cdd:cd06629   158 sDDIYGNNGATSMQGSVFWMAPEVihsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPP----V 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  510 PAQY---PEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06629   234 PEDVnlsPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
285-543 1.40e-33

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: 131.27  E-value: 1.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQEsklnKTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYIVLV 362
Cdd:cd06613     6 QRIGSGTYGDVYKARNIATGelAAVKVIKLEP----GDDFEIIQQEISMLKECRHPNIVAYFGSYL------RRDKLWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd06613    76 MEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTG--KIHRDIKGANILLT-EDGDVKLADFGVSAQLTATIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 K--SVIGTPEFMAPEMYEE----MYDESVDVYAFGMCLLEMVTGEYPYSEcMNPA-TIYRKVISGVKPECFSRIPAQYPE 515
Cdd:cd06613   153 KrkSFIGTPYWMAPEVAAVerkgGYDGKCDIWALGITAIELAELQPPMFD-LHPMrALFLIPKSNFDPPKLKDKEKWSPD 231
                         250       260
                  ....*....|....*....|....*...
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06613   232 FHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
287-542 2.28e-33

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: 130.25  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcGKRKYIVLVTELM 366
Cdd:cd08223     8 IGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFE-----GEDGFLYIVMGFC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINI--KVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA-TLKNKS-FA 442
Cdd:cd08223    83 EGGDLYTRLKEQKGVLLeeRQVVEWFVQIAMALQYMHERN--ILHRDLKTQNIFLT-KSNIIKVGDLGIArVLESSSdMA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYS-ECMNpATIYrKVISGVKPEcfsrIPAQY-PEIREI 519
Cdd:cd08223   160 TTLIGTPYYMSPELFSNKpYNHKSDVWALGCCVYEMATLKHAFNaKDMN-SLVY-KILEGKLPP----MPKQYsPELGEL 233
                         250       260
                  ....*....|....*....|...
gi 392899979  520 IDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd08223   234 IKAMLHQDPEKRPSVKRILRQPY 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
287-538 3.84e-33

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: 130.09  E-value: 3.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG-LDTETGVAVAWcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDY-WESADLCgkrkyivLVTE 364
Cdd:cd14066     1 IGSGGFGTVYKGvLENGTVVAVKR---LNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYcLESDEKL-------LVYE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKriNIKVLkSW------CRQILKGLSFLHT-RNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLK 437
Cdd:cd14066    71 YMPNGSLEDRLHCHK--GSPPL-PWpqrlkiAKGIARGLEYLHEeCPPPIIHGDIKSSNILLD-EDFEPKLTDFGLARLI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKS----VIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPAT------IYRKVISGVKPECF 506
Cdd:cd14066   147 PPSESVSktsaVKGTIGYLAPEYIRTGrVSTKSDVYSFGVVLLELLTGKPAVDENRENASrkdlveWVESKGKEELEDIL 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  507 S-RIPAQYPEIREIIDR-------CIRVRREERSTVKQLL 538
Cdd:cd14066   227 DkRLVDDDGVEEEEVEAllrlallCTRSDPSLRPSMKEVV 266
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
274-543 4.78e-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: 4.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  274 KSKNGRFLKfdeeLGRGSFKTVFRGLDTETGVAVAwcelqESKLNKTERQRfRE----EAEMLKDLQHPNIVRFYDYWes 349
Cdd:cd06648     6 RSDLDNFVK----IGEGSTGIVCIATDKSTGRQVA-----VKKMDLRKQQR-REllfnEVVIMRDYQHPNIVEMYSSY-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  350 adLCGKRKYIVLvtELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIG 429
Cdd:cd06648    74 --LVGDELWVVM--EFLEGGALTDIVTH-TRMNEEQIATVCRAVLKALSFLHSQG--VIHRDIKSDSILLT-SDGRVKLS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLATLKNKSFA--KSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcmNPATIYRKVISGVKPECF 506
Cdd:cd06648   146 DFGFCAQVSKEVPrrKSLVGTPYWMAPEVIsRLPYGTEVDIWSLGIMVIEMVDGEPPYFN--EPPLQAMKRIRDNEPPKL 223
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  507 SRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06648   224 KNLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
281-544 5.00e-32

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: 126.69  E-value: 5.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQeSKLNKTERQRFREEAEMLKDLQHPNIVRFYD--YWESAdlcgkrky 358
Cdd:cd06605     3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIR-LEIDEALQKQILRELDVLHKCNSPYIVGFYGafYSEGD-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd06605    74 ISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHE-KHKIIHRDVKPSNILVN-SRGQVKLCDFGVSGQLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEC-----MNPATIYRKVISGVKPecfsRIPAQ 512
Cdd:cd06605   152 DSLAKTFVGTRSYMAPErISGGKYTVKSDIWSLGLSLVELATGRFPYPPPnakpsMMIFELLSYIVDEPPP----LLPSG 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  513 Y--PEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06605   228 KfsPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
287-481 6.16e-32

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: 126.20  E-value: 6.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDL----QHPNIVRFYDYWESadlcGKRKYIVLV 362
Cdd:cd05118     7 IGEGAFGTVWLARDKVTGEKVA---IKKIKNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEH----RGGNHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd05118    80 FELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNG--IIHRDLKPENILINLELGQLKLADFGLARSFTSPPY 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392899979  443 KSVIGTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd05118   158 TPYVATRWYRAPEVLLGAkpYGSSIDIWSLGCILAELLTGR 198
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
285-538 7.18e-32

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: 126.59  E-value: 7.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRfreEAEMLKDLQHPNIVRFYdywESAdLCGKRKYIVLv 362
Cdd:cd06609     7 ERIGKGSFGEVYKGIDKRTNqvVAIKVIDLEEAEDEIEDIQQ---EIQFLSQCDSPYITKYY---GSF-LKGSKLWIIM- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTLKMYLK--RFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT----- 435
Cdd:cd06609    79 -EYCGGGSVLDLLKpgPLDETYIAFI---LREVLLGLEYLHSEG--KIHRDIKAANILLS-EEGDVKLADFGVSGqltst 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 -LKNKSFaksvIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPAtiyrKVIsgvkpecfSRIPAQY 513
Cdd:cd06609   152 mSKRNTF----VGTPFWMAPEvIKQSGYDEKADIWSLGITAIELAKGEPPLSD-LHPM----RVL--------FLIPKNN 214
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  514 P----------EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd06609   215 PpslegnkfskPFKDFVELCLNKDPKERPSAKELL 249
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
277-543 4.76e-31

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: 123.88  E-value: 4.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKFdEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERqrFREEAEMLKDLQHPNIVRFYDYWesadLCGKR 356
Cdd:cd06647     6 KKKYTRF-EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSY----LVGDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLvtELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGL-AT 435
Cdd:cd06647    79 LWVVM--EYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDFGFcAQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAKS-VIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPEcFSRIPAQY 513
Cdd:cd06647   153 ITPEQSKRStMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPE-LQNPEKLS 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06647   231 AIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
287-542 4.80e-31

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: 124.18  E-value: 4.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQR-----FREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYI 359
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGelMAVKQVELPSVSAENKDRKKsmldaLQREIALLRELQHENIVQYLGSSSDAN------HL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA----- 434
Cdd:cd06628    82 NIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRG--IIHRDIKGANILVD-NKGGIKISDFGISkklea 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 ---TLKNKSFAKSVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrKVISGVKPECFSRIP 510
Cdd:cd06628   159 nslSTKNNGARPSLQGSVFWMAPEVVKQtSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIF-KIGENASPTIPSNIS 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  511 AqypEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06628   238 S---EARDFLEKTFEIDHNKRPTADELLKHPF 266
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
287-537 5.03e-31

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: 123.70  E-value: 5.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSF----KTVFRGLDtetgVAVAWCELQesklnkTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLV 362
Cdd:cd14058     1 VGRGSFgvvcKARWRNQI----VAVKIIESE------SEKKAFEVEVRQLSRVDHPNIIKLYG------ACSNQKPVCLV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLK---SWCRQILKGLSFLHTRNP-PVIHRDLKCDNIFITGTTGSVKIGDLGLATLK- 437
Cdd:cd14058    65 MEYAEGGSLYNVLHGKEPKPIYTAAhamSWALQCAKGVAYLHSMKPkALIHRDLKPPNLLLTNGGTVLKICDFGTACDIs 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 -NKSFAKsviGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVIS-GVKPECFSRIPAQyp 514
Cdd:cd14058   145 tHMTNNK---GSAAWMAPEVFEgSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHnGERPPLIKNCPKP-- 219
                         250       260
                  ....*....|....*....|...
gi 392899979  515 eIREIIDRCIRVRREERSTVKQL 537
Cdd:cd14058   220 -IESLMTRCWSKDPEKRPSMKEI 241
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
287-538 6.97e-31

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: 123.35  E-value: 6.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK--LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd14098     8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQ------HIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLATL-KNKSFA 442
Cdd:cd14098    82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMG--ITHRDLKPENILITQDDPViVKISDFGLAKViHTGTFL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYEEM-------YDESVDVYAFGMCLLEMVTGEYPYSECmNPATIYRKVISG---VKPECFSRIPaq 512
Cdd:cd14098   160 VTFCGTMAYLAPEILMSKeqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGS-SQLPVEKRIRKGrytQPPLVDFNIS-- 236
                         250       260
                  ....*....|....*....|....*.
gi 392899979  513 yPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14098   237 -EEAIDFILRLLDVDPEKRMTAAQAL 261
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
286-544 7.01e-31

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: 124.08  E-value: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGV--AVAWCELQESKlnktERQRFREEAEMLKDLQHPNIVRFYD-------YWESADLCGKR 356
Cdd:cd06611    12 ELGDGAFGKVYKAQHKETGLfaAAKIIQIESEE----ELEDFMVEIDILSECKHPNIVGLYEayfyenkLWILIEFCDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMtsgtlkmylKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd06611    88 ALDSIMLELE---------RGLTEPQIRYV---CRQMLEALNFLHSHK--VIHRDLKAGNILLT-LDGDVKLADFGVSAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAK--SVIGTPEFMAPE--MYEEM----YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGvKPECFSR 508
Cdd:cd06611   153 NKSTLQKrdTFIGTPYWMAPEvvACETFkdnpYDYKADIWSLGITLIELAQMEPPHHE-LNPMRVLLKILKS-EPPTLDQ 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  509 IPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06611   231 PSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
287-542 1.66e-30

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: 122.52  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYIVLVTELM 366
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIPER--DSREVQPLHEEIALHSRLSHKNIVQYLGS------VSEDGFFKIFMEQV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLkRFK----RINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITGTTGSVKIGDLG----LATLK- 437
Cdd:cd06624    88 PGGSLSALL-RSKwgplKDNENTIGYYTKQILEGLKYLH--DNKIVHRDIKGDNVLVNTYSGVVKISDFGtskrLAGINp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 -NKSFAksviGTPEFMAPEMYEE---MYDESVDVYAFGMCLLEMVTGEYPYSECMNP-ATIYRKVISGVKPEcfsrIPAQ 512
Cdd:cd06624   165 cTETFT----GTLQYMAPEVIDKgqrGYGPPADIWSLGCTIIEMATGKPPFIELGEPqAAMFKVGMFKIHPE----IPES 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  513 YPE-IREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06624   237 LSEeAKSFILRCFEPDPDKRATASDLLQDPF 267
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
286-542 2.04e-30

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: 122.83  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGvAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYD--YWEsadlcGKrkyIVLVT 363
Cdd:cd06644    19 ELGDGAFGKVYKAKNKETG-ALAAAKVIETK-SEEELEDYMVEIEILATCNHPYIVKLLGafYWD-----GK---LWIMI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd06644    89 EFCPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMK--IIHRDLKAGNVLLT-LDGDIKLADFGVSAKNVKTLQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 K--SVIGTPEFMAPE--MYEEM----YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSriPAQY- 513
Cdd:cd06644   166 RrdSFIGTPYWMAPEvvMCETMkdtpYDYKADIWSLGITLIEMAQIEPPHHE-LNPMRVLLKIAKSEPPTLSQ--PSKWs 242
                         250       260
                  ....*....|....*....|....*....
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06644   243 MEFRDFLKTALDKHPETRPSAAQLLEHPF 271
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
287-543 2.11e-30

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: 121.59  E-value: 2.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVA------WCELQESKLNKTERqrfreEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14081     9 LGKGQTGLVKLAKHCVTGQKVAikivnkEKLSKESVLMKVER-----EIAIMKLIEHPNVLKLYDVYEN------KKYLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-KNK 439
Cdd:cd14081    78 LVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHS--ICHRDLKPENLLLDE-KNNIKIADFGMASLqPEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEM-YEEMYD-ESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVkpecFsRIPAQY-PEI 516
Cdd:cd14081   155 SLLETSCGSPHYACPEViKGEKYDgRKADIWSCGVILYALLVGALPFDD-DNLRQLLEKVKRGV----F-HIPHFIsPDA 228
                         250       260
                  ....*....|....*....|....*..
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14081   229 QDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
287-522 2.73e-30

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: 121.63  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTELM 366
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIAL------RGVCLNPPHLCLVMEYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNP-PVIHRDLKCDNIFI---------TGTTgsVKIGDLGLATL 436
Cdd:cd14148    76 RGGALNRALAG-KKVPPHVLVNWAVQIARGMNYLHNEAIvPIIHRDLKSSNILIlepienddlSGKT--LKITDFGLARE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSE----------CMNPATIyrkVISGVKPEC 505
Cdd:cd14148   153 WHKTTKMSAAGTYAWMAPEVIRlSLFSKSSDVWSFGVLLWELLTGEVPYREidalavaygvAMNKLTL---PIPSTCPEP 229
                         250       260
                  ....*....|....*....|....*
gi 392899979  506 FSRI--------PAQYPEIREIIDR 522
Cdd:cd14148   230 FARLleecwdpdPHGRPDFGSILKR 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
281-535 3.25e-30

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: 121.94  E-value: 3.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR--FREEaEMLKDLQHPNIVRFYDYWESADlcgkRKY 358
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKyvTIEK-EVLSRLAHPGIVKLYYTFQDES----KLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-- 436
Cdd:cd05581    78 FVL--EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKG--IIHRDLKPENILLDE-DMHIKITDFGTAKVlg 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -----------------KNKSFAKSVIGTPEFMAPEMYEEMY-DESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVI 498
Cdd:cd05581   153 pdsspestkgdadsqiaYNQARAASFVGTAEYVSPELLNEKPaGKSSDLWALGCIIYQMLTGKPPFR-GSNEYLTFQKIV 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  499 SgvkpeCFSRIPAQYPEI-REIIDRCIRVRREERSTVK 535
Cdd:cd05581   232 K-----LEYEFPENFPPDaKDLIQKLLVLDPSKRLGVN 264
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
285-484 4.93e-30

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: 120.82  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELqeSKLNKTER--QRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLV 362
Cdd:cd14002     7 ELIGEGSFGKVYKGRRKYTGQVVALKFI--PKRGKSEKelRNLRQEIEILRKLNHPNIIEMLDSFET------KKEFVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELmTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL--KNKS 440
Cdd:cd14002    79 TEY-AQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNR--IIHRDMKPQNILI-GKGGVVKLCDFGFARAmsCNTL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  441 FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14002   155 VLTSIKGTPLYMAPELVQEQpYDHTADLWSLGCILYELFVGQPPF 199
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
288-538 6.56e-30

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: 120.06  E-value: 6.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETGVAVAwcelqESKLNKTERqrfreEAEMLKDLQHPNIVRFYDY-WESADLCgkrkyivLVTELM 366
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVA-----VKKLLKIEK-----EAEILSVLSHRNIIQFYGAiLEAPNYG-------IVTEYA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYL--KRFKRINIKVLKSWCRQILKGLSFLHTRNP-PVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAK 443
Cdd:cd14060    65 SYGSLFDYLnsNESEEMDMDQIMTWATDIAKGMHYLHMEAPvKVIHRDLKSRNVVIA-ADGVLKICDFGASRFHSHTTHM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQYPeirEIIDR 522
Cdd:cd14060   144 SLVGTFPWMAPEVIQSLpVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPTIPSSCPRSFA---ELMRR 220
                         250
                  ....*....|....*.
gi 392899979  523 CIRVRREERSTVKQLL 538
Cdd:cd14060   221 CWEADVKERPSFKQII 236
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
285-485 7.43e-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: 120.09  E-value: 7.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL---DTETGVAVAwCeLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDY-WESadlcgkrKYIV 360
Cdd:cd14121     1 EKLGSGTYATVYKAYrksGAREVVAVK-C-VSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFqWDE-------EHIY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSV-KIGDLGLAT-LKN 438
Cdd:cd14121    72 LIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHN--ISHMDLKPQNLLLSSRYNPVlKLADFGFAQhLKP 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  439 KSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:cd14121   150 NDEAHSLRGSPLYMAPEMIlKKKYDARVDLWSVGVILYECLFGRAPFA 197
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
287-538 9.49e-30

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: 119.84  E-value: 9.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDTETGVAVAWCELQEskLNKTERQRFREEAEMLKDLQHPNIVRFYD-YWESadlcgkrKYIVLVT 363
Cdd:cd08220     8 VGRGAYGTVYlcRRKDDNKLVIIKQIPVEQ--MTKEERQAALNEVKVLSMLHHPNIIEYYEsFLED-------KALMIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINI---KVLKSWCrQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLA-TLKNK 439
Cdd:cd08220    79 EYAPGGTLFEYIQQRKGSLLseeEILHFFV-QILLALHHVHSKQ--ILHRDLKTQNILLNKKRTVVKIGDFGISkILSSK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQY-PEIR 517
Cdd:cd08220   156 SKAYTVVGTPCYISPELCEgKPYNQKSDIWALGCVLYELASLKRAF-EAANLPALVLKIMRGT----FAPISDRYsEELR 230
                         250       260
                  ....*....|....*....|.
gi 392899979  518 EIIDRCIRVRREERSTVKQLL 538
Cdd:cd08220   231 HLILSMLHLDPNKRPTLSEIM 251
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
286-544 1.91e-29

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: 119.75  E-value: 1.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYD--YWESAdlcgkrkyIVLVT 363
Cdd:cd06643    12 ELGDGAFGKVYKAQNKETGILAA-AKVIDTK-SEEELEDYMVEIDILASCDHPNIVKLLDafYYENN--------LWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRI----NIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd06643    82 EFCAGGAVDAVMLELERPltepQIRVV---CKQTLEALVYLHENK--IIHRDLKAGNILFT-LDGDIKLADFGVSAKNTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAK--SVIGTPEFMAPEMY------EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSriPA 511
Cdd:cd06643   156 TLQRrdSFIGTPYWMAPEVVmcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHE-LNPMRVLLKIAKSEPPTLAQ--PS 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  512 QY-PEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06643   233 RWsPEFKDFLRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
285-538 3.48e-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: 119.12  E-value: 3.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRfreEAEMLKDLQH---PNIVRFYDYWesadLCGKRKYI 359
Cdd:cd06917     7 ELVGRGSYGAVYRGYHVKTGrvVALKVLNLDTDDDDVSDIQK---EVALLSQLKLgqpKNIIKYYGSY----LKGPSLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLvtELMTSGTLKMyLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd06917    80 IM--DYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDG--IIHRDIKAANILVT-NTGNVKLCDFGVAASLNQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAK--SVIGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrkVISGVKPecfSRIPAQY-- 513
Cdd:cd06917   154 NSSKrsTFVGTPYWMAPEVITEgkYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVM--LIPKSKP---PRLEGNGys 228
                         250       260
                  ....*....|....*....|....*
gi 392899979  514 PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd06917   229 PLLKEFVAACLDEEPKDRLSADELL 253
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
285-538 6.09e-29

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: 117.60  E-value: 6.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYIVLVTE 364
Cdd:cd08218     6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFE------ENGNLYIVMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLkmylkrFKRINIK---------VLkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT 435
Cdd:cd08218    80 YCDGGDL------YKRINAQrgvlfpedqIL-DWFVQLCLALKHVHDRK--ILHRDIKSQNIFLT-KDGIIKLGDFGIAR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKS--FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVKPEcfsrIPAQ 512
Cdd:cd08218   150 VLNSTveLARTCIGTPYYLSPEICENKpYNNKSDIWALGCVLYEMCTLKHAF-EAGNMKNLVLKIIRGSYPP----VPSR 224
                         250       260
                  ....*....|....*....|....*..
gi 392899979  513 YP-EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd08218   225 YSyDLRSLVSQLFKRNPRDRPSINSIL 251
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
287-538 1.23e-28

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: 117.11  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRF------REEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIV 360
Cdd:cd14084    14 LGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREInkprniETEIEILKKLSHPCIIKIEDFFDAED----DYYIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGT--TGSVKIGDLGLAT-LK 437
Cdd:cd14084    90 L--ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNG--IIHRDLKPENVLLSSQeeECLIKITDFGLSKiLG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTPEFMAPEMY----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVkpecFSRIPAQY 513
Cdd:cd14084   166 ETSLMKTLCGTPTYLAPEVLrsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSGK----YTFIPKAW 241
                         250       260
                  ....*....|....*....|....*....
gi 392899979  514 PEIRE----IIDRCIRVRREERSTVKQLL 538
Cdd:cd14084   242 KNVSEeakdLVKKMLVVDPSRRPSIEEAL 270
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
285-539 1.28e-28

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: 117.04  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGlDTETGVAVAWceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWesadlcgKRKYIVLVTE 364
Cdd:cd14150     6 KRIGTGSFGTVFRG-KWHGDVAVKI--LKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFM-------TRPNFAIITQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI-TGTTgsVKIGDLGLATLKNKSFA 442
Cdd:cd14150    76 WCEGSSLYRHLHVTEtRFDTMQLIDVARQTAQGMDYLHAKN--IIHRDLKSNNIFLhEGLT--VKIGDFGLATVKTRWSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPE----FMAPEMYEEM----YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQYP 514
Cdd:cd14150   152 SQQVEQPSgsilWMAPEVIRMQdtnpYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLSKLSSNCP 231
                         250       260
                  ....*....|....*....|....*.
gi 392899979  515 E-IREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd14150   232 KaMKRLLIDCLKFKREERPLFPQILV 257
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
272-546 2.11e-28

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: 116.35  E-value: 2.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  272 IDKSKngrfLKFDEELGRGSFKTVFRGL-DTETGVAVAwcELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYDywesa 350
Cdd:cd05068     5 IDRKS----LKLLRKLGSGQFGEVWEGLwNNTTPVAVK--TLKPGTMDPED---FLREAQIMKKLRHPKLIQLYA----- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  351 dLCGKRKYIVLVTELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIG 429
Cdd:cd05068    71 -VCTLEEPIYIITELMKHGSLLEYLQGKGRsLQLPQLIDMAAQVASGMAYLESQN--YIHRDLAARNVLV-GENNICKVA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLA-TLKNKSFAKSVIGTP---EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVK 502
Cdd:cd05068   147 DFGLArVIKVEDEYEAREGAKfpiKWTAPEaaNYNRFSIKS-DVWSFGILLTEIVTyGRIPYPG-MTNAEVLQQVERGYR 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 392899979  503 PECFSRIPaqyPEIREIIDRCIRVRREERSTVK--QLLVDDFFTPE 546
Cdd:cd05068   225 MPCPPNCP---PQLYDIMLECWKADPMERPTFEtlQWKLEDFFVND 267
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
287-542 2.82e-28

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: 115.91  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ---ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLVT 363
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKQVQfdpESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDP----QERTLSIFM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLG----LATL-KN 438
Cdd:cd06652    86 EYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNM--IVHRDIKGANI-LRDSVGNVKLGDFGaskrLQTIcLS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrIPAQYPE-I 516
Cdd:cd06652   163 GTGMKSVTGTPYWMSPEVISgEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQ----LPAHVSDhC 238
                         250       260
                  ....*....|....*....|....*.
gi 392899979  517 REIIDRcIRVRREERSTVKQLLVDDF 542
Cdd:cd06652   239 RDFLKR-IFVEAKLRPSADELLRHTF 263
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
283-541 4.13e-28

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: 115.17  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEE--LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDYWESADlcgkrkYI 359
Cdd:cd13997     2 FHELeqIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGG------HL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINI---KVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd13997    76 YIQMELCENGSLQDALEELSPISKlseAEVWDLLLQVALGLAFIHSKG--IVHLDIKPDNIFIS-NKGTCKIGDFGLATR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSViGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTG-EYPYSecmnpATIYRKVISGVKPECFSRIPAQy 513
Cdd:cd13997   153 LETSGDVEE-GDSRYLAPELLNEnyTHLPKADIFSLGVTVYEAATGePLPRN-----GQQWQQLRQGKLPLPPGLVLSQ- 225
                         250       260
                  ....*....|....*....|....*...
gi 392899979  514 pEIREIIDRCIRVRREERSTVKQLLVDD 541
Cdd:cd13997   226 -ELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
281-534 5.46e-28

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: 115.12  E-value: 5.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG---LDTETgVAVAWCELQEsKLNKTERQRFREEAEMLKDLQHPNIVRFYD-YWESADLCgkr 356
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRAtclLDRKP-VALKKVQIFE-MMDAKARQDCVKEIDLLKQLNHPNVIKYLDsFIEDNELN--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kyivLVTELMTSGTLKMYLKRFKR----INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLG 432
Cdd:cd08228    79 ----IVLELADAGDLSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMHSRR--VMHRDIKPANVFITA-TGVVKLGDLG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATL--KNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYP-YSECMNPATIYRKVisgvkPEC-FS 507
Cdd:cd08228   152 LGRFfsSKTTAAHSLVGTPYYMSPErIHENGYNFKSDIWSLGCLLYEMAALQSPfYGDKMNLFSLCQKI-----EQCdYP 226
                         250       260
                  ....*....|....*....|....*....
gi 392899979  508 RIPAQY--PEIREIIDRCIRVRREERSTV 534
Cdd:cd08228   227 PLPTEHysEKLRELVSMCIYPDPDQRPDI 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
282-543 7.19e-28

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: 114.76  E-value: 7.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRG--LDTETGVAVAWCELQESKlnkTERQRFREEAEMLKDLQHPNIVRFYdyweSADLCGKRKYI 359
Cdd:cd06610     4 ELIEVIGSGATAVVYAAycLPKKEKVAIKRIDLEKCQ---TSMDELRKEIQAMSQCNHPNVVSYY----TSFVVGDELWL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLvtELMTSGTLKMYLKRfkRINIKVLKSWC-----RQILKGLSFLHtRNPpVIHRDLKCDNIFItGTTGSVKIGDLGLA 434
Cdd:cd06610    77 VM--PLLSGGSLLDIMKS--SYPRGGLDEAIiatvlKEVLKGLEYLH-SNG-QIHRDVKAGNILL-GEDGSVKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 -------TLKNKSfAKSVIGTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPEC 505
Cdd:cd06610   150 aslatggDRTRKV-RKTFVGTPCWMAPEVMEQVrgYDFKADIWSFGITAIELATGAAPYSK-YPPMKVLMLTLQNDPPSL 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 392899979  506 --------FSRipaqypEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06610   228 etgadykkYSK------SFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
287-544 1.49e-27

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: 113.51  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT--ERQrFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLvtE 364
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgvEHQ-LRREVEIQSHLRHPNILRLYGYFHDA----TRVYLIL--E 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKNKSFAKS 444
Cdd:cd14116    86 YAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKR--VIHRDIKPENLLL-GSAGELKIADFGWSVHAPSSRRTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVisgvkpecfSRIPAQYP-----EIRE 518
Cdd:cd14116   163 LCGTLDYLPPEMIEgRMHDEKVDLWSLGVLCYEFLVGKPPF-EANTYQETYKRI---------SRVEFTFPdfvteGARD 232
                         250       260
                  ....*....|....*....|....*.
gi 392899979  519 IIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd14116   233 LISRLLKHNPSQRPMLREVLEHPWIT 258
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
279-537 2.20e-27

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: 112.87  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFlKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLN-KTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrk 357
Cdd:cd14073     2 RY-ELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEdEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKD------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL- 436
Cdd:cd14073    75 KIVIVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNG--VVHRDLKLENILLD-QNGNAKIADFGLSNLy 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVKPEcfsriPAQYP 514
Cdd:cd14073   152 SKDKLLQTFCGSPLYASPEIVNGTpyQGPEVDCWSLGVLLYTLVYGTMPF-DGSDFKRLVKQISSGDYRE-----PTQPS 225
                         250       260
                  ....*....|....*....|...
gi 392899979  515 EIREIIDRCIRVRREERSTVKQL 537
Cdd:cd14073   226 DASGLIRWMLTVNPKRRATIEDI 248
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
287-505 2.50e-27

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: 113.70  E-value: 2.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTE 364
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGeyVAIKKCRQELSPSDK-NRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPNDLPLLAME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRF------KRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSV--KIGDLGLAT- 435
Cdd:cd13989    80 YCSGGDLRKVLNQPenccglKESEVRTL---LSDISSAISYLHENR--IIHRDLKPENIVLQQGGGRViyKLIDLGYAKe 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  436 LKNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGvKPEC 505
Cdd:cd13989   155 LDQGSLCTSFVGTLQYLAPElFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQPVQWHGKVKQK-KPEH 224
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
285-486 3.57e-27

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: 112.42  E-value: 3.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCgkrkYIVLvtE 364
Cdd:cd14069     7 QTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQ----YLFL--E 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLkmylkrFKRIN------IKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-- 436
Cdd:cd14069    81 YASGGEL------FDKIEpdvgmpEDVAQFYFQQLMAGLKYLHSCG--ITHRDIKPENLLLDE-NDNLKISDFGLATVfr 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392899979  437 -KNKS-FAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14069   152 yKGKErLLNKMCGTLPYVAPELLakKKYRAEPVDVWSCGIVLFAMLAGELPWDQ 205
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
282-538 6.66e-27

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: 111.63  E-value: 6.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDYWESADlcgkRKYIV 360
Cdd:cd14050     4 TILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKG----ILYIQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 lvTELmTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNK 439
Cdd:cd14050    80 --TEL-CDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHG--LIHLDIKPANIFLS-KDGVCKLGDFGLVVeLDKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTG-EYPYSecmnpATIYRKVISGVKP-ECFSRIPaqyPEIR 517
Cdd:cd14050   154 DIHDAQEGDPRYMAPELLQGSFTKAADIFSLGITILELACNlELPSG-----GDGWHQLRQGYLPeEFTAGLS---PELR 225
                         250       260
                  ....*....|....*....|.
gi 392899979  518 EIIDRCIRVRREERSTVKQLL 538
Cdd:cd14050   226 SIIKLMMDPDPERRPTAEDLL 246
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
287-542 8.73e-27

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: 112.03  E-value: 8.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwCELQEskLNKT----ERQRFRE----EAEMLKDLQHPNIVRFYDYWE--SADLCgkr 356
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVA-CKIHQ--LNKDwseeKKQNYIKhalrEYEIHKSLDHPRIVKLYDVFEidTDSFC--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kyivLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFI--TGTTGSVKIGDLGLA 434
Cdd:cd13990    82 ----TVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKPPIIHYDLKPGNILLhsGNVSGEIKITDFGLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TL-KNKSFAKSVI-------GTPEFMAPEMYE-----EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYR-KVISG 500
Cdd:cd13990   158 KImDDESYNSDGMeltsqgaGTYWYLPPECFVvgktpPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEeNTILK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392899979  501 VKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd13990   238 ATEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
287-543 1.10e-26

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: 111.17  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLvtEL 365
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPhQREKIVNEIELHRDLHHKHVVKFSHHFEDAE----NIYIFL--EL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKS--FAK 443
Cdd:cd14189    83 CSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKG--ILHRDLKLGNFFINENM-ELKVGDFGLAARLEPPeqRKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYR--KVISGVKPECFSripaqyPEIREII 520
Cdd:cd14189   160 TICGTPNYLAPEvLLRQGHGPESDVWSLGCVMYTLLCGNPPF-ETLDLKETYRciKQVKYTLPASLS------LPARHLL 232
                         250       260
                  ....*....|....*....|...
gi 392899979  521 DRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14189   233 AGILKRNPGDRLTLDQILEHEFF 255
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
287-545 1.20e-26

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: 111.27  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ---ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgKRKYIVLVt 363
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPE---EKKLSIFV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLGLAT-----LKN 438
Cdd:cd06653    86 EYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGASKriqtiCMS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPecfsripaQYPEir 517
Cdd:cd06653   163 GTGIKSVTGTPYWMSPEVISgEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKP--------QLPD-- 232
                         250       260
                  ....*....|....*....|....*...
gi 392899979  518 EIIDRCirvrreeRSTVKQLLVDDFFTP 545
Cdd:cd06653   233 GVSDAC-------RDFLRQIFVEEKRRP 253
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
281-544 1.50e-26

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: 110.75  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesadLCGKRKYI 359
Cdd:cd05067     9 LKLVERLGAGQFGEVWMGYyNGHTKVAI-----KSLKQGSMSPDAFLAEANLMKQLQHQRLVRLY-------AVVTQEPI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINIKVLK--SWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL- 436
Cdd:cd05067    77 YIITEYMENGSLVDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERN--YIHRDLRAANILVSDTL-SCKIADFGLARLi 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATIyRKVISGVKPECFSRIPA 511
Cdd:cd05067   154 eDNEYTAREGAKFPiKWTAPEAinYGTFTIKS-DVWSFGILLTEIVThGRIPYPGMTNPEVI-QNLERGYRMPRPDNCPE 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  512 qypEIREIIDRCIRVRREERSTVKQL--LVDDFFT 544
Cdd:cd05067   232 ---ELYQLMRLCWKERPEDRPTFEYLrsVLEDFFT 263
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
287-538 1.58e-26

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: 109.89  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVawcelqesklnkterQRFREEAEM----LKDLQHPNIVRFydywesADLCGKRKYIVLV 362
Cdd:cd14059     1 LGSGAQGAVFLGKFRGEEVAV---------------KKVRDEKETdikhLRKLNHPNIIKF------KGVCTQAPCYCIL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKSF 441
Cdd:cd14059    60 MEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHK--IIHRDLKSPNVLVT-YNDVLKISDFGTSKeLSEKST 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrkvisGVKPECFS-RIPAQYPE-IRE 518
Cdd:cd14059   137 KMSFAGTVAWMAPEVIRnEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIW-----GVGSNSLQlPVPSTCPDgFKL 211
                         250       260
                  ....*....|....*....|
gi 392899979  519 IIDRCIRVRREERSTVKQLL 538
Cdd:cd14059   212 LMKQCWNSKPRNRPSFRQIL 231
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
281-500 1.59e-26

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: 111.52  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETG--VAVawcelqeSKLNKTERQRFRE------EAEMLKDLQHPNIVRFYDYWESAdl 352
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGkyYAL-------KILKKAKIIKLKQvehvlnEKRILSEVRHPFIVNLLGSFQDD-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 cgkrKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLG 432
Cdd:cd05580    74 ----RNLYMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLD--IVYRDLKPENLLL-DSDGHIKITDFG 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  433 LAT-LKNKSFakSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGeYP--YSEcmNPATIYRKVISG 500
Cdd:cd05580   147 FAKrVKDRTY--TLCGTPEYLAPEiILSKGHGKAVDWWALGILIYEMLAG-YPpfFDE--NPMKIYEKILEG 213
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
285-543 1.86e-26

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: 110.91  E-value: 1.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRFRE----EAEMLKDLQ-HPNIVRFYDYWESAdlcgkrK 357
Cdd:cd14093     9 EILGRGVSSTVRRCIEKETGqeFAVKIIDITGEKSSENEAEELREatrrEIEILRQVSgHPNIIELHDVFESP------T 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT-L 436
Cdd:cd14093    83 FIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLN--IVHRDLKPENILLDD-NLNVKISDFGFATrL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPE-----MYEEM--YDESVDVYAFGMCLLEMVTGEYPY---SECMnpatIYRKVISG----VK 502
Cdd:cd14093   160 DEGEKLRELCGTPGYLAPEvlkcsMYDNApgYGKEVDMWACGVIMYTLLAGCPPFwhrKQMV----MLRNIMEGkyefGS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 392899979  503 PEcFSRIPAqypEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14093   236 PE-WDDISD---TAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
287-522 2.27e-26

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: 110.18  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGL--DTETGVAVAWCELQESkLNKTErQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTE 364
Cdd:cd14061     2 IGVGGFGKVYRGIwrGEEVAVKAARQDPDED-ISVTL-ENVRQEARLFWMLRHPNIIAL------RGVCLQPPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNP-PVIHRDLKCDNIFITGTTGS-------VKIGDLGLATL 436
Cdd:cd14061    74 YARGGALNRVLAG-RKIPPHVLVDWAIQIARGMNYLHNEAPvPIIHRDLKSSNILILEAIENedlenktLKITDFGLARE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYR---------------KVISG 500
Cdd:cd14061   153 WHKTTRMSAAGTYAWMAPEVIKsSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGvavnkltlpipstcpEPFAQ 232
                         250       260
                  ....*....|....*....|..
gi 392899979  501 VKPECFSRIPAQYPEIREIIDR 522
Cdd:cd14061   233 LMKDCWQPDPHDRPSFADILKQ 254
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
281-545 2.80e-26

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: 110.59  E-value: 2.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESkLNKTERQRfreeaeMLKDLQ-------HPNIVRFY-------DY 346
Cdd:cd06617     3 LEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRAT-VNSQEQKR------LLMDLDismrsvdCPYTVTFYgalfregDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  347 WesadLCgkrkyivlvTELMTSGTLKMYLKRFK---RINIKVLKSWCRQILKGLSFLHTrNPPVIHRDLKCDNIFITgTT 423
Cdd:cd06617    76 W----IC---------MEVMDTSLDKFYKKVYDkglTIPEDILGKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLIN-RN 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  424 GSVKIGDLGLATLKNKSFAKSV-IGTPEFMAPE-----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKV 497
Cdd:cd06617   141 GQVKLCDFGISGYLVDSVAKTIdAGCKPYMAPErinpeLNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQV 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  498 ISGVKP----ECFSripaqyPEIREIIDRCIRVRREERSTVKQLLVDDFFTP 545
Cdd:cd06617   221 VEEPSPqlpaEKFS------PEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
288-481 3.13e-26

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: 110.67  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRfreEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELMt 367
Cdd:cd14137    13 GSGSFGVVYQAKLLETGEVVA---IKKVLQDKRYKNR---ELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYLNLVMEYM- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  368 SGTL----KMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT-LKNKSFA 442
Cdd:cd14137    86 PETLyrviRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLG--ICHRDIKPQNLLVDPETGVLKLCDFGSAKrLVPGEPN 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392899979  443 KSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd14137   164 VSYICSRYYRAPELIfgATDYTTAIDIWSAGCVLAELLLGQ 204
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
285-543 3.24e-26

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: 110.97  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKlnKTERQRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLvtE 364
Cdd:cd06655    25 EKIGQGASGTVFTAIDVATGQEVAIKQINLQK--QPKKELIINEILVMKELKNPNIVNFLDSF----LVGDELFVVM--E 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd06655    97 YLAGGSLTDVVTE-TCMDEAQIAAVCRECLQALEFLHANQ--VIHRDIKSDNVLL-GMDGSVKLTDFGFCAqiTPEQSKR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPEcFSRIPAQYPEIREIID 521
Cdd:cd06655   173 STMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPE-LQNPEKLSPIFRDFLN 250
                         250       260
                  ....*....|....*....|..
gi 392899979  522 RCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06655   251 RCLEMDVEKRGSAKELLQHPFL 272
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
285-481 5.26e-26

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: 109.96  E-value: 5.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLnKTERQRF----REEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIV 360
Cdd:cd07840     5 AQIGEGTYGQVYKARNKKTGELVA---LKKIRM-ENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGSIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMT---SGTLKMYLKRFKRINIKvlkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATLK 437
Cdd:cd07840    81 MVFEYMDhdlTGLLDNPEVKFTESQIK---CYMKQLLEGLQYLHSNG--ILHRDIKGSNILINN-DGVLKLADFGLARPY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKS----VIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07840   155 TKENNADytnrVI-TLWYRPPEllLGATRYGPEVDMWSVGCILAELFTGK 203
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
280-521 5.76e-26

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: 108.96  E-value: 5.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLN-KTERQRFREEAEMLKdLQHPNIVRFYDYWESAdlcgKRKY 358
Cdd:cd14075     3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDqKTQRLLSREISSMEK-LHHPNIIRLYEVVETL----SKLH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 ivLVTELMTSGTLKMYLK---RFKRINIKVLKSwcrQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT 435
Cdd:cd14075    78 --LVMEYASGGELYTKIStegKLSESEAKPLFA---QIVSAVKHMHENN--IIHRDLKAENVFYA-SNNCVKVGDFGFST 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 -LKNKSFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISG-------VKPEC 505
Cdd:cd14075   150 hAKRGETLNTFCGSPPYAAPELFkdEHYIGIYVDIWALGVLLYFMVTGVMPF-RAETVAKLKKCILEGtytipsyVSEPC 228
                         250       260
                  ....*....|....*....|...
gi 392899979  506 FSRI-------PAQYPEIREIID 521
Cdd:cd14075   229 QELIrgilqpvPSDRYSIDEIKN 251
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
277-533 6.41e-26

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: 109.01  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKFDEELGRGSFKTVFRGldTETGVAVAWCELQESKLNKTERQRFREEAEMLKdLQHPNIVRFYDYwESAdlCGKR 356
Cdd:cd13979     1 DWEPLRLQEPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLAA-ETG--TDFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMTSGTL--KMY-----LKRFKRINIkvlkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIG 429
Cdd:cd13979    75 SLGLIIMEYCGNGTLqqLIYegsepLPLAHRILI------SLDIARALRFCHSHG--IVHLDVKPANILISEQ-GVCKLC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLATLKNK-----SFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKP 503
Cdd:cd13979   146 DFGCSVKLGEgnevgTPRSHIGGTYTYRAPELLKgERVTPKADIYSFGITLWQMLTRELPYAG-LRQHVLYAVVAKDLRP 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  504 eCFSRIPAQYP--EIREIIDRCIRVRREERST 533
Cdd:cd13979   225 -DLSGLEDSEFgqRLRSLISRCWSAQPAERPN 255
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
287-455 8.74e-26

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: 108.08  E-value: 8.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKlnKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELM 366
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK--AKDREDVRNEIEIMNQLRHPRLLQLYDAFET------PREMVLVMEYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLkmylkrFKRI-------NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLA-TLK 437
Cdd:cd14103    73 AGGEL------FERVvdddfelTERDCILFMRQICEGVQYMHKQG--ILHLDLKPENILCVSRTGNqIKIIDFGLArKYD 144
                         170
                  ....*....|....*...
gi 392899979  438 NKSFAKSVIGTPEFMAPE 455
Cdd:cd14103   145 PDKKLKVLFGTPEFVAPE 162
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
287-542 1.03e-25

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: 108.63  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ---ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLVT 363
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDR----AEKTLTIFM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLG----LATL-KN 438
Cdd:cd06651    91 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGaskrLQTIcMS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPEcfsrIPAQYPEIR 517
Cdd:cd06651   168 GTGIRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQ----LPSHISEHA 243
                         250       260
                  ....*....|....*....|....*
gi 392899979  518 EIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06651   244 RDFLGCIFVEARHRPSAEELLRHPF 268
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
287-486 1.43e-25

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: 107.35  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeSKLNK---TERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVT 363
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFA------AKFIPkrdKKKEAVLREISILNQLQHPRIIQLHEAYES------PTELVLIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI-TGTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd14006    69 ELCSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHH--ILHLDLKPENILLaDRPSPQIKIIDFGLARKLNPGEE 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392899979  443 KSVI-GTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14006   147 LKEIfGTPEFVAPEIVNgEPVSLATDMWSIGVLTYVLLSGLSPFLG 192
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
284-486 1.45e-25

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: 107.88  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVT 363
Cdd:cd14082     8 DEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPE------RVFVVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG--SVKIGDLGLA-TLKNK 439
Cdd:cd14082    82 EKLHGDMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKN--IVHCDLKPENVLLASAEPfpQVKLCDFGFArIIGEK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  440 SFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14082   160 SFRRSVVGTPAYLAPEVLRnKGYNRSLDMWSVGVIIYVSLSGTFPFNE 207
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
287-517 1.47e-25

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: 108.20  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLVTELM 366
Cdd:cd14146     2 IGVGGFGKVYRATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEG------VCLEEPNLCLVMEFA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYL---------KRFKRINIKVLKSWCRQILKGLSFLHTRN-PPVIHRDLKCDNIFITGT-------TGSVKIG 429
Cdd:cd14146    76 RGGTLNRALaaanaapgpRRARRIPPHILVNWAVQIARGMLYLHEEAvVPILHRDLKSSNILLLEKiehddicNKTLKIT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLATLKNKSFAKSVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVK------ 502
Cdd:cd14146   156 DFGLAREWHRTTKMSAAGTYAWMAPEVIKSsLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTlpipst 235
                         250       260
                  ....*....|....*....|
gi 392899979  503 -PECFSRIPA----QYPEIR 517
Cdd:cd14146   236 cPEPFAKLMKecweQDPHIR 255
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
287-538 1.65e-25

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: 108.03  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNK--TERQrFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKegVEHQ-LRREIEIQSHLRHPNILRLYNYFHD------RKRIYLILE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKNKSFAKS 444
Cdd:cd14117    87 YAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKK--VIHRDIKPENLLM-GYKGELKIADFGWSVHAPSLRRRT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATiYRKVisgVKPECfsRIPAQYPE-IREIIDR 522
Cdd:cd14117   164 MCGTLDYLPPEMIEgRTHDEKVDLWCIGVLCYELLVGMPPFESASHTET-YRRI---VKVDL--KFPPFLSDgSRDLISK 237
                         250
                  ....*....|....*.
gi 392899979  523 CIRVRREERSTVKQLL 538
Cdd:cd14117   238 LLRYHPSERLPLKGVM 253
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
281-534 1.71e-25

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: 108.58  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFY-DYWESADLCgkrky 358
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYaSFIEDNELN----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 ivLVTELMTSGTLKMYLKRFKR----INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA 434
Cdd:cd08229   101 --IVLELADAGDLSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRR--VMHRDIKPANVFITA-TGVVKLGDLGLG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TL--KNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYP-YSECMNPATIYRKVisgvkPEC-FSRI 509
Cdd:cd08229   176 RFfsSKTTAAHSLVGTPYYMSPErIHENGYNFKSDIWSLGCLLYEMAALQSPfYGDKMNLYSLCKKI-----EQCdYPPL 250
                         250       260
                  ....*....|....*....|....*..
gi 392899979  510 PAQY--PEIREIIDRCIRVRREERSTV 534
Cdd:cd08229   251 PSDHysEELRQLVNMCINPDPEKRPDI 277
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
286-538 1.92e-25

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: 107.81  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQR-FREEAEMLKDL-QHPNIVRFYDYWESADlcGKRKYIVLVT 363
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYA---LKRMYFNDEEQLRvAIKEIEIMKRLcGHPNIVQYYDSAILSS--EGRKEVLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELmTSGTL-----KMYLKRFKRIniKVLKSWCrQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd13985    82 EY-CPGSLvdileKSPPSPLSEE--EVLRIFY-QICQAVGHLHSQSPPIIHRDIKIENILFS-NTGRFKLCDFGSATTEH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSF--------AKSVIG---TPEFMAPEMYE----EMYDESVDVYAFGMCLLEMVTGEYPYSEcmnpATIYRkvISGVKp 503
Cdd:cd13985   157 YPLeraeevniIEEEIQkntTPMYRAPEMIDlyskKPIGEKADIWALGCLLYKLCFFKLPFDE----SSKLA--IVAGK- 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  504 ecfSRIPAQ---YPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd13985   230 ---YSIPEQprySPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
287-537 2.30e-25

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: 107.70  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAW-------CELQESKLNKTERQR----------FREEAEMLKDLQHPNIVrfydywes 349
Cdd:cd14000     2 LGDGGFGSVYRASYKGEPVAVKIfnkhtssNFANVPADTMLRHLRatdamknfrlLRQELTVLSHLHHPSIV-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  350 ADLCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKV----LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI----TG 421
Cdd:cd14000    74 YLLGIGIHPLMLVLELAPLGSLDHLLQQDSRSFASLgrtlQQRIALQVADGLRYLHSAM--IIYRDLKSHNVLVwtlyPN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  422 TTGSVKIGDLGLATLKNKSFAKSVIGTPEFMAPEM--YEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNpATIYRKVIS 499
Cdd:cd14000   152 SAIIIKIADYGISRQCCRMGAKGSEGTPGFRAPEIarGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLK-FPNEFDIHG 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  500 GVKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd14000   231 GLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
274-543 2.30e-25

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: 108.27  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  274 KSKNGRFlkfdEELGRGSFKTVFRGLDTETG--VAVAWCELQEsklnKTERQRFREEAEMLKDLQHPNIVRFYDYWesad 351
Cdd:cd06654    19 KKKYTRF----EKIGQGASGTVYTAMDVATGqeVAIRQMNLQQ----QPKKELIINEILVMRENKNPNIVNYLDSY---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  352 LCGKRKYIVLvtELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDL 431
Cdd:cd06654    87 LVGDELWVVM--EYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLAT--LKNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECfsr 508
Cdd:cd06654   161 GFCAqiTPEQSKRSTMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPEL--- 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  509 ipaQYPE-----IREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06654   237 ---QNPEklsaiFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
287-543 2.96e-25

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: 107.01  E-value: 2.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTV--FRGLDTETGVAVAWCELQESKLNKTERQ---RFREEAEMLKDLQHPNIVRFYDYweSADLCGKrkyIVL 361
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKDyvkRLTSEYIISSKLHHPNIVKVLDL--CQDLHGK---WCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL----- 436
Cdd:cd13994    76 VMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHG--IAHRDLKPENILLDE-DGVLKLTDFGTAEVfgmpa 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTPEFMAPEMYEEM-YD-ESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAqy 513
Cdd:cd13994   153 eKESPMSAGLCGSEPYMAPEVFTSGsYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPI-- 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  514 peIREIIDRCIRVRR-------EERSTVKQLLVDDFF 543
Cdd:cd13994   231 --ENLLPSECRRLIYrmlhpdpEKRITIDEALNDPWV 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
287-522 3.27e-25

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: 106.74  E-value: 3.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQE---SKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVT 363
Cdd:cd08222     8 LGSGNFGTVYLVSDLKATADEELKVLKEisvGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKE------SFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTL----KMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItgTTGSVKIGDLGLATLKNK 439
Cdd:cd08222    82 EYCEGGDLddkiSEYKKSGTTIDENQILDWFIQLLLAVQYMHERR--ILHRDLKAKNIFL--KNNVIKVGDFGISRILMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 S--FAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVKPEcfsrIPAQYP-E 515
Cdd:cd08222   158 TsdLATTFTGTPYYMSPEVLKhEGYNSKSDIWSLGCILYEMCCLKHAF-DGQNLLSVMYKIVEGETPS----LPDKYSkE 232

                  ....*..
gi 392899979  516 IREIIDR 522
Cdd:cd08222   233 LNAIYSR 239
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
287-550 3.71e-25

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: 106.93  E-value: 3.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR-FREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTEL 365
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKD------KKYLYMLMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLA-TLKNKSFAKS 444
Cdd:cd05572    75 CLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRG--IIYRDLKPENLLL-DSNGYVKLVDFGFAkKLGSGRKTWT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEC-MNPATIYRKVISGVKpecfsriPAQYPEIreiidr 522
Cdd:cd05572   152 FCGTPEYVAPEIILNKgYDFSVDYWSLGILLYELLTGRPPFGGDdEDPMKIYNIILKGID-------KIEFPKY------ 218
                         250       260
                  ....*....|....*....|....*...
gi 392899979  523 cirVRREERSTVKQLLVDdffTPEDLIG 550
Cdd:cd05572   219 ---IDKNAKNLIKQLLRR---NPEERLG 240
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
285-538 4.50e-25

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: 106.67  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLK-DLQHPNIVRFYDYWESadlcgkRKYIVLVT 363
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLElCKDCPRVVNLHEVYET------RSELILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGLA-TLKNKS 440
Cdd:cd14106    88 ELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERN--IVHLDLKPQNILLTSEFplGDIKLCDFGISrVIGEGE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEM--YEEMyDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRkvISGVK----PECFSRIPaqyP 514
Cdd:cd14106   166 EIREILGTPDYVAPEIlsYEPI-SLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLN--ISQCNldfpEELFKDVS---P 239
                         250       260
                  ....*....|....*....|....
gi 392899979  515 EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14106   240 LAIDFIKRLLVKDPEKRLTAKECL 263
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
281-538 4.98e-25

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: 106.67  E-value: 4.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRF------REEAEMLKDLQHPNIVRFYDYWESADlcg 354
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFqklpqlREIDLHRRVSRHPNIITLHDVFETEV--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 krkYIVLVTELMTSGTLKMYL--KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLG 432
Cdd:cd13993    79 ---AIYIVLEYCPNGDLFEAIteNRIYVGKTELIKNVFLQLIDAVKHCHSLG--IYHRDIKPENILLSQDEGTVKLCDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATLKNKSFAKSViGTPEFMAPEMYEEMYDE-------SVDVYAFGMCLLEMVTGEYPYSECmNPATIYRKVISGVKPEC 505
Cdd:cd13993   154 LATTEKISMDFGV-GSEFYMAPECFDEVGRSlkgypcaAGDIWSLGIILLNLTFGRNPWKIA-SESDPIFYDYYLNSPNL 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  506 FSRIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd13993   232 FDVILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
274-543 5.40e-25

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: 107.50  E-value: 5.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  274 KSKNGRFlkfdEELGRGSFKTVFRGLDTETG--VAVAWCELQEsklnKTERQRFREEAEMLKDLQHPNIVRFYDYWesad 351
Cdd:cd06656    18 KKKYTRF----EKIGQGASGTVYTAIDIATGqeVAIKQMNLQQ----QPKKELIINEILVMRENKNPNIVNYLDSY---- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  352 LCGKRKYIVLvtELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDL 431
Cdd:cd06656    86 LVGDELWVVM--EYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLAT--LKNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECfsr 508
Cdd:cd06656   160 GFCAqiTPEQSKRSTMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPEL--- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  509 ipaQYPE-----IREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06656   236 ---QNPErlsavFRDFLNRCLEMDVDRRGSAKELLQHPFL 272
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
279-475 6.35e-25

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: 106.89  E-value: 6.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKfDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQR-------FREeAEMLKDLQHPNIVRFYDYWesad 351
Cdd:cd07841     1 RYEK-GKKLGEGTYAVVYKARDKETGRIVA---IKKIKLGERKEAKdginftaLRE-IKLLQELKHPNIIGLLDVF---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  352 lcGKRKYIVLVTELMtSGTLKMYLKRfKRINIKV--LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIG 429
Cdd:cd07841    72 --GHKSNINLVFEFM-ETDLEKVIKD-KSIVLTPadIKSYMLMTLRGLEYLHSNW--ILHRDLKPNNLLIA-SDGVLKLA 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  430 DLGLAtlknKSFAKS-------VIgTPEFMAPEMY--EEMYDESVDVYAFGmCLL 475
Cdd:cd07841   145 DFGLA----RSFGSPnrkmthqVV-TRWYRAPELLfgARHYGVGVDMWSVG-CIF 193
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
285-540 7.35e-25

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-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. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-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: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 106.30  E-value: 7.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGlDTETGVAVAWceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadlcGKRKYIVLVTE 364
Cdd:cd14151    14 QRIGSGSFGTVYKG-KWHGDVAVKM--LNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY-------STKPQLAIVTQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA- 442
Cdd:cd14151    84 WCEGSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLH-EDLTVKIGDFGLATVKSRWSGs 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 ---KSVIGTPEFMAPEMY----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQYPE 515
Cdd:cd14151   161 hqfEQLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPK 240
                         250       260
                  ....*....|....*....|....*.
gi 392899979  516 -IREIIDRCIRVRREERSTVKQLLVD 540
Cdd:cd14151   241 aMKRLMAECLKKKRDERPLFPQILAS 266
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
287-478 8.05e-25

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: 105.65  E-value: 8.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG-VAVawceLQESKlNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLVTEL 365
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGkVMV----MKELK-RFDEQRSFLKEVKLMRRLSHPNILRFIG------VCVKDNKLNFITEY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG--SVKIGDLGLATLKNKSFA 442
Cdd:cd14065    70 VNGGTLEELLKSMDeQLPWSQRVSLAKDIASGMAYLHSKN--IIHRDLNSKNCLVREANRgrNAVVADFGLAREMPDEKT 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  443 K--------SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMV 478
Cdd:cd14065   148 KkpdrkkrlTVVGSPYWMAPEMLRgESYDEKVDVFSFGIVLCEII 192
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
287-533 8.30e-25

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: 106.50  E-value: 8.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTetgvaVAWCELQESKL----NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRK----- 357
Cdd:cd14048    14 LGRGGFGVVFEAKNK-----VDDCNYAVKRIrlpnNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPEGWQEkmdev 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYLKRFKRINIK---VLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA 434
Cdd:cd14048    89 YLYIQMQLCRKENLKDWMNRRCTMESRelfVCLNIFKQIASAVEYLHSKG--LIHRDLKPSNVFFS-LDDVVKVGDFGLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLKNK------------SFAKSV--IGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVtgeYPYSECMNPATIYRKVIS 499
Cdd:cd14048   166 TAMDQgepeqtvltpmpAYAKHTgqVGTRLYMSPEqIHGNQYSEKVDIFALGLILFELI---YSFSTQMERIRTLTDVRK 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  500 GVKPECFSRipaQYPEIREIIDRCIRVRREERST 533
Cdd:cd14048   243 LKFPALFTN---KYPEERDMVQQMLSPSPSERPE 273
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
281-522 1.16e-24

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: 105.51  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIV 360
Cdd:cd14145     8 LVLEEIIGIGGFGKVYRAIWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIAL------RGVCLKEPNLC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRN-PPVIHRDLKCDNIFITG-------TTGSVKIGDLG 432
Cdd:cd14145    82 LVMEFARGGPLNRVLSG-KRIPPDILVNWAVQIARGMNYLHCEAiVPVIHRDLKSSNILILEkvengdlSNKILKITDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYP----------YSECMNPATIyrkVISGV 501
Cdd:cd14145   161 LAREWHRTTKMSAAGTYAWMAPEVIRsSMFSKGSDVWSYGVLLWELLTGEVPfrgidglavaYGVAMNKLSL---PIPST 237
                         250       260
                  ....*....|....*....|....*....
gi 392899979  502 KPECFSRI--------PAQYPEIREIIDR 522
Cdd:cd14145   238 CPEPFARLmedcwnpdPHSRPPFTNILDQ 266
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
314-538 1.17e-24

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: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  314 ESKLNKterqRFREEAEMLKDLQHPNIVRFYDYW-ESADLcgkrkYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQ 392
Cdd:cd14046    44 ESKNNS----RILREVMLLSRLNHQHVVRYYQAWiERANL-----YIQM--EYCEKSTLRDLIDSGLFQDTDRLWRLFRQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  393 ILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT-----------LKNKSFAK---------SVIGTPEFM 452
Cdd:cd14046   113 ILEGLAYIHSQG--IIHRDLKPVNIFLDS-NGNVKIGDFGLATsnklnvelatqDINKSTSAalgssgdltGNVGTALYV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  453 APEM---YEEMYDESVDVYAFGMCLLEMVtgeYPYSECMNPATIYRKV--ISGVKPECFSRipAQYPEIREIIDRCIRVR 527
Cdd:cd14046   190 APEVqsgTKSTYNEKVDMYSLGIIFFEMC---YPFSTGMERVQILTALrsVSIEFPPDFDD--NKHSKQAKLIRWLLNHD 264
                         250
                  ....*....|.
gi 392899979  528 REERSTVKQLL 538
Cdd:cd14046   265 PAKRPSAQELL 275
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
279-537 1.18e-24

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: 105.93  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRG----LDTETGVAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRfYDYWESADlcg 354
Cdd:cd05038     4 RHLKFIKQLGEGHFGSVELCrydpLGDNTGEQVAVKSLQPSG-EEQHMSDFKREIEILRTLDHEYIVK-YKGVCESP--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL 433
Cdd:cd05038    79 GRRSLRLIMEYLPSGSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLGSQR--YIHRDLAARNILVE-SEDLVKISDFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 ATLKNKS----FAKSVIGTPEF-MAPEMYEE--MYDESvDVYAFGMCLLEMVTgeYPYSECMNPATIYRKVISGVKPECF 506
Cdd:cd05038   156 AKVLPEDkeyyYVKEPGESPIFwYAPECLREsrFSSAS-DVWSFGVTLYELFT--YGDPSQSPPALFLRMIGIAQGQMIV 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 392899979  507 SRI------------PAQYP-EIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05038   233 TRLlellksgerlprPPSCPdEVYDLMKECWEYEPQDRPSFSDL 276
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
280-484 1.30e-24

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: 105.42  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAE----MLKDLQHPNIVRFYDYWESadlcgk 355
Cdd:cd14196     6 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIErevsILRQVLHPNIITLHDVYEN------ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS---VKIGDLG 432
Cdd:cd14196    80 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDKNIPiphIKLIDFG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  433 LA-TLKNKSFAKSVIGTPEFMAPEM--YEEMYDESvDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14196   158 LAhEIEDGVEFKNIFGTPEFVAPEIvnYEPLGLEA-DMWSIGVITYILLSGASPF 211
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
281-538 1.45e-24

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: 105.12  E-value: 1.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLdTETGVAVAwcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYIV 360
Cdd:cd14063     2 LEIKEVIGKGRFGRVHRGR-WHGDVAIK--LLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGA------CMDPPHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLK-RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGttGSVKIGDLGLATLKNK 439
Cdd:cd14063    73 IVTSLCKGRTLYSLIHeRKEKFDFNKTVQIAQQICQGMGYLHAKG--IIHKDLKSKNIFLEN--GRVVITDFGLFSLSGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGT---PE----FMAPEMYEEM-----------YDESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVISGV 501
Cdd:cd14063   149 LQPGRREDTlviPNgwlcYLAPEIIRALspdldfeeslpFTKASDVYAFGTVWYELLAGRWPFK-EQPAESIIWQVGCGK 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  502 KPEcFSRIpaQYP-EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14063   228 KQS-LSQL--DIGrEVKDILMQCWAYDPEKRPTFSDLL 262
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
281-543 1.75e-24

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: 105.60  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREeAEMLKDLQHPNIVRFYD--YWESADlcgkrky 358
Cdd:cd06620     7 LETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRE-LQILHECHSPYIVSFYGafLNENNN------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITGTtGSVKIGDLGLATLKN 438
Cdd:cd06620    79 IIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHR-IIHRDIKPSNILVNSK-GQIKLCDFGVSGELI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSE-------CMNPATIYrKVISGVKPECFSRIP 510
Cdd:cd06620   157 NSIADTFVGTSTYMSPERIQgGKYSVKSDVWSLGLSIIELALGEFPFAGsnddddgYNGPMGIL-DLLQRIVNEPPPRLP 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  511 AQ--YPEI-REIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06620   236 KDriFPKDlRDFVDRCLLKDPRERPSPQLLLDHDPF 271
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
281-543 1.82e-24

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: 105.52  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQeSKLNKTERQRFREEAEMLKDLQH-PNIVRFY-------DYWesadL 352
Cdd:cd06616     8 LKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIR-STVDEKEQKRLLMDLDVVMRSSDcPYIVKFYgalfregDCW----I 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CgkrkyivlvTELMTSGTLKMY----LKRFKRINIKVLKSWCRQILKGLSFLHTrNPPVIHRDLKCDNIFITGtTGSVKI 428
Cdd:cd06616    83 C---------MELMDISLDKFYkyvyEVLDSVIPEEILGKIAVATVKALNYLKE-ELKIIHRDVKPSNILLDR-NGNIKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLATLKNKSFAKSV-IGTPEFMAPE-----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVK 502
Cdd:cd06616   152 CDFGISGQLVDSIAKTRdAGCRPYMAPEridpsASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGDP 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392899979  503 PECFSRIPAQY-PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06616   232 PILSNSEEREFsPSFVNFVNLCLIKDESKRPKYKELLKHPFI 273
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
279-497 1.85e-24

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: 105.48  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTV----FRGLDTETGVAVAWCELQESKlnkTERQR-FREEAEMLKDLQHPNIVRFYDYWESADlc 353
Cdd:cd14205     4 RHLKFLQQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHST---EEHLRdFEREIEILKSLQHDNIVKYKGVCYSAG-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gkRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG 432
Cdd:cd14205    79 --RRNLRLIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKR--YIHRDLATRNILVE-NENRVKIGDFG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  433 LATL--KNKSF--AKSVIGTPEF-MAPE-MYEEMYDESVDVYAFGMCLLEMVTgeYPYSECMNPATIYRKV 497
Cdd:cd14205   154 LTKVlpQDKEYykVKEPGESPIFwYAPEsLTESKFSVASDVWSFGVVLYELFT--YIEKSKSPPAEFMRMI 222
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
285-485 2.07e-24

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: 104.68  E-value: 2.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTET--GVAVAwcelqesKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLV 362
Cdd:cd14010     6 DEIGRGKHSVVYKGRRKGTieFVAIK-------CVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYET------SNHLWLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL------ 436
Cdd:cd14010    73 VEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKG--IIYCDLKPSNILLDG-NGTLKLSDFGLARRegeilk 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  437 ------------KNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGmCLL-EMVTGEYPYS 485
Cdd:cd14010   150 elfgqfsdegnvNKVSKKQAKRGTPYYMAPELFqGGVHSFASDLWALG-CVLyEMFTGKPPFV 211
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
285-533 2.10e-24

Catalytic domain 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. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. 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. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-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: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 104.29  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL-DTETGVAVAwcELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLVT 363
Cdd:cd05034     1 KKLGAGQFGEVWMGVwNGTTKVAVK--TLKPGTMSPEA---FLQEAQIMKKLRHDKLVQLY------AVCSDEEPIYIVT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL--KNK 439
Cdd:cd05034    70 ELMSKGSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRN--YIHRDLAARNILV-GENNVCKVADFGLARLieDDE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYsECMNPATIYRKVISGVKPECfsriPAQYP- 514
Cdd:cd05034   147 YTAREGAKFPiKWTAPEaaLYGRFTIKS-DVWSFGILLYEIVTyGRVPY-PGMTNREVLEQVERGYRMPK----PPGCPd 220
                         250
                  ....*....|....*....
gi 392899979  515 EIREIIDRCIRVRREERST 533
Cdd:cd05034   221 ELYDIMLQCWKKEPEERPT 239
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
287-540 2.32e-24

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: 104.41  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTE-RQRFREEAEMLKDLQHPNIVRFYDYWESadlcgKRKyIVLVTEL 365
Cdd:cd14663     8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGmVEQIKREIAIMKLLRHPNIVELHEVMAT-----KTK-IFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK----SF 441
Cdd:cd14663    82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRG--VFHRDLKPENLLLD-EDGNLKISDFGLSALSEQfrqdGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPEFMAPEMYEEM-YD-ESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKvISGVKPECFSRIPaqyPEIREI 519
Cdd:cd14663   159 LHTTCGTPNYVAPEVLARRgYDgAKADIWSCGVILFVLLAGYLPFDD-ENLMALYRK-IMKGEFEYPRWFS---PGAKSL 233
                         250       260
                  ....*....|....*....|.
gi 392899979  520 IDRCIRVRREERSTVKQLLVD 540
Cdd:cd14663   234 IKRILDPNPSTRITVEQIMAS 254
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
287-543 2.46e-24

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: 104.26  E-value: 2.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTE--RQRFREEAEMLKDLQHPNIVRFYDYWESADlcgKRK-YIVLvt 363
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPngEANVKREIQILRRLNHRNVIKLVDVLYNEE---KQKlYMVM-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKR-FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKsFA 442
Cdd:cd14119    76 EYCVGGLQEMLDSApDKRLPIWQAHGYFVQLIDGLEYLHSQG--IIHKDIKPGNLLLT-TDGTLKISDFGVAEALDL-FA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KS-----VIGTPEFMAPEMY--EEMYDE-SVDVYAFGMCLLEMVTGEYPYsECMNpatIYR--KVISgvkpECFSRIPAQ 512
Cdd:cd14119   152 EDdtcttSQGSPAFQPPEIAngQDSFSGfKVDIWSAGVTLYNMTTGKYPF-EGDN---IYKlfENIG----KGEYTIPDD 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  513 Y-PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14119   224 VdPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
287-538 2.64e-24

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: 104.29  E-value: 2.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKtvfRGLDTETGVAVAWCELQESKLNKTER--QRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd08219     8 VGEGSFG---RALLVQHVNSDQKYAMKEIRLPKSSSavEDSRKEAVLLAKMKHPNIVAFKESFEA------DGHLYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTL--KMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK--S 440
Cdd:cd08219    79 YCDGGDLmqKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKR--VLHRDIKSKNIFLT-QNGKVKLGDFGSARLLTSpgA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSecmnpATIYRKVISGVKPECFSRIPAQYP-EIRE 518
Cdd:cd08219   156 YACTYVGTPYYVPPEIWENMpYNNKSDIWSLGCILYELCTLKHPFQ-----ANSWKNLILKVCQGSYKPLPSHYSyELRS 230
                         250       260
                  ....*....|....*....|
gi 392899979  519 IIDRCIRVRREERSTVKQLL 538
Cdd:cd08219   231 LIKQMFKRNPRSRPSATTIL 250
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
272-538 2.80e-24

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: 104.07  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  272 IDKSKngrfLKFDEELGRGSFKTVFRGlDTETGVAVAWCELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYdywesaD 351
Cdd:cd05059     1 IDPSE----LTFLKELGSGQFGVVHLG-KWRGKIDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLY------G 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  352 LCGKRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGD 430
Cdd:cd05059    67 VCTKQRPIFIVTEYMANGCLLNYLRERRgKFQTEQLLEMCKDVCEAMEYLESNG--FIHRDLAARNCLV-GEQNVVKVSD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLATLKNKSFAKSVIGTP---EFMAPEMYE-EMYDESVDVYAFGMCLLEMVT-GEYPYSECMNPATIYRkVISGV---K 502
Cdd:cd05059   144 FGLARYVLDDEYTSSVGTKfpvKWSPPEVFMySKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEH-ISQGYrlyR 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  503 PECFSripaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05059   223 PHLAP------TEVYTIMYSCWHEKPEERPTFKILL 252
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
286-544 2.93e-24

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: 104.07  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDywesadlCGKRKYIV-LVT 363
Cdd:cd06607     8 EIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKG-------CYLREHTAwLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELM---TSGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKnkS 440
Cdd:cd06607    81 EYClgsASDIVEVHKKPLQEVEIAAI---CHGALQGLAYLHSHN--RIHRDVKAGNILLT-EPGTVKLADFGSASLV--C 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPE----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNP-ATIYRkvISGVKPECFSRIPAQyPE 515
Cdd:cd06607   153 PANSFVGTPYWMAPEvilaMDEGQYDGKVDVWSLGITCIELAERKPPLFN-MNAmSALYH--IAQNDSPTLSSGEWS-DD 228
                         250       260
                  ....*....|....*....|....*....
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06607   229 FRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
287-543 3.28e-24

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: 103.88  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLvtELM 366
Cdd:cd08225     8 IGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENG----RLFIVM--EYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLkmylkrFKRINIK--VLKS------WCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN 438
Cdd:cd08225    82 DGGDL------MKRINRQrgVLFSedqilsWFVQISLGLKHIHDRK--ILHRDIKSQNIFLSKNGMVAKLGDFGIARQLN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KS--FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISG----VKPEcFSRipa 511
Cdd:cd08225   154 DSmeLAYTCVGTPYYLSPEICQNRpYNNKTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKICQGyfapISPN-FSR--- 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  512 qypEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd08225   229 ---DLRSLISQLFKVSPRDRPSITSILKRPFL 257
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
303-484 3.78e-24

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: 104.43  E-value: 3.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  303 TGVAVAWCELQESKL---NKT---------ERQRFREeAEMLKDLQHPNIVRFYdyweSADLCGKRKYIVLVTELMTSGT 370
Cdd:cd06621    13 AGGSVTKCRLRNTKTifaLKTittdpnpdvQKQILRE-LEINKSCASPYIVKYY----GAFLDEQDSSIGIAMEYCEGGS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  371 LKMYLKRFK----RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKSVI 446
Cdd:cd06621    88 LDSIYKKVKkkggRIGEKVLGKIAESVLKGLSYLHSRK--IIHRDIKPSNILLT-RKGQVKLCDFGVSGELVNSLAGTFT 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392899979  447 GTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd06621   165 GTSYYMAPERIQgGPYSITSDVWSLGLTLLEVAQNRFPF 203
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
287-538 3.93e-24

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: 103.66  E-value: 3.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSF--KTVFRglDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLvtE 364
Cdd:cd08221     8 LGRGAFgeAVLYR--KTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHF----LDGESLFIEM--E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTL--KMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK--S 440
Cdd:cd08221    80 YCNGGNLhdKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAG--ILHRDIKTLNIFLT-KADLVKLGDFGISKVLDSesS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVKPEcfsrIPAQYPE-IRE 518
Cdd:cd08221   157 MAESIVGTPYYMSPELVQgVKYNFKSDIWAVGCVLYELLTLKRTF-DATNPLRLAVKIVQGEYED----IDEQYSEeIIQ 231
                         250       260
                  ....*....|....*....|
gi 392899979  519 IIDRCIRVRREERSTVKQLL 538
Cdd:cd08221   232 LVHDCLHQDPEDRPTAEELL 251
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
261-538 3.95e-24

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: 104.50  E-value: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  261 VEDDFDaqEKPIdkSKNGRflkfdeELGRGSFKTVFRGLDTETGVAVawcelqeSKLNKT-------ERQRFREEAEMLK 333
Cdd:cd14158     7 MTNNFD--ERPI--SVGGN------KLGEGGFGVVFKGYINDKNVAV-------KKLAAMvdistedLTKQFEQEIQVMA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  334 DLQHPNIVRFYDYWESAD-LCgkrkyivLVTELMTSGTLkmyLKRFKRINIKVLKSWCRQI------LKGLSFLHTRNpp 406
Cdd:cd14158    70 KCQHENLVELLGYSCDGPqLC-------LVYTYMPNGSL---LDRLACLNDTPPLSWHMRCkiaqgtANGINYLHENN-- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  407 VIHRDLKCDNIFITGTTgSVKIGDLGLATlKNKSFAKS-----VIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd14158   138 HIHRDIKSANILLDETF-VPKISDFGLAR-ASEKFSQTimterIVGTTAYMAPEALRGEITPKSDIFSFGVVLLEIITGL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  482 YPYSECMNPA--------------TIY----RKVISGVKPEcfsrIPAQYpeirEIIDRCIRVRREERSTVKQLL 538
Cdd:cd14158   216 PPVDENRDPQllldikeeiedeekTIEdyvdKKMGDWDSTS----IEAMY----SVASQCLNDKKNRRPDIAKVQ 282
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
285-542 4.32e-24

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: 104.32  E-value: 4.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELqeSKLNKTERQrFREEAEMLKDLQ-HPNIVRFYD-YWESADLCGKRKYIVLv 362
Cdd:cd06638    24 ETIGKGTYGKVFKVLNKKNGSKAAVKIL--DPIHDIDEE-IEAEYNILKALSdHPNVVKFYGmYYKKDVKNGDQLWLVL- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTL----KMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGL-ATLK 437
Cdd:cd06638   100 -ELCNGGSVtdlvKGFLKRGERMEEPIIAYILHEALMGLQHLH--VNKTIHRDVKGNNILLT-TEGGVKLVDFGVsAQLT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSV-IGTPEFMAPEM------YEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECfsRIP 510
Cdd:cd06638   176 STRLRRNTsVGTPFWMAPEViaceqqLDSTYDARCDVWSLGITAIELGDGDPPLAD-LHPMRALFKIPRNPPPTL--HQP 252
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  511 AQYP-EIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06638   253 ELWSnEFNDFIRKCLTKDYEKRPTVSDLLQHVF 285
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
278-544 5.48e-24

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: 103.47  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  278 GRFLkfdeelGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkr 356
Cdd:cd14187    12 GRFL------GKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPhQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND----- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL 436
Cdd:cd14187    81 -FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNR--VIHRDLKLGNLFLNDDM-EVKIGDFGLATK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 --KNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRkvisgVKPECFSrIPAQY 513
Cdd:cd14187   157 veYDGERKKTLCGTPNYIAPEVLsKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLR-----IKKNEYS-IPKHI 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  514 -PEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd14187   231 nPVAASLIQKMLQTDPTARPTINELLNDEFFT 262
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
288-543 6.02e-24

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: 103.10  E-value: 6.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELM 366
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKcIEKDSVRNVLNELEILQELEHPFLVNLWYSFQD------EEDMYMVVDLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLGLAT-LKNKSFAKSV 445
Cdd:cd05578    83 LGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKN--IIHRDIKPDNI-LLDEQGHVHITDFNIATkLTDGTLATST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  446 IGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMN-PATIYRKVISGVKPEcfsrIPAQYP-EIREIIDR 522
Cdd:cd05578   160 SGTKPYMAPEVFMrAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRtSIEEIRAKFETASVL----YPAGWSeEAIDLINK 235
                         250       260
                  ....*....|....*....|..
gi 392899979  523 CIRVRREER-STVKQLLVDDFF 543
Cdd:cd05578   236 LLERDPQKRlGDLSDLKNHPYF 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
287-484 1.03e-23

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: 102.78  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTET-GVAVAWCELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKhDLEVAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEIAN------SVYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS--------VKIGDLGLAT-L 436
Cdd:cd14202    83 CNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKG--IIHRDLKPQNILLSYSGGRksnpnnirIKIADFGFARyL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14202   161 QNNMMAATLCGSPMYMAPEvIMSQHYDAKADLWSIGTIIYQCLTGKAPF 209
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
287-538 1.20e-23

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: 102.80  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGlDTETGVAVAWceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyiVLVTELM 366
Cdd:cd14149    20 IGSGSFGTVYKG-KWHGDVAVKI--LKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNL-------AIVTQWC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYL-------KRFKRINIkvlkswCRQILKGLSFLHTRNppVIHRDLKCDNIFI-TGTTgsVKIGDLGLATLKN 438
Cdd:cd14149    90 EGSSLYKHLhvqetkfQMFQLIDI------ARQTAQGMDYLHAKN--IIHRDMKSNNIFLhEGLT--VKIGDFGLATVKS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPE----FMAPEMYEEM----YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIP 510
Cdd:cd14149   160 RWSGSQQVEQPTgsilWMAPEVIRMQdnnpFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLY 239
                         250       260
                  ....*....|....*....|....*....
gi 392899979  511 AQYPE-IREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14149   240 KNCPKaMKRLVADCIKKVKEERPLFPQIL 268
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
328-543 1.89e-23

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: 101.88  E-value: 1.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  328 EAEMLKDLQHPNIVRFYDYWEsadlCGKRKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppV 407
Cdd:cd14080    52 ELEILRKLRHPNIIQVYSIFE----RGSKVFIFM--EYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLD--I 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  408 IHRDLKCDNIFITGtTGSVKIGDLGLATL----KNKSFAKSVIGTPEFMAPEMYE-EMYD-ESVDVYAFGMCLLEMVTGE 481
Cdd:cd14080   124 AHRDLKCENILLDS-NNNVKLSDFGFARLcpddDGDVLSKTFCGSAAYAAPEILQgIPYDpKKYDIWSLGVILYIMLCGS 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  482 YPYSEcMNPATIYRKVISgvKPECFSRIPAQY-PEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14080   203 MPFDD-SNIKKMLKDQQN--RKVRFPSSVKKLsPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
285-481 2.00e-23

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: 102.23  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVawcelqesklnKTERQRFR--EEAEMLKDLQ-------HPNIVRFYD-YWESADL 352
Cdd:cd07830     5 KQLGDGTFGSVYLARNKETGelVAI-----------KKMKKKFYswEECMNLREVKslrklneHPNIVKLKEvFRENDEL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CgkrkyivLVTELMTSGTLKMYLKR-FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDL 431
Cdd:cd07830    74 Y-------FVFEYMEGNLYQLMKDRkGKPFSESVIRSIIYQILQGLAHIHKHG--FFHRDLKPENLLVSG-PEVVKIADF 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  432 GLA-TLKNKSFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07830   144 GLArEIRSRPPYTDYVSTRWYRAPEILlrSTSYSSPVDIWALGCIMAELYTLR 196
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
287-542 2.51e-23

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: 101.48  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPSILELYNYFEDSN------YVYLVLEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAK- 443
Cdd:cd14186    83 CHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHG--ILHRDLTLSNLLLT-RNMNIKIADFGLATQLKMPHEKh 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 -SVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQypeirEIID 521
Cdd:cd14186   160 fTMCGTPNYISPEIAtRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQ-----DLIH 234
                         250       260
                  ....*....|....*....|.
gi 392899979  522 RCIRVRREERSTVKQLLVDDF 542
Cdd:cd14186   235 QLLRKNPADRLSLSSVLDHPF 255
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
277-545 2.58e-23

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: 102.83  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKFdEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFRE--------EAEMLKDLQHPNIVRFYDYW- 347
Cdd:cd14041     5 NDRYLLL-HLLGRGGFSEVYKAFDLTEQRYVA---VKIHQLNKNWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYFs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  348 -ESADLCgkrkyivLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTT--G 424
Cdd:cd14041    81 lDTDSFC-------TVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTacG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  425 SVKIGDLGLATLKNKSFAKSV---------IGTPEFMAPEMY-----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNP 490
Cdd:cd14041   154 EIKITDFGLSKIMDDDSYNSVdgmeltsqgAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQ 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  491 ATIYRK-VISGVKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFTP 545
Cdd:cd14041   234 QDILQEnTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLP 289
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
279-484 2.62e-23

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: 101.64  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKY 358
Cdd:cd14147     3 QELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIAL------KAVCLEEPN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRN-PPVIHRDLKCDNIFITGTT-------GSVKIGD 430
Cdd:cd14147    77 LCLVMEYAAGGPLSRALAG-RRVPPHVLVNWAVQIARGMHYLHCEAlVPVIHRDLKSNNILLLQPIenddmehKTLKITD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  431 LGLATLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14147   156 FGLAREWHKTTQMSAAGTYAWMAPEVIKaSTFSKGSDVWSFGVLLWELLTGEVPY 210
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
285-537 3.08e-23

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general 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). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk 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: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 100.97  E-value: 3.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL-DTETGVAVAWCElQESKLNKTErqrFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLVT 363
Cdd:cd05148    12 RKLGSGYFGEVWEGLwKNRVRVAIKILK-SDDLLKQQD---FQKEVQALKRLRHKHLISLFA------VCSVGEPVYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKV--LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL-KNKS 440
Cdd:cd05148    82 ELMEKGSLLAFLRSPEGQVLPVasLIDMACQVAEGMAYLEEQN--SIHRDLAARNILV-GEDLVCKVADFGLARLiKEDV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYsECMNPATIYRKVISGVKPECFSRIPaqyPEIR 517
Cdd:cd05148   159 YLSSDKKIPyKWTAPEaASHGTFSTKSDVWSFGILLYEMFTyGQVPY-PGMNNHEVYDQITAGYRMPCPAKCP---QEIY 234
                         250       260
                  ....*....|....*....|
gi 392899979  518 EIIDRCIRVRREERSTVKQL 537
Cdd:cd05148   235 KIMLECWAAEPEDRPSFKAL 254
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
281-537 4.68e-23

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR 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: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 100.95  E-value: 4.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETG----VAVAWCELQESklnkTERQRFRE---EAEMLKDLQHPNIVRFYDYWESADLC 353
Cdd:cd05057     9 LEKGKVLGSGAFGTVYKGVWIPEGekvkIPVAIKVLREE----TGPKANEEildEAYVMASVDHPHLVRLLGICLSSQVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gkrkyivLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG 432
Cdd:cd05057    85 -------LITQLMPLGCLLDYVRNHRdNIGSQLLLNWCVQIAKGMSYLEEKR--LVHRDLAARNVLVK-TPNHVKITDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LATL---KNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYsECMNPATIYRKVISGvkpecf 506
Cdd:cd05057   155 LAKLldvDEKEYHAEGGKVPiKWMALEsIQYRIYTHKSDVWSYGVTVWELMTfGAKPY-EGIPAVEIPDLLEKG------ 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  507 SRIPAqyPEIREI-----IDRCIRVRREERSTVKQL 537
Cdd:cd05057   228 ERLPQ--PPICTIdvymvLVKCWMIDAESRPTFKEL 261
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
277-484 5.77e-23

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: 100.29  E-value: 5.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKfdeELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkR 356
Cdd:cd14072     1 NYRLLK---TIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIET------E 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLA-- 434
Cdd:cd14072    72 KTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKR--IVHRDLKAENLLLDADM-NIKIADFGFSne 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  435 -TLKNKsfAKSVIGTPEFMAPEMYE-EMYD-ESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14072   149 fTPGNK--LDTFCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPF 199
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
280-543 7.72e-23

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: 100.43  E-value: 7.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFD--EELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRFRE----EAEMLKDLQ-HPNIVRFYDYWESA 350
Cdd:cd14181     9 YQKYDpkEVIGRGVSSVVRRCVHRHTGqeFAVKIIEVTAERLSPEQLEEVRSstlkEIHILRQVSgHPSIITLIDSYESS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  351 dlcgkrKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGD 430
Cdd:cd14181    89 ------TFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANN--IVHRDLKPENILLD-DQLHIKLSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLAT-LKNKSFAKSVIGTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG-- 500
Cdd:cd14181   160 FGFSChLEPGEKLRELCGTPGYLAPEILKCSMDEThpgygkeVDLWACGVILFTLLAGSPPFWH-RRQMLMLRMIMEGry 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  501 --VKPECFSRIPAqypeIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14181   239 qfSSPEWDDRSST----VKDLISRLLVVDPEIRLTAEQALQHPFF 279
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
281-538 8.02e-23

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: 100.50  E-value: 8.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-------DTETGVAVAwcELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLC 353
Cdd:cd05032     8 ITLIRELGQGSFGMVYEGLakgvvkgEPETRVAIK--TVNENA-SMRERIEFLNEASVMKEFNCHHVVRLL------GVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLK--RFKRINIKVLKS--------WCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtT 423
Cdd:cd05032    79 STGQPTLVVMELMAKGDLKSYLRsrRPEAENNPGLGPptlqkfiqMAAEIADGMAYLAAKK--FVHRDLAARNCMVAE-D 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  424 GSVKIGDLGLATLKNKS--FAKSVIGT-P-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNPATIyRKV 497
Cdd:cd05032   156 LTVKIGDFGMTRDIYETdyYRKGGKGLlPvRWMAPEsLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVL-KFV 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  498 ISG---VKPECFsripaqyPEI-REIIDRCIRVRREERSTVKQLL 538
Cdd:cd05032   235 IDGghlDLPENC-------PDKlLELMRMCWQYNPKMRPTFLEIV 272
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
285-531 9.62e-23

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: 99.44  E-value: 9.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL--DTETGVAVAWCElqeSKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLV 362
Cdd:cd05041     1 EKIGRGNFGDVYRGVlkPDNTEVAVKTCR---ETLPPDLKRKFLQEARILKQYDHPNIVKL------IGVCVQKQPIMIV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKNKSF 441
Cdd:cd05041    72 MELVPGGSLLTFLRKKGaRLTVKQLLQMCLDAAAGMEYLESKN--CIHRDLAARNCLV-GENNVLKISDFGMSREEEDGE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPE----FMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNPATiyRKVI-SGVKPECFSRIPAqyp 514
Cdd:cd05041   149 YTVSDGLKQipikWTAPEaLNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQT--REQIeSGYRMPAPELCPE--- 223
                         250
                  ....*....|....*..
gi 392899979  515 EIREIIDRCIRVRREER 531
Cdd:cd05041   224 AVYRLMLQCWAYDPENR 240
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
287-543 1.06e-22

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: 99.68  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRF-REEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLvtEL 365
Cdd:cd14162     8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFlPREIEVIKGLKHPNLICFYEAIETT----SRVYIIM--EL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA--TLKNKS--- 440
Cdd:cd14162    82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKG--VVHRDLKCENLLLDK-NNNLKITDFGFArgVMKTKDgkp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 -FAKSVIGTPEFMAPEMYEEM-YDESV-DVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKpecFSRIPAQYPEIR 517
Cdd:cd14162   159 kLSETYCGSYAYASPEILRGIpYDPFLsDIWSMGVVLYTMVYGRLPFDD-SNLKVLLKQVQRRVV---FPKNPTVSEECK 234
                         250       260
                  ....*....|....*....|....*.
gi 392899979  518 EIIDRcIRVRREERSTVKQLLVDDFF 543
Cdd:cd14162   235 DLILR-MLSPVKKRITIEEIKRDPWF 259
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
280-484 1.14e-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: 99.31  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAvaWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYI 359
Cdd:cd14191     3 FYDIEERLGSGKFGQVFRLVEKKTKKV--WAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFE------EKANI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTL--KMYLKRFKRINIKVLKsWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLA-T 435
Cdd:cd14191    75 VMVLEMVSGGELfeRIIDEDFELTERECIK-YMRQISEGVEYIHKQG--IVHLDLKPENIMCVNKTGTkIKLIDFGLArR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  436 LKNKSFAKSVIGTPEFMAPEM--YEEMYDESvDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14191   152 LENAGSLKVLFGTPEFVAPEVinYEPIGYAT-DMWSIGVICYILVSGLSPF 201
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
281-538 1.19e-22

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: 100.31  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAW----CELQESKLNKterqrFREEAEMLKDLQHPNIVRFYD--YWESAdlcg 354
Cdd:cd06622     3 IEVLDELGKGNYGSVYKVLHRPTGVTMAMkeirLELDESKFNQ-----IIMELDILHKAVSPYIVDFYGafFIEGA---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 krkyIVLVTELMTSGTL-KMY--LKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITGTtGSVKIGDL 431
Cdd:cd06622    74 ----VYMCMEYMDAGSLdKLYagGVATEGIPEDVLRRITYAVVKGLKFLKEEHN-IIHRDVKPTNVLVNGN-GQVKLCDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLATLKNKSFAKSVIGTPEFMAPEMYEEM-------YDESVDVYAFGMCLLEMVTGEYPYsecmnPATIYRKVISGVKPE 504
Cdd:cd06622   148 GVSGNLVASLAKTNIGCQSYMAPERIKSGgpnqnptYTVQSDVWSLGLSILEMALGRYPY-----PPETYANIFAQLSAI 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  505 CFS---RIPAQY-PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd06622   223 VDGdppTLPSGYsDDAQDFVAKCLNKIPNRRPTYAQLL 260
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
281-544 1.34e-22

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: 99.73  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYI 359
Cdd:cd05072     9 IKLVKKLGAGQFGEVWMGYyNNSTKVAV-----KTLKPGTMSVQAFLEEANLMKTLQHDKLVRLY------AVVTKEEPI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFK--RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL- 436
Cdd:cd05072    78 YIITEYMAKGSLLDFLKSDEggKVLLPKLIDFSAQIAEGMAYIERKN--YIHRDLRAANVLVSESL-MCKIADFGLARVi 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:cd05072   155 eDNEYTAREGAKFPiKWTAPEAinFGSFTIKS-DVWSFGILLYEIVTyGKIPYPG-MSNSDVMSALQRGYRMPRMENCPD 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  512 qypEIREIIDRCIRVRREERSTVK--QLLVDDFFT 544
Cdd:cd05072   233 ---ELYDIMKTCWKEKAEERPTFDylQSVLDDFYT 264
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
286-549 1.53e-22

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: 100.06  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQRFRE----EAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVL 361
Cdd:cd06659    28 KIGEGSTGVVCIAREKHSGRQVA------VKMMDLRKQQRREllfnEVVIMRDYQHPNVVEMYKSY----LVGEELWVLM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 vtELMTSGTLKMYLKRFkRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSF 441
Cdd:cd06659    98 --EYLQGGALTDIVSQT-RLNEEQIATVCEAVLQALAYLHSQG--VIHRDIKSDSILLT-LDGRVKLSDFGFCAQISKDV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AK--SVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPY-SEcmNPATIYRKVISGVKPEC--FSRIPaqyPE 515
Cdd:cd06659   172 PKrkSLVGTPYWMAPEVISRcPYGTEVDIWSLGIMVIEMVDGEPPYfSD--SPVQAMKRLRDSPPPKLknSHKAS---PV 246
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLvDDFF-----TPEDLI 549
Cdd:cd06659   247 LRDFLERMLVRDPQERATAQELL-DHPFllqtgLPECLV 284
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
279-538 1.69e-22

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: 99.62  E-value: 1.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSF-KTVFRGLDTE---TGVAVAWCELQ-ESKLNKTerQRFREEAEMLKDLQHPNIVRFydywesADLC 353
Cdd:cd05079     4 RFLKRIRDLGEGHFgKVELCRYDPEgdnTGEQVAVKSLKpESGGNHI--ADLKKEIEILRNLYHENIVKY------KGIC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 --GKRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGD 430
Cdd:cd05079    76 teDGGNGIKLIMEFLPSGSLKEYLPRNKnKINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVE-SEHQVKIGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGL--ATLKNKSF--AKSVIGTPEF-MAPE--MYEEMYDESvDVYAFGMCLLEMVTgeYPYSECmNPATIYRKVISGVKP 503
Cdd:cd05079   153 FGLtkAIETDKEYytVKDDLDSPVFwYAPEclIQSKFYIAS-DVWSFGVTLYELLT--YCDSES-SPMTLFLKMIGPTHG 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  504 E-CFSR------------IPAQYPE-IREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05079   229 QmTVTRlvrvleegkrlpRPPNCPEeVYQLMRKCWEFQPSKRTTFQNLI 277
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
285-480 2.05e-22

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: 99.48  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTE---RQRFREeAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVL 361
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVA---LKEIHLDAEEgtpSTAIRE-ISLMKELKHENIVRLHDVIHTEN------KLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMtSGTLKMYLKRFKR---INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLAT--- 435
Cdd:cd07836    76 VFEYM-DKDLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENR--VLHRDLKPQNLLINK-RGELKLADFGLARafg 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  436 LKNKSFAKSVIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07836   152 IPVNTFSNEVV-TLWYRAPDvlLGSRTYSTSIDIWSVGCIMAEMITG 197
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
286-561 2.64e-22

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: 99.73  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFydywESADLCGKRKYIVLVTE 364
Cdd:cd06633    28 EIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEY----KGCYLKDHTAWLVMEYC 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMT-SGTLKMYLKRFKRINIKVLKswcRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKnkSFAK 443
Cdd:cd06633   104 LGSaSDLLEVHKKPLQEVEIAAIT---HGALQGLAYLHSHN--MIHRDIKAGNILLT-EPGQVKLADFGSASIA--SPAN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPE----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRipAQYPEIREI 519
Cdd:cd06633   176 SFVGTPYWMAPEvilaMDEGQYDGKVDIWSLGITCIELAERKPPLFN-MNAMSALYHIAQNDSPTLQSN--EWTDSFRGF 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392899979  520 IDRCIRVRREERSTVKQLLVDDFFTPEDLIGIRVEIKNRDAD 561
Cdd:cd06633   253 VDYCLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTKD 294
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
285-537 3.34e-22

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: 98.19  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG---VAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCgkrkyivL 361
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSgkeVEVAVKTLKQEH-EKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-------L 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL--ATLKNK 439
Cdd:cd05060    73 VMELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKH--FVHRDLAARNVLLV-NRHQAKISDFGMsrALGAGS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGT--P-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPaqyP 514
Cdd:cd05060   150 DYYRATTAGrwPlKWYAPEcINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGE-MKGPEVIAMLESGERLPRPEECP---Q 225
                         250       260
                  ....*....|....*....|...
gi 392899979  515 EIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05060   226 EIYSIMLSCWKYRPEDRPTFSEL 248
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
280-484 3.82e-22

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: 98.15  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAE----MLKDLQHPNIVRFYDYWESadlcgk 355
Cdd:cd14195     6 HYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIErevnILREIQHPNIITLHDIFEN------ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIGDLG 432
Cdd:cd14195    80 KTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKR--IAHFDLKPENIMLldkNVPNPRIKLIDFG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  433 LA-TLKNKSFAKSVIGTPEFMAPEM--YEEMYDESvDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14195   158 IAhKIEAGNEFKNIFGTPEFVAPEIvnYEPLGLEA-DMWSIGVITYILLSGASPF 211
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
287-543 3.95e-22

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: 98.65  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLVTELM 366
Cdd:cd07846     9 VGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLI------EVFRRKKRWYLVFEFV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA-TLK--NKSFA 442
Cdd:cd07846    83 DH-TVLDDLEKYPNgLDESRVRKYLFQILRGIDFCHSHN--IIHRDIKPENILVS-QSGVVKLCDFGFArTLAapGEVYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSViGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE--YPYSE---------------CMNPATIYRK--VISGV 501
Cdd:cd07846   159 DYV-ATRWYRAPELLvgDTKYGKAVDVWAVGCLVTEMLTGEplFPGDSdidqlyhiikclgnlIPRHQELFQKnpLFAGV 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  502 K-PECFSRIPAQ--YPEIREI-ID---RCIRVRREERSTVKQLLVDDFF 543
Cdd:cd07846   238 RlPEVKEVEPLErrYPKLSGVvIDlakKCLHIDPDKRPSCSELLHHEFF 286
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
282-538 4.12e-22

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: 98.65  E-value: 4.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVL 361
Cdd:cd14086     4 DLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEG------FHYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLkmylkrFKRINIKVL-----KSWC-RQILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGL 433
Cdd:cd14086    78 VFDLVTGGEL------FEDIVAREFyseadASHCiQQILESVNHCHQNG--IVHRDLKPENLLLASKSkgAAVKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 ATLKNKS------FAksviGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGV----K 502
Cdd:cd14086   150 AIEVQGDqqawfgFA----GTPGYLSPEVLRKDpYGKPVDIWACGVILYILLVGYPPFWD-EDQHRLYAQIKAGAydypS 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  503 PEcFSRIPaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14086   225 PE-WDTVT---PEAKDLINQMLTVNPAKRITAAEAL 256
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
287-504 4.38e-22

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: 98.45  E-value: 4.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLVTEL 365
Cdd:cd14026     5 LSRGAFGTVSRARHADWRVTVAIKCLKlDSPVGDSERNCLLKEAEILHKARFSYILPILG------ICNEPEFLGIVTEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRfKRINIKVlkSWC------RQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNK 439
Cdd:cd14026    79 MTNGSLNELLHE-KDIYPDV--AWPlrlrilYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEF-HVKIADFGLSKWRQL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  440 SFAKS-------VIGTPEFMAPEMYE----EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPE 504
Cdd:cd14026   155 SISQSrssksapEGGTIIYMPPEEYEpsqkRRASVKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGHRPD 230
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
287-543 4.69e-22

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: 97.72  E-value: 4.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQ-RFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14079    10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEeKIRREIQILKLFRHPHIIRLYEVIETPT------DIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLATL-KNKSFAKS 444
Cdd:cd14079    84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCH-RHM-VVHRDLKPENLLLD-SNMNVKIADFGLSNImRDGEFLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VIGTPEFMAPEMYE-EMYDES-VDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPecfsrIPAQY-PEIREIID 521
Cdd:cd14079   161 SCGSPNYAAPEVISgKLYAGPeVDVWSCGVILYALLCGSLPFDD-EHIPNLFKKIKSGIYT-----IPSHLsPGARDLIK 234
                         250       260
                  ....*....|....*....|..
gi 392899979  522 RCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14079   235 RMLVVDPLKRITIPEIRQHPWF 256
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
287-545 4.76e-22

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: 98.59  E-value: 4.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTetgVAVAWCELQESKLNKTERQRFRE--------EAEMLKDLQHPNIVRFYDYW--ESADLCgkr 356
Cdd:cd14040    14 LGRGGFSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYFslDTDTFC--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kyivLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTT--GSVKIGDLGLA 434
Cdd:cd14040    88 ----TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacGEIKITDFGLS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLKNK--------SFAKSVIGTPEFMAPEMY-----EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRK-VISG 500
Cdd:cd14040   164 KIMDDdsygvdgmDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEnTILK 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  501 VKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFTP 545
Cdd:cd14040   244 ATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLP 288
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
285-542 5.20e-22

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: 98.53  E-value: 5.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQE-SKLNkterQRFREEAEMLKDL-QHPNIVRFYDYWESADLC-GKRKYIVL 361
Cdd:cd06639    28 ETIGKGTYGKVYKVTNKKDGSLAAVKILDPiSDVD----EEIEAEYNILRSLpNHPNVVKFYGMFYKADQYvGGQLWLVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 vtELMTSGT----LKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGL-ATL 436
Cdd:cd06639   104 --ELCNGGSvtelVKGLLKCGQRLDEAMISYILYGALLGLQHLH--NNRIIHRDVKGNNILLT-TEGGVKLVDFGVsAQL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSV-IGTPEFMAPEM------YEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSri 509
Cdd:cd06639   179 TSARLRRNTsVGTPFWMAPEViaceqqYDYSYDARCDVWSLGITAIELADGDPPLFD-MHPVKALFKIPRNPPPTLLN-- 255
                         250       260       270
                  ....*....|....*....|....*....|....
gi 392899979  510 PAQY-PEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06639   256 PEKWcRGFSHFISQCLIKDFEKRPSVTHLLEHPF 289
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
277-485 5.28e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.57  E-value: 5.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFlKFDEELGRGSFKTVFRGLDTETG--VAVawcelqesKLNKTE-------RQRFREEAEMLKDLQHPNIVRFYDYW 347
Cdd:NF033483    6 GGRY-EIGERIGRGGMAEVYLAKDTRLDrdVAV--------KVLRPDlardpefVARFRREAQSAASLSHPNIVSVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  348 ESADLcgkrKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVK 427
Cdd:NF033483   77 EDGGI----PYIVM--EYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILIT-KDGRVK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  428 IGDLGLA------TLKNKSfakSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:NF033483  148 VTDFGIAralsstTMTQTN---SVLGTVHYLSPEQARgGTVDARSDIYSLGIVLYEMLTGRPPFD 209
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
285-523 7.28e-22

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: 97.57  E-value: 7.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVF---RGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKD-------LQHPNIVRFYDYWesadLCG 354
Cdd:cd08528     6 ELLGSGAFGCVYkvrKKSNGQTLLALKEINMTNPAFGRTEQERDKSVGDIISEvniikeqLRHPNIVRYYKTF----LEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVL-------VTELMTSgtLKMYLKRF--KRI-NIKVlkswcrQILKGLSFLHtRNPPVIHRDLKCDNIFItGTTG 424
Cdd:cd08528    82 DRLYIVMeliegapLGEHFSS--LKEKNEHFteDRIwNIFV------QMVLALRYLH-KEKQIVHRDLKPNNIML-GEDD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  425 SVKIGDLGLATLK--NKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYP-YSECM------------ 488
Cdd:cd08528   152 KVTITDFGLAKQKgpESSKMTSVVGTILYSCPEIVQnEPYGEKADIWALGCILYQMCTLQPPfYSTNMltlatkiveaey 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  489 --NPATIYRKVISGVKPECFSRIPAQYPEIREIIDRC 523
Cdd:cd08528   232 epLPEGMYSDDITFVIRSCLTPDPEARPDIVEVSSMI 268
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
286-561 7.44e-22

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: 98.58  E-value: 7.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDywesadlCGKRKYIV-LVT 363
Cdd:cd06635    32 EIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKG-------CYLREHTAwLVM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELM---TSGTLKMYLKRFKRINIKVLKswcRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKnkS 440
Cdd:cd06635   105 EYClgsASDLLEVHKKPLQEIEIAAIT---HGALQGLAYLHSHN--MIHRDIKAGNILLT-EPGQVKLADFGSASIA--S 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPE----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPAQYpeI 516
Cdd:cd06635   177 PANSFVGTPYWMAPEvilaMDEGQYDGKVDVWSLGITCIELAERKPPLFN-MNAMSALYHIAQNESPTLQSNEWSDY--F 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDFFTPEDLIGIRVEIKNRDAD 561
Cdd:cd06635   254 RNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKD 298
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
287-478 1.15e-21

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: 96.81  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQesKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTELM 366
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELI--RFDEEAQRNFLKEVKVMRSLDHPNVLKF------IGVLYKDKKLNLITEYI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRI---NIKVlkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL------- 436
Cdd:cd14154    73 PGGTLKDVLKDMARPlpwAQRV--RFAKDIASGMAYLHSMN--IIHRDLNSHNCLVREDK-TVVVADFGLARLiveerlp 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  437 -------KNKSFAKS--------VIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMV 478
Cdd:cd14154   148 sgnmspsETLRHLKSpdrkkrytVVGNPYWMAPEMLNgRSYDEKVDIFSFGIVLCEII 205
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
286-544 1.23e-21

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: 97.40  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR-EEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLvtE 364
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVA---VKKMDLRKQQRRELLfNEVVIMRDYQHENVVEMYNSY----LVGDELWVVM--E 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA-- 442
Cdd:cd06657    98 FLEGGALTDIVTH-TRMNEEQIAAVCLAVLKALSVLHAQG--VIHRDIKSDSILLT-HDGRVKLSDFGFCAQVSKEVPrr 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcmNPATIYRKVISGVKPECFSRIPAQYPEIREIID 521
Cdd:cd06657   174 KSLVGTPYWMAPELISRLpYGPEVDIWSLGIMVIEMVDGEPPYFN--EPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLD 251
                         250       260
                  ....*....|....*....|...
gi 392899979  522 RCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06657   252 RLLVRDPAQRATAAELLKHPFLA 274
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
282-488 1.31e-21

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: 96.47  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRF-REEAEMLKDLQHPNIVRFYDYWEsadLCGKRKYIV 360
Cdd:cd14164     3 TLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFlPRELSILRRVNHPNIVQMFECIE---VANGRLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTelmTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLATLKN-- 438
Cdd:cd14164    80 MEA---AATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMN--IVHRDLKCENILLSADDRKIKIADFGFARFVEdy 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEM-YD-ESVDVYAFGMCLLEMVTGEYPYSECM 488
Cdd:cd14164   155 PELSTTFCGSRAYTPPEVILGTpYDpKKYDVWSLGVVLYVMVTGTMPFDETN 206
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
286-543 1.55e-21

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: 97.51  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTE-----RQRFREEAEMLKDLQHPNIVRFYD-YWESADLCgkrkyi 359
Cdd:cd06615     8 ELGAGNGGVVTKVLHRPSGLIMA------RKLIHLEikpaiRNQIIRELKVLHECNSPYIVGFYGaFYSDGEIS------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 vLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd06615    76 -ICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHK-IMHRDVKPSNILVN-SRGEIKLCDFGVSGQLID 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYS-------ECMNPatiyRKVISGVKPECFSRIPA 511
Cdd:cd06615   153 SMANSFVGTRSYMSPERLQgTHYTVQSDIWSLGLSLVEMAIGRYPIPppdakelEAMFG----RPVSEGEAKESHRPVSG 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  512 QYP------------------------------EIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06615   229 HPPdsprpmaifelldyivnepppklpsgafsdEFQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
285-542 1.79e-21

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: 96.29  E-value: 1.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLD--TETGVAVAWCELQESKlnkTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYIVLV 362
Cdd:cd06641    10 EKIGKGSFGEVFKGIDnrTQKVVAIKIIDLEEAE---DEIEDIQQEITVLSQCDSPYVTKYYGSYL------KDTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTlKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpvIHRDLKCDNIFITgTTGSVKIGDLGLA-TLKNKSF 441
Cdd:cd06641    81 MEYLGGGS-ALDLLEPGPLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLS-EHGEVKLADFGVAgQLTDTQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSV-IGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSECM-----------NPATI---YRKVISGVKPEC 505
Cdd:cd06641   157 KRN*fVGTPFWMAPEVIKQsAYDSKADIWSLGITAIELARGEPPHSELHpmkvlflipknNPPTLegnYSKPLKEFVEAC 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  506 FSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06641   237 LNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRY 273
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
287-486 1.92e-21

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: 96.03  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTEtGVAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYIVLVTELM 366
Cdd:cd14664     1 IGRGGAGTVYKGVMPN-GTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGY------CSNPTTNLLVYEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTL----------KMYLKRFKRINIKVlkswcrQILKGLSFLHTR-NPPVIHRDLKCDNIFITGTTGSVkIGDLGLAT 435
Cdd:cd14664    73 PNGSLgellhsrpesQPPLDWETRQRIAL------GSARGLAYLHHDcSPLIIHRDVKSNNILLDEEFEAH-VADFGLAK 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  436 L---KNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14664   146 LmddKDSHVMSSVAGSYGYIAPEyAYTGKVSEKSDVYSYGVVLLELITGKRPFDE 200
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
285-542 2.82e-21

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: 95.89  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLD--TETGVAVAWCELQESklnKTERQRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLv 362
Cdd:cd06640    10 ERIGKGSFGEVFKGIDnrTQQVVAIKIIDLEEA---EDEIEDIQQEITVLSQCDSPYVTKYYGSY----LKGTKLWIIM- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTLKMYLKR--FKRINIKVLkswCRQILKGLSFLHTRNPpvIHRDLKCDNIFITgTTGSVKIGDLGLA------ 434
Cdd:cd06640    82 -EYLGGGSALDLLRAgpFDEFQIATM---LKEILKGLDYLHSEKK--IHRDIKAANVLLS-EQGDVKLADFGVAgqltdt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLKNKSFaksvIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPAQY 513
Cdd:cd06640   155 QIKRNTF----VGTPFWMAPEVIQQsAYDSKADIWSLGITAIELAKGEPPNSD-MHPMRVLFLIPKNNPPTLVGDFSKPF 229
                         250       260
                  ....*....|....*....|....*....
gi 392899979  514 peiREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06640   230 ---KEFIDACLNKDPSFRPTAKELLKHKF 255
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
285-480 2.84e-21

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: 96.24  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGR---GSFKTVFRGLDTETGVAVAWCELQESKLN-KTERQRFREeAEMLKDLQ-HPNIVRFYD-YWESADLcgkrky 358
Cdd:cd07832     3 KILGRigeGAHGIVFKAKDRETGETVALKKVALRKLEgGIPNQALRE-IKALQACQgHPYVVKLRDvFPHGTGF------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 iVLVTELMTSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLK 437
Cdd:cd07832    76 -VLVFEYMLS-SLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLI-SSTGVLKIADFGLARLF 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  438 NKSFAK---SVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07832   151 SEEDPRlysHQVATRWYRAPELLygSRKYDEGVDLWAVGCIFAELLNG 198
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
287-543 3.71e-21

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: 95.08  E-value: 3.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTEL 365
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPhQREKIDKEIELHRILHHKHVVQFYHYFED------KENIYILLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT----LKNKSf 441
Cdd:cd14188    83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQE--ILHRDLKLGNFFINENM-ELKVGDFGLAArlepLEHRR- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 aKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRkvisGVKPECFSRIPAQYPEIREII 520
Cdd:cd14188   159 -RTICGTPNYLSPEvLNKQGHGCESDIWALGCVMYTMLLGRPPF-ETTNLKETYR----CIREARYSLPSSLLAPAKHLI 232
                         250       260
                  ....*....|....*....|...
gi 392899979  521 DRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14188   233 ASMLSKNPEDRPSLDEIIRHDFF 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
283-542 3.90e-21

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: 94.79  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLv 362
Cdd:cd14074     7 LEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQ----TKLYLIL- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT--LKNK 439
Cdd:cd14074    82 -ELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLH--VVHRDLKPENVVFFEKQGLVKLTDFGFSNkfQPGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSViGTPEFMAPE-MYEEMYDE-SVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVisgvkpECFSRIPAQY-PEI 516
Cdd:cd14074   159 KLETSC-GSLAYSAPEiLLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIM------DCKYTVPAHVsPEC 231
                         250       260
                  ....*....|....*....|....*.
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd14074   232 KDLIRRMLIRDPKKRASLEEIENHPW 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
282-537 4.01e-21

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: 95.02  E-value: 4.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTeTGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIV 360
Cdd:cd14161     6 EFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIkDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSS------KIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK- 439
Cdd:cd14161    79 IVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANG--IVHRDLKLENILLD-ANGNIKIADFGLSNLYNQd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEYPYSecmnpATIYRKVISGVKPECFsRIPAQYPEIR 517
Cdd:cd14161   156 KFLQTYCGSPLYASPEIVngRPYIGPEVDSWSLGVLLYILVHGTMPFD-----GHDYKILVKQISSGAY-REPTKPSDAC 229
                         250       260
                  ....*....|....*....|
gi 392899979  518 EIIDRCIRVRREERSTVKQL 537
Cdd:cd14161   230 GLIRWLLMVNPERRATLEDV 249
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
285-544 4.23e-21

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: 95.51  E-value: 4.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETG--VAVAWCELQESKlnkTERQRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLv 362
Cdd:cd06642    10 ERIGKGSFGEVYKGIDNRTKevVAIKIIDLEEAE---DEIEDIQQEITVLSQCDSPYITRYYGSY----LKGTKLWIIM- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNPpvIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd06642    82 -EYLGGGSALDLLKP-GPLEETYIATILREILKGLDYLHSERK--IHRDIKAANVLLS-EQGDVKLADFGVAGQLTDTQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 K--SVIGTPEFMAPEMYEE-MYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPEcfsrIPAQYPE-IRE 518
Cdd:cd06642   157 KrnTFVGTPFWMAPEVIKQsAYDFKADIWSLGITAIELAKGEPPNSD-LHPMRVLFLIPKNSPPT----LEGQHSKpFKE 231
                         250       260
                  ....*....|....*....|....*.
gi 392899979  519 IIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06642   232 FVEACLNKDPRFRPTAKELLKHKFIT 257
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
319-538 4.28e-21

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: 94.73  E-value: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  319 KTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLS 398
Cdd:cd14012    39 KKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  399 FLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGDLGLATLKNKSFAKSVIGTPE---FMAPEMYEE--MYDESVDVYAFG 471
Cdd:cd14012   119 YLHRNG--VVHKSLHAGNVLLDrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKqtyWLPPELAQGskSPTRKTDVWDLG 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  472 MCLLEMVTGeypySECMNPATIYRKVISgvkPECFSripaqyPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14012   197 LLFLQMLFG----LDVLEKYTSPNPVLV---SLDLS------ASLQDFLSKCLSLDPKKRPTALELL 250
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
285-547 4.43e-21

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: 95.48  E-value: 4.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSF----KTVFRGLDTETGVAVawcelqeskLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIV 360
Cdd:cd14175     7 ETIGVGSYsvckRCVHKATNMEYAVKV---------IDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDG------KHVY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG---SVKIGDLGLAtlK 437
Cdd:cd14175    72 LVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQG--VVHRDLKPSNILYVDESGnpeSLRICDFGFA--K 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTP----EFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcmNPATIYRKVISGVKPECFSRIPAQ 512
Cdd:cd14175   148 QLRAENGLLMTPcytaNFVAPEVLKRQgYDEGCDIWSLGILLYTMLAGYTPFAN--GPSDTPEEILTRIGSGKFTLSGGN 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  513 YPEI----REIIDRCIRVRREERSTVKQLLVDDFFTPED 547
Cdd:cd14175   226 WNTVsdaaKDLVSKMLHVDPHQRLTAKQVLQHPWITQKD 264
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
285-484 5.29e-21

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: 94.70  E-value: 5.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAE----MLKDLQHPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14194    11 EELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIErevsILKEIQHPNVITLHEVYEN------KTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG---SVKIGDLGLA-TL 436
Cdd:cd14194    85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQ--IAHFDLKPENIMLLDRNVpkpRIKIIDFGLAhKI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEM--YEEMYDESvDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14194   163 DFGNEFKNIFGTPEFVAPEIvnYEPLGLEA-DMWSIGVITYILLSGASPF 211
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
287-493 5.44e-21

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: 95.01  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELqeSKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTELM 366
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSLDHPNVLKF------IGVLYKDKRLNLLTEFI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL------------- 433
Cdd:cd14222    73 EGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMS--IIHRDLNSHNCLIK-LDKTVVVADFGLsrliveekkkppp 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 --ATLKNKSFAK-------SVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMnPATI 493
Cdd:cd14222   150 dkPTTKKRTLRKndrkkryTVVGNPYWMAPEMLNgKSYDEKVDIFSFGIVLCEIIGQVYADPDCL-PRTL 218
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
277-482 5.85e-21

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: 95.72  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKFdEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLK--------DLQHPNIVRFYDYWE 348
Cdd:cd14136     9 NGRYHVV-RKLGWGHFSTVWLCWDLQNKRFVA---LKVVKSAQHYTEAALDEIKLLKcvreadpkDPGREHVVQLLDDFK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 SADLCGKrkYIVLVTELMTSGTLKMyLKR--FKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITGTTGSV 426
Cdd:cd14136    85 HTGPNGT--HVCMVFEVLGPNLLKL-IKRynYRGIPLPLVKKIARQVLQGLDYLHTKCG-IIHTDIKPENVLLCISKIEV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  427 KIGDLGLATLKNKSFAKSvIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEY 482
Cdd:cd14136   161 KIADLGNACWTDKHFTED-IQTRQYRSPEvILGAGYGTPADIWSTACMAFELATGDY 216
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
285-537 7.11e-21

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: 93.92  E-value: 7.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG-LDTETGVAVAWCElqeSKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVT 363
Cdd:cd05085     2 ELLGKGNFGEVYKGtLKDKTPVAVKTCK---EDLPQELKIKFLSEARILKQYDHPNIVKL------IGVCTQRQPIYIVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd05085    73 ELVPGGDFLSFLRKKKdELKTKQLVKFSLDAAAGMAYLESKN--CIHRDLAARNCLV-GENNALKISDFGMSRQEDDGVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KS--VIGTP-EFMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATiYRKVISGVKPECFSRIPAqypEI 516
Cdd:cd05085   150 SSsgLKQIPiKWTAPEAlnYGRYSSES-DVWSFGILLWETFSlGVCPYPGMTNQQA-REQVEKGYRMSAPQRCPE---DI 224
                         250       260
                  ....*....|....*....|.
gi 392899979  517 REIIDRCIRVRREERSTVKQL 537
Cdd:cd05085   225 YKIMQRCWDYNPENRPKFSEL 245
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
280-500 8.75e-21

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: 93.61  E-value: 8.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyI 359
Cdd:cd14071     1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDM------L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATL-KN 438
Cdd:cd14071    75 YLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRH--IVHRDLKAENLLLDA-NMNIKIADFGFSNFfKP 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE--EMYDESVDVYAFGMCLLEMVTGEYPYsECMNPATIYRKVISG 500
Cdd:cd14071   152 GELLKTWCGSPPYAAPEVFEgkEYEGPQLDIWSLGVVLYVLVCGALPF-DGSTLQTLRDRVLSG 214
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
286-561 1.02e-20

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: 95.09  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDywesadlCGKRKYIV-LVT 363
Cdd:cd06634    22 EIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRG-------CYLREHTAwLVM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELM---TSGTLKMYLKRFKRINIKVLKswcRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKnkS 440
Cdd:cd06634    95 EYClgsASDLLEVHKKPLQEVEIAAIT---HGALQGLAYLHSHN--MIHRDVKAGNILLT-EPGLVKLGDFGSASIM--A 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPE----MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPAQYpeI 516
Cdd:cd06634   167 PANSFVGTPYWMAPEvilaMDEGQYDGKVDVWSLGITCIELAERKPPLFN-MNAMSALYHIAQNESPALQSGHWSEY--F 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDFFTPEDLIGIRVEIKNRDAD 561
Cdd:cd06634   244 RNFVDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTKD 288
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
287-484 1.12e-20

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: 93.59  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTE-TGVAVAWCELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQ-NLLGKEIKILKELSHENVVALLDCQETSS------SVYLVMEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS--------VKIGDLGLAT-L 436
Cdd:cd14120    74 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKG--IVHRDLKPQNILLSHNSGRkpspndirLKIADFGFARfL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14120   152 QDGMMAATLCGSPMYMAPEVIMSLqYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
287-552 1.49e-20

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: 93.75  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFR-EEAEMLKDLQHPNIVRF-YDYWESADLCgkrkyivLVTE 364
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMAlNEKIILEKVSSPFIVSLaYAFETKDKLC-------LVLT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKS--WCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKSF 441
Cdd:cd05577    74 LMNGGDLKYHIYNVGTRGFSEARAifYAAEIICGLEHLHNRF--IVYRDLKPENILLD-DHGHVRISDLGLAVeFKGGKK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYP---YSECMNPATIYRKVISgvkpecfsrIPAQYPEi 516
Cdd:cd05577   151 IKGRVGTHGYMAPEvlQKEVAYDFSVDWFALGCMLYEMIAGRSPfrqRKEKVDKEELKRRTLE---------MAVEYPD- 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  517 reiidrciRVRREERSTVKQLLVDDfftPEDLIGIR 552
Cdd:cd05577   221 --------SFSPEARSLCEGLLQKD---PERRLGCR 245
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
287-497 1.76e-20

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: 93.87  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCElQEskLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTE 364
Cdd:cd14038     2 LGTGGFGNVLRWINQETGeqVAIKQCR-QE--LSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLAPNDLPLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKR---INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSV--KIGDLGLAT-LKN 438
Cdd:cd14038    79 YCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENR--IIHRDLKPENIVLQQGEQRLihKIIDLGYAKeLDQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKV 497
Cdd:cd14038   157 GSLCTSFVGTLQYLAPELLEQQkYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHGKV 216
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
281-522 2.00e-20

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: 93.59  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG-----LDTETGVAVAWCELQESKLNKTeRQRFREEAEMLKDLQHPNIVrfydywESADLCGK 355
Cdd:cd05048     7 VRFLEELGEGAFGKVYKGellgpSSEESAISVAIKTLKENASPKT-QQDFRREAELMSDLQHPNIV------CLLGVCTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKR--------FKRINIKVLKS-WCR-------QILKGLSFLHTRNppVIHRDLKCDNIFI 419
Cdd:cd05048    80 EQPQCMLFEYMAHGDLHEFLVRhsphsdvgVSSDDDGTASSlDQSdflhiaiQIAAGMEYLSSHH--YVHRDLAARNCLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  420 tGTTGSVKIGDLGLATLKNKS-----FAKSVIgtP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPY------ 484
Cdd:cd05048   158 -GDGLTVKISDFGLSRDIYSSdyyrvQSKSLL--PvRWMPPEaiLYGKFTTES-DVWSFGVVLWEIFSyGLQPYygysnq 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  485 ---------------SECmnPATIYRKVIsgvkpECFSRIPAQYPEIREIIDR 522
Cdd:cd05048   234 eviemirsrqllpcpEDC--PARVYSLMV-----ECWHEIPSRRPRFKEIHTR 279
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
287-526 2.02e-20

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: 93.62  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14209     9 LGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQvEHTLNEKRILQAINFPFLVKLEYSFKDNS------NLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGlatlknksFAKSV 445
Cdd:cd14209    83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLD--LIYRDLKPENLLID-QQGYIKVTDFG--------FAKRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  446 -------IGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVISG-VK-PECFSripaqyPE 515
Cdd:cd14209   152 kgrtwtlCGTPEYLAPEIILSKgYNKAVDWWALGVLIYEMAAGYPPFF-ADQPIQIYEKIVSGkVRfPSHFS------SD 224
                         250
                  ....*....|.
gi 392899979  516 IREIIDRCIRV 526
Cdd:cd14209   225 LKDLLRNLLQV 235
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
285-484 2.21e-20

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: 92.94  E-value: 2.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAE----MLKDLQHPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14105    11 EELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIErevsILRQVLHPNIITLHDVFEN------KTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT---GSVKIGDLGLA-TL 436
Cdd:cd14105    85 LILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKN--IAHFDLKPENIMLLDKNvpiPRIKLIDFGLAhKI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTPEFMAPEM--YEEMYDESvDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14105   163 EDGNEFKNIFGTPEFVAPEIvnYEPLGLEA-DMWSIGVITYILLSGASPF 211
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
285-480 2.30e-20

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: 93.21  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLV 362
Cdd:cd07844     6 DKLGEGSYATVYKGRSKLTGQLVA---LKEIRLEHEEGAPFTaiREASLLKDLKHANIVTLH------DIIHTKKTLTLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSgTLKMYLKRFKRI----NIKVlksWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd07844    77 FEYLDT-DLKQYMDDCGGGlsmhNVRL---FLFQLLRGLAYCHQRR--VLHRDLKPQNLLIS-ERGELKLADFGLARAKS 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  439 ---KSFAKSVIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07844   150 vpsKTYSNEVV-TLWYRPPDvlLGSTEYSTSLDMWGVGCIFYEMATG 195
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
286-543 2.55e-20

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: 93.56  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR-EEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIVLvtE 364
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVA---VKKMDLRKQQRRELLfNEVVIMRDYHHENVVDMYNSY----LVGDELWVVM--E 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAK- 443
Cdd:cd06658   100 FLEGGALTDIVTH-TRMNEEQIATVCLSVLRALSYLHNQG--VIHRDIKSDSILLT-SDGRIKLSDFGFCAQVSKEVPKr 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 -SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPEcFSRIPAQYPEIREIID 521
Cdd:cd06658   176 kSLVGTPYWMAPEVISRLpYGTEVDIWSLGIMVIEMIDGEPPYFN-EPPLQAMRRIRDNLPPR-VKDSHKVSSVLRGFLD 253
                         250       260
                  ....*....|....*....|..
gi 392899979  522 RCIRVRREERSTVKQLLVDDFF 543
Cdd:cd06658   254 LMLVREPSQRATAQELLQHPFL 275
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
285-542 2.68e-20

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: 93.15  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDYWESADLCGKRKYIVLVT 363
Cdd:cd06636    22 EVVGNGTYGQVYKGRHVKTGQLAA---IKVMDVTEDEEEEIKLEINMLKKYsHHRNIATYYGAFIKKSPPGHDDQLWLVM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKvlKSW----CRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd06636    99 EFCGAGSVTDLVKNTKGNALK--EDWiayiCREILRGLAHLHAHK--VIHRDIKGQNVLLT-ENAEVKLVDFGVSAQLDR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAK--SVIGTPEFMAPEMY------EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:cd06636   174 TVGRrnTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD-MHPMRALFLIPRNPPPKLKSKKWS 252
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  512 QypEIREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd06636   253 K--KFIDFIEGCLVKNYLSRPSTEQLLKHPF 281
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
287-479 2.72e-20

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 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: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 93.58  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwCELQESKLN-KTERQRFReeaemLKDLQHPNIVRFYDYWESADLCGKRKYIvLVTEL 365
Cdd:cd14054     3 IGQGRYGTVWKGSLDERPVAVK-VFPARHRQNfQNEKDIYE-----LPLMEHSNILRFIGADERPTADGRMEYL-LVLEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLkrfkRINIKVLKSWCR---QILKGLSFLHTR-------NPPVIHRDLKCDNIFItGTTGSVKIGDLGLAT 435
Cdd:cd14054    76 APKGSLCSYL----RENTLDWMSSCRmalSLTRGLAYLHTDlrrgdqyKPAIAHRDLNSRNVLV-KADGSCVICDFGLAM 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  436 L--------------KNKSFAKsvIGTPEFMAPEMYE--------EMYDESVDVYAFGMCLLEMVT 479
Cdd:cd14054   151 VlrgsslvrgrpgaaENASISE--VGTLRYMAPEVLEgavnlrdcESALKQVDVYALGLVLWEIAM 214
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
287-497 2.78e-20

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: 93.06  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCELQeskLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCgKRKYIVLVTE 364
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGekIAIKSCRLE---LSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFL-VNDVPLLAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKrfKRINIKVLK-----SWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSV--KIGDLGLAT-L 436
Cdd:cd14039    77 YCSGGDLRKLLN--KPENCCGLKesqvlSLLSDIGSGIQYLHENK--IIHRDLKPENIVLQEINGKIvhKIIDLGYAKdL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKV 497
Cdd:cd14039   153 DQGSLCTSFVGTLQYLAPELFEnKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWHEKI 214
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
282-476 2.85e-20

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: 92.87  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFD--EELGRGSFKTVFRGLD-TETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQ---HPNIVRFYDYWESADlcgk 355
Cdd:cd14052     1 RFAnvELIGSGEFSQVYKVSErVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHG---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 rkYIVLVTELMTSGTLKMYLKRFKRIniKVLKSWcR------QILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIG 429
Cdd:cd14052    77 --HLYIQTELCENGSLDVFLSELGLL--GRLDEF-RvwkilvELSLGLRFIHDHH--FVHLDLKPANVLIT-FEGTLKIG 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  430 DLGLATLKNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLE 476
Cdd:cd14052   149 DFGMATVWPLIRGIEREGDREYIAPEiLSEHMYDKPADIFSLGLILLE 196
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
279-538 2.93e-20

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: 92.96  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFL-KFDE--ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWE------- 348
Cdd:cd14049     3 RYLnEFEEiaRLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMehvqlml 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 --SADLCGK--RKYIVLVTELMTSGTLKMYLKRFKRINI--KVLkswcRQILKGLSFLHTRNppVIHRDLKCDNIFITGT 422
Cdd:cd14049    83 yiQMQLCELslWDWIVERNKRPCEEEFKSAPYTPVDVDVttKIL----QQLLEGVTYIHSMG--IVHRDLKPRNIFLHGS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  423 TGSVKIGDLGLA-----TLKNKSFAKSVI---------GTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTgeyPYSEC 487
Cdd:cd14049   157 DIHVRIGDFGLAcpdilQDGNDSTTMSRLnglthtsgvGTCLYAAPEQLEgSHYDFKSDMYSIGVILLELFQ---PFGTE 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  488 MNPATIYRKVISGVKPECFSRipaQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14049   234 MERAEVLTQLRNGQIPKSLCK---RWPVQAKYIKLLTSTEPSERPSASQLL 281
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
289-479 4.52e-20

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 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: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 92.78  E-value: 4.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  289 RGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAemlkdLQHPNIVRFYDywesADLCGKRKYIV--LVTELM 366
Cdd:cd14053     5 RGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPG-----MKHENILQFIG----AEKHGESLEAEywLITEFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKrFKRINIKVLKSWCRQILKGLSFLHT--------RNPPVIHRDLKCDNIFITGTTGSVkIGDLGLATL-- 436
Cdd:cd14053    76 ERGSLCDYLK-GNVISWNELCKIAESMARGLAYLHEdipatnggHKPSIAHRDFKSKNVLLKSDLTAC-IADFGLALKfe 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  437 --KNKSFAKSVIGTPEFMAPEMYE---EMYDES---VDVYAFGMCLLEMVT 479
Cdd:cd14053   154 pgKSCGDTHGQVGTRRYMAPEVLEgaiNFTRDAflrIDMYAMGLVLWELLS 204
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
336-517 4.59e-20

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: 93.22  E-value: 4.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  336 QHPNIVRFYDYWESADlcgkrkYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCD 415
Cdd:cd05592    54 QHPFLTHLFCTFQTES------HLFFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRG--IIYRDLKLD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  416 NIFITGTtGSVKIGDLGLATLK--NKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEC----- 487
Cdd:cd05592   126 NVLLDRE-GHIKIADFGMCKENiyGENKASTFCGTPDYIAPEILKgQKYNQSVDWWSFGVLLYEMLIGQSPFHGEdedel 204
                         170       180       190
                  ....*....|....*....|....*....|....
gi 392899979  488 ----MNPATIYRKVISGVKPECFSRIPAQYPEIR 517
Cdd:cd05592   205 fwsiCNDTPHYPRWLTKEAASCLSLLLERNPEKR 238
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
281-542 5.52e-20

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: 91.63  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG-LDTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesadLCGKRKYI 359
Cdd:cd05073    13 LKLEKKLGAGQFGEVWMAtYNKHTKVAV-----KTMKPGSMSVEAFLAEANVMKTLQHDKLVKLH-------AVVTKEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFK--RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL- 436
Cdd:cd05073    81 YIITEFMAKGSLLDFLKSDEgsKQPLPKLIDFSAQIAEGMAFIEQRN--YIHRDLRAANILVSASL-VCKIADFGLARVi 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATIyRKVISGVKpecFSRIPA 511
Cdd:cd05073   158 eDNEYTAREGAKFPiKWTAPEAinFGSFTIKS-DVWSFGILLMEIVTyGRIPYPGMSNPEVI-RALERGYR---MPRPEN 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  512 QYPEIREIIDRCIRVRREERSTVK--QLLVDDF 542
Cdd:cd05073   233 CPEELYNIMMRCWKNRPEERPTFEyiQSVLDDF 265
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
285-543 6.21e-20

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: 92.00  E-value: 6.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcGKRKYIVLvtE 364
Cdd:cd07833     7 GVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRR----KGRLYLVF--E 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA---TLKNKS 440
Cdd:cd07833    81 YVER-TLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHN--IIHRDIKPENILVS-ESGVLKLCDFGFAralTARPAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE--YPYSECMNPATIYRKVISGVKP---ECFSRIP--- 510
Cdd:cd07833   157 PLTDYVATRWYRAPELLvgDTNYGKPVDVWAIGCIMAELLDGEplFPGDSDIDQLYLIQKCLGPLPPshqELFSSNPrfa 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  511 -AQYPEIREIIDR------------------CIRVRREERSTVKQLLVDDFF 543
Cdd:cd07833   237 gVAFPEPSQPESLerrypgkvsspaldflkaCLRMDPKERLTCDELLQHPYF 288
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
285-483 7.61e-20

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: 91.73  E-value: 7.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqesklnkTERQRFREEAE-----------MLKDLQHPNIVRFYDYWESadlc 353
Cdd:cd07839     6 EKIGEGTYGTVFKAKNRETHEIVA-----------LKRVRLDDDDEgvpssalreicLLKELKHKNIVRLYDVLHS---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gkRKYIVLVTELMTSgTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLG 432
Cdd:cd07839    71 --DKKLTLVFEYCDQ-DLKKYFDSCNgDIDPEIVKSFMFQLLKGLAFCHSHN--VLHRDLKPQNLLINK-NGELKLADFG 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  433 LAT---LKNKSFAKSVIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYP 483
Cdd:cd07839   145 LARafgIPVRCYSAEVV-TLWYRPPDvlFGAKLYSTSIDMWSAGCIFAELANAGRP 199
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
318-545 8.07e-20

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: 91.41  E-value: 8.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  318 NKTERQR-FREEAEMLKDLQHPNIVRFYDY-WESADLCgkrkyivLVTELMTSGTLKMYLKRFKrINIKVLKSWCRQILK 395
Cdd:cd14027    30 NCIEHNEaLLEEGKMMNRLRHSRVVKLLGViLEEGKYS-------LVMEYMEKGNLMHVLKKVS-VPLSVKGRIILEIIE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  396 GLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKN---------------KSFAKSVIGTPEFMAPEMYEEM 460
Cdd:cd14027   102 GMAYLHGKG--VIHKDLKPENILVDNDF-HIKIADLGLASFKMwskltkeehneqrevDGTAKKNAGTLYYMAPEHLNDV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  461 YDESV---DVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQl 537
Cdd:cd14027   179 NAKPTeksDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREIIDLMKLCWEANPEARPTFPG- 257

                  ....*...
gi 392899979  538 lVDDFFTP 545
Cdd:cd14027   258 -IEEKFRP 264
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
279-538 8.09e-20

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: 91.09  E-value: 8.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTV----FRGldtETGVAVAWceLQESKLNKTErqrFREEAEMLKDLQHPNIVRFYdywesaDLCG 354
Cdd:cd05113     4 KDLTFLKELGTGQFGVVkygkWRG---QYDVAIKM--IKEGSMSEDE---FIEEAKVMMNLSHEKLVQLY------GVCT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKMYLKRF-KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL 433
Cdd:cd05113    70 KQRPIFIITEYMANGCLLNYLREMrKRFQTQQLLEMCKDVCEAMEYLESKQ--FLHRDLAARNCLVN-DQGVVKVSDFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 ATLKNKSFAKSVIGTP---EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYsECMNPATIYRKVISGVKpecFS 507
Cdd:cd05113   147 SRYVLDDEYTSSVGSKfpvRWSPPEvlMYSKFSSKS-DVWAFGVLMWEVYSlGKMPY-ERFTNSETVEHVSQGLR---LY 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  508 RIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05113   222 RPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
279-480 8.29e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.90  E-value: 8.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLnKTERQRFRE-------------EAEMLKDLQHPNIVRFYD 345
Cdd:PTZ00024    9 RYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEI-SNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  346 YWESADlcgkrkYIVLVTELMtSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGS 425
Cdd:PTZ00024   88 VYVEGD------FINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWY--FMHRDLSPANIFIN-SKGI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  426 VKIGDLGLA-----------TLKNKSFAKSVIGTPE-----FMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:PTZ00024  158 CKIADFGLArrygyppysdtLSKDETMQRREEMTSKvvtlwYRAPEllMGAEKYHFAVDMWSVGCIFAELLTG 230
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
285-582 8.47e-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: 92.09  E-value: 8.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDYWESADLCGKRKYIVLVT 363
Cdd:cd06637    12 ELVGNGTYGQVYKGRHVKTGQLAA---IKVMDVTGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPPGMDDQLWLVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKvlKSW----CRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd06637    89 EFCGAGSVTDLIKNTKGNTLK--EEWiayiCREILRGLSHLHQHK--VIHRDIKGQNVLLT-ENAEVKLVDFGVSAQLDR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAK--SVIGTPEFMAPEMY------EEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:cd06637   164 TVGRrnTFIGTPYWMAPEVIacdenpDATYDFKSDLWSLGITAIEMAEGAPPLCD-MHPMRALFLIPRNPAPRLKSKKWS 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  512 QypEIREIIDRCIRVRREERSTVKQLLVDDFFtpedligirveiknRDADlNDLNVEIQMQLRVYDEKKRK 582
Cdd:cd06637   243 K--KFQSFIESCLVKNHSQRPSTEQLMKHPFI--------------RDQP-NERQVRIQLKDHIDRTKKKR 296
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
286-484 9.75e-20

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: 91.15  E-value: 9.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQ-HPNIVRFYDYWESAdlcgkrKYIVLVTE 364
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETA------SEMILVLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTL--KMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGLA-TLKNK 439
Cdd:cd14197    90 YAAGGEIfnQCVADREEAFKEKDVKRLMKQILEGVSFLHNNN--VVHLDLKPQNILLTSESplGDIKIVDFGLSrILKNS 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  440 SFAKSVIGTPEFMAPEM--YEEMyDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14197   168 EELREIMGTPEYVAPEIlsYEPI-STATDMWSIGVLAYVMLTGISPF 213
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
281-538 1.16e-19

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: 90.78  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVAwcELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYI 359
Cdd:cd05112     6 LTFVQEIGSGQFGLVHLGYwLNKDKVAIK--TIREGAMSEED---FIEEAEVMMKLSHPKLVQLY------GVCLEQAPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATLKN 438
Cdd:cd05112    75 CLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEAS--VIHRDLAARNCLV-GENQVVKVSDFGMTRFVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTP---EFMAPEMYE-EMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISG---VKPECFSRip 510
Cdd:cd05112   152 DDQYTSSTGTKfpvKWSSPEVFSfSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSN-SEVVEDINAGfrlYKPRLAST-- 228
                         250       260
                  ....*....|....*....|....*...
gi 392899979  511 aqypEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05112   229 ----HVYEIMNHCWKERPEDRPSFSLLL 252
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
285-478 1.24e-19

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 91.35  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG-LDTETgVAVAWCELQESKLNKTERQRFReeAEMLKdlqHPNIVRFYDYWESADlcGKRKYIVLVT 363
Cdd:cd13998     1 EVIGKGRFGEVWKAsLKNEP-VAVKIFSSRDKQSWFREKEIYR--TPMLK---HENILQFIAADERDT--ALRTELWLVT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRfkriNIKVLKSWCR---QILKGLSFLHTR-------NPPVIHRDLKCDNIFITgTTGSVKIGDLGL 433
Cdd:cd13998    73 AFHPNGSL*DYLSL----HTIDWVSLCRlalSVARGLAHLHSEipgctqgKPAIAHRDLKSKNILVK-NDGTCCIADFGL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  434 ATLKNKSFAK------SVIGTPEFMAPEMYEE---MYDES----VDVYAFGMCLLEMV 478
Cdd:cd13998   148 AVRLSPSTGEednannGQVGTKRYMAPEVLEGainLRDFEsfkrVDIYAMGLVLWEMA 205
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
281-539 1.31e-19

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: 90.49  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIV 360
Cdd:cd05039     8 LKLGELIGKGEFGDVMLGDYRGQKVAV-----KCLKDDSTAAQAFLAEASVMTTLRHPNLVQL------LGVVLEGNGLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd05039    77 IVTEYMAKGSLVDYLRSRGRavITRKDQLGFALDVCEGMEYLESKK--FVHRDLAARNVLVS-EDNVAKVSDFGLAKEAS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSF--AKSVIgtpEFMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPaqyP 514
Cdd:cd05039   154 SNQdgGKLPI---KWTAPEALREkKFSTKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPHVEKGYRMEAPEGCP---P 226
                         250       260
                  ....*....|....*....|....*
gi 392899979  515 EIREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd05039   227 EVYKVMKNCWELDPAKRPTFKQLRE 251
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
281-544 1.43e-19

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: 90.90  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesadLCGKRKYI 359
Cdd:cd05070    11 LQLIKRLGNGQFGEVWMGTwNGNTKVAI-----KTLKPGTMSPESFLEEAQIMKKLKHDKLVQLY-------AVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL- 436
Cdd:cd05070    79 YIVTEYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMN--YIHRDLRSANILV-GNGLICKIADFGLARLi 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPA 511
Cdd:cd05070   156 eDNEYTARQGAKFPiKWTAPEaaLYGRFTIKS-DVWSFGILLTELVTkGRVPYPG-MNNREVLEQVERGYRMPCPQDCPI 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  512 QypeIREIIDRCIRVRREERSTVKQL--LVDDFFT 544
Cdd:cd05070   234 S---LHELMIHCWKKDPEERPTFEYLqgFLEDYFT 265
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
282-500 1.47e-19

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: 90.51  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAwCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVL 361
Cdd:cd14083     6 EFKEVLGTGAFSEVVLAEDKATGKLVA-IKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYES------KSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLkmylkrFKRInikVLKS---------WCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKI--GD 430
Cdd:cd14083    79 VMELVTGGEL------FDRI---VEKGsytekdashLIRQVLEAVDYLHSLG--IVHRDLKPENLLYYSPDEDSKImiSD 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  431 LGLATLKNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYP--YSEcmNPATIYRKVISG 500
Cdd:cd14083   148 FGLSKMEDSGVMSTACGTPGYVAPEVLAQKpYGKAVDCWSIGVISYILLCG-YPpfYDE--NDSKLFAQILKA 217
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
281-540 1.50e-19

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 91.62  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETG----VAVAWCELQESKLNKTERQRFrEEAEMLKDLQHPNIVRFYDywesadLCgKR 356
Cdd:cd05108     9 FKKIKVLGSGAFGTVYKGLWIPEGekvkIPVAIKELREATSPKANKEIL-DEAYVMASVDNPHVCRLLG------IC-LT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT 435
Cdd:cd05108    81 STVQLITQLMPFGCLLDYVREHKdNIGSQYLLNWCVQIAKGMNYLEDRR--LVHRDLAARNVLVKTPQ-HVKITDFGLAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 L---KNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECmnPATIYRKVISgvKPECFSRI 509
Cdd:cd05108   158 LlgaEEKEYHAEGGKVPiKWMALEsILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGI--PASEISSILE--KGERLPQP 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  510 PAQYPEIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:cd05108   234 PICTIDVYMIMVKCWMIDADSRPKFRELIIE 264
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
287-478 1.52e-19

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: 90.40  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELqeSKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTELM 366
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKEL--IRFDEETQRTFLKEVKVMRCLEHPNVLKF------IGVLYKDKRLNFITEYI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRF-------KRInikvlkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL--- 436
Cdd:cd14221    73 KGGTLRGIIKSMdshypwsQRV------SFAKDIASGMAYLHSMN--IIHRDLNSHNCLVR-ENKSVVVADFGLARLmvd 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  437 -------------KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMV 478
Cdd:cd14221   144 ektqpeglrslkkPDRKKRYTVVGNPYWMAPEMINgRSYDEKVDVFSFGIVLCEII 199
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
287-484 1.53e-19

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: 90.45  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLD-TETGVAVAWCELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd14201    14 VGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQ-ILLGKEIKILKELQHENIVALYDVQEMPN------SVFLVMEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT-------GTTG-SVKIGDLGLAT-L 436
Cdd:cd14201    87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKG--IIHRDLKPQNILLSyasrkksSVSGiRIKIADFGFARyL 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14201   165 QSNMMAATLCGSPMYMAPEvIMSQHYDAKADLWSIGTVIYQCLVGKPPF 213
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
285-479 1.70e-19

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: 90.64  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNkTERQ-----RFREEAeMLKDLQHPNIVRFYDYWESadlcgkRKYI 359
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVA---LKKIRLD-TETEgvpstAIREIS-LLKELNHPNIVKLLDVIHT------ENKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMtSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-- 435
Cdd:cd07860    75 YLVFEFL-HQDLKKFMDasALTGIPLPLIKSYLFQLLQGLAFCHSHR--VLHRDLKPQNLLIN-TEGAIKLADFGLARaf 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  436 -LKNKSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07860   151 gVPVRTYTHEVV-TLWYRAPEILlgCKYYSTAVDIWSLGCIFAEMVT 196
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
328-557 1.79e-19

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: 90.35  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  328 EAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppV 407
Cdd:cd05579    43 ERNILSQAQNPFVVKLYYSFQG------KKNLYLVMEYLPGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHG--I 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  408 IHRDLKCDNIFITGtTGSVKIGDLGLATL------KNKSFA-----------KSVIGTPEFMAPEMYEEM-YDESVDVYA 469
Cdd:cd05579   115 IHRDLKPDNILIDA-NGHLKLTDFGLSKVglvrrqIKLSIQkksngapekedRRIVGTPDYLAPEILLGQgHGKTVDWWS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  470 FGMCLLEMVTGEYPYSEcMNPATIYRKVISGvkpecfsRIPaqYPEIREIIDRCIrvrreerSTVKQLLVDDfftPEDLI 549
Cdd:cd05579   194 LGVILYEFLVGIPPFHA-ETPEEIFQNILNG-------KIE--WPEDPEVSDEAK-------DLISKLLTPD---PEKRL 253
                         250
                  ....*....|
gi 392899979  550 GIR--VEIKN 557
Cdd:cd05579   254 GAKgiEEIKN 263
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
285-483 2.10e-19

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: 91.07  E-value: 2.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERqRFRE----EAEMLKDLQH------PNIVRFYDYWESadlcg 354
Cdd:cd14210    19 SVLGKGSFGQVVKCLDHKTGQLVA------IKIIRNKK-RFHQqalvEVKILKHLNDndpddkHNIVRYKDSFIF----- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 kRKYIVLVTELMtSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI-FITGTTGSVKIGDL 431
Cdd:cd14210    87 -RGHLCIVFELL-SINLYELLKsnNFQGLSLSLIRKFAKQILQALQFLHKLN--IIHCDLKPENIlLKQPSKSSIKVIDF 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392899979  432 GLATLKN-KSFakSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGeYP 483
Cdd:cd14210   163 GSSCFEGeKVY--TYIQSRFYRAPEvILGLPYDTAIDMWSLGCILAELYTG-YP 213
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
287-541 2.19e-19

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: 89.69  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTELM 366
Cdd:cd14095     8 IGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDT------ELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLkmylkrFKRINIKV------LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI----TGTTgSVKIGDLGLAT- 435
Cdd:cd14095    81 KGGDL------FDAITSSTkfterdASRMVTDLAQALKYLHSLS--IVHRDIKPENLLVveheDGSK-SLKLADFGLATe 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFakSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY-SECMNPATIYRKVISGVkpecFSRIPAQY 513
Cdd:cd14095   152 VKEPLF--TVCGTPTYVAPEILAETgYGLKVDIWAAGVITYILLCGFPPFrSPDRDQEELFDLILAGE----FEFLSPYW 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  514 PEI----REIIDRCIRVRREERSTVKQLLVDD 541
Cdd:cd14095   226 DNIsdsaKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
287-540 2.38e-19

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: 90.63  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNkTERQRFR----EEAEMLKDLQHPNIVRFY----DYWESADLCGKRKY 358
Cdd:cd07864    15 IGEGTYGQVYKAKDKDTGELVA---LKKVRLD-NEKEGFPitaiREIKILRQLNHRSVVNLKeivtDKQDALDFKKDKGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTS---GTLKMYLKRFKRINIKvlkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT 435
Cdd:cd07864    91 FYLVFEYMDHdlmGLLESGLVHFSEDHIK---SFMKQLLEGLNYCHKKN--FLHRDIKCSNILLN-NKGQIKLADFGLAR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKS----FAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEYPYSEcmNPATIYRKVISGVkpeCFSRI 509
Cdd:cd07864   165 LYNSEesrpYTNKVI-TLWYRPPELLlgEERYGPAIDVWSCGCILGELFTKKPIFQA--NQELAQLELISRL---CGSPC 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  510 PAQYPEIREII-------DRCIRVR-REERSTVKQLLVD 540
Cdd:cd07864   239 PAVWPDVIKLPyfntmkpKKQYRRRlREEFSFIPTPALD 277
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
285-486 2.44e-19

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: 90.57  E-value: 2.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTE-TGVAVAW-----CELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKY 358
Cdd:cd14096     7 NKIGEGAFSNVYKAVPLRnTGKPVAIkvvrkADLSSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQES------DEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI--------------------- 417
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIG--VVHRDIKPENLlfepipfipsivklrkaddde 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 -------FI----TGTTGSVKIGDLGLATLKNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:cd14096   159 tkvdegeFIpgvgGGGIGIVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVVkDERYSKKVDMWALGCVLYTLLCGFPPFY 238

                  .
gi 392899979  486 E 486
Cdd:cd14096   239 D 239
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
285-538 2.45e-19

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: 89.75  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd14078     9 ETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGD-DLPRVKTEIEALKNLSHQHICRLYHVIETDN------KIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATlKNKSFAKS 444
Cdd:cd14078    82 YCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQG--YAHRDLKPENLLLD-EDQNLKLIDFGLCA-KPKGGMDH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VI----GTPEFMAPEMYE--EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGV--KPECFSripaqyPEI 516
Cdd:cd14078   158 HLetccGSPAYAAPELIQgkPYIGSEADVWSMGVLLYALLCGFLPFDD-DNVMALYRKIQSGKyeEPEWLS------PSS 230
                         250       260
                  ....*....|....*....|..
gi 392899979  517 REIIDRCIRVRREERSTVKQLL 538
Cdd:cd14078   231 KLLLDQMLQVDPKKRITVKELL 252
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
285-542 2.54e-19

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: 89.97  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGV-AVAWCELQESklNKTERQRFREEAEMLKDLQH-PNIVRFYDYwesaDLCGKRKYIVLV 362
Cdd:cd14131     7 KQLGKGGSSKVYKVLNPKKKIyALKRVDLEGA--DEQTLQSYKNEIELLKKLKGsDRIIQLYDY----EVTDEDDYLYMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELmTSGTLKMYL--KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGttGSVKIGDLGLAtlknKS 440
Cdd:cd14131    81 MEC-GEIDLATILkkKRPKPIDPNFIRYYWKQMLEAVHTIHEEG--IVHSDLKPANFLLVK--GRLKLIDFGIA----KA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAK--------SVIGTPEFMAPE-MYEEMYDESV----------DVYAFGMCLLEMVTGEYPYSECMNPatiYRKV--IS 499
Cdd:cd14131   152 IQNdttsivrdSQVGTLNYMSPEaIKDTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQHITNP---IAKLqaII 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  500 GVKPEcfsrIPaqYPEIR-----EIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:cd14131   229 DPNHE----IE--FPDIPnpdliDVMKRCLQRDPKKRPSIPELLNHPF 270
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
279-495 2.75e-19

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: 90.34  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTV----FRGLDTETGVAVAWCELQESKLNktERQRFREEAEMLKDLQHPNIVRFYDYWESADlcg 354
Cdd:cd05081     4 RHLKYISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPD--QQRDFQREIQILKALHSDFIVKYRGVSYGPG--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 kRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGL 433
Cdd:cd05081    79 -RRSLRLVMEYLPSGCLRDFLQRHRaRLDASRLLLYSSQICKGMEYLGSRR--CVHRDLAARNILVESEA-HVKIADFGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  434 ATL----KNKSFAKSVIGTPEF-MAPE-MYEEMYDESVDVYAFGMCLLEMVTgeYPYSECMNPATIYR 495
Cdd:cd05081   155 AKLlpldKDYYVVREPGQSPIFwYAPEsLSDNIFSRQSDVWSFGVVLYELFT--YCDKSCSPSAEFLR 220
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
285-581 2.98e-19

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: 90.29  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKT---ERQRFREEAEMLKDLQHPNIVRF-------------YDYWE 348
Cdd:cd14094     9 EVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELletyssdgmlymvFEFMD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 SADLCGKrkyivlVTELMTSGTLkmylkrfkrINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS--V 426
Cdd:cd14094    89 GADLCFE------IVKRADAGFV---------YSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  427 KIGDLGLATL--KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYseCMNPATIYRKVISG--- 500
Cdd:cd14094   152 KLGGFGVAIQlgESGLVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGkyk 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  501 VKPECFSRIPAQypeIREIIDRCIRVRREERSTVKQLLVDDFftpedligirveIKNRDADLNDLNV-EIQMQLRVYDEK 579
Cdd:cd14094   230 MNPRQWSHISES---AKDLVRRMLMLDPAERITVYEALNHPW------------IKERDRYAYRIHLpETVEQLRKFNAR 294

                  ..
gi 392899979  580 KR 581
Cdd:cd14094   295 RK 296
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
285-543 3.33e-19

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: 89.18  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAvawCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd14107     8 EEIGRGTFGFVKRVTHKGNGEC---CAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFET------RKTLILILE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIF-ITGTTGSVKIGDLGLA---TLKNKS 440
Cdd:cd14107    79 LCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMN--ILHLDIKPDNILmVSPTREDIKICDFGFAqeiTPSEHQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKsvIGTPEFMAPEM-YEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPAT---IYRKVISGVKPECFSRipaqYPEI 516
Cdd:cd14107   157 FSK--YGSPEFVAPEIvHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATllnVAEGVVSWDTPEITHL----SEDA 230
                         250       260
                  ....*....|....*....|....*..
gi 392899979  517 REIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14107   231 KDFIKRVLQPDPEKRPSASECLSHEWF 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
281-500 4.01e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 90.65  E-value: 4.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYI 359
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQvQHVAQEKSILMELSHPFIVNMMCSFQDEN----RVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLAT-LKN 438
Cdd:PTZ00263   96 LL--EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKD--IIYRDLKPENLLLDNK-GHVKVTDFGFAKkVPD 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  439 KSFakSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG 500
Cdd:PTZ00263  171 RTF--TLCGTPEYLAPEVIQSKgHGKAVDWWTMGVLLYEFIAGYPPFFD-DTPFRIYEKILAG 230
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
280-484 4.03e-19

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: 89.94  E-value: 4.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFdEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKteRQRFRE---EAEMLKDLQHPNIVRF-YDYWESADLCgk 355
Cdd:cd05608     3 FLDF-RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKK--RKGYEGamvEKRILAKVHSRFIVSLaYAFQTKTDLC-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 rkyivLVTELMTSGTLKMYLKRFKRINIKVLKS----WCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDL 431
Cdd:cd05608    78 -----LVMTIMNGGDLRYHIYNVDEENPGFQEPracfYTAQIISGLEHLHQRR--IIYRDLKPENVLLD-DDGNVRISDL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  432 GLAT-LKN-KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05608   150 GLAVeLKDgQTKTKGYAGTPGFMAPELLLgEEYDYSVDYFTLGVTLYEMIAARGPF 205
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
287-539 4.29e-19

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 89.45  E-value: 4.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGL-------DTETGVAVAwcELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYI 359
Cdd:cd05046    13 LGRGEFGEVFLAKakgieeeGGETLVLVK--ALQKTKDENLQ-SEFRRELDMFRKLSHKNVVRLL------GLCREAEPH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKR---------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGD 430
Cdd:cd05046    84 YMILEYTDLGDLKQFLRATKSkdeklkpppLSTKQKVALCTQIALGMDHLSNAR--FVHRDLAARNCLVS-SQREVKVSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLATLKNKS---FAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpatiyRKVISGVKPEC 505
Cdd:cd05046   161 LSLSKDVYNSeyyKLRNALIPLRWLAPEaVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSD-----EEVLNRLQAGK 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  506 FS-RIPAQYPE-IREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd05046   236 LElPVPEGCPSrLYKLMTRCWAVNPKDRPSFSELVS 271
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
285-477 4.31e-19

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: 89.64  E-value: 4.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTER----QRFREEAeMLKDLQ---HPNIVRFYDYWESADLCGKRK 357
Cdd:cd07838     5 AEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEgiplSTIREIA-LLKQLEsfeHPNVVRLLDVCHGPRTDRELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 yIVLVTELMTSgTLKMYLKRF--KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA- 434
Cdd:cd07838    81 -LTLVFEHVDQ-DLATYLDKCpkPGLPPETIKDLMRQLLRGLDFLHSHR--IVHRDLKPQNILVT-SDGQVKLADFGLAr 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392899979  435 TLKNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEM 477
Cdd:cd07838   156 IYSFEMALTSVVVTLWYRAPEvLLQSSYATPVDMWSVGCIFAEL 199
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
283-538 4.54e-19

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: 89.04  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAwCELQE--SKLNKTERQRFREEAEMLKD------------LQHPNIVRFYDYwe 348
Cdd:cd14077     5 FVKTIGAGSMGKVKLAKHIRTGEKCA-IKIIPraSNAGLKKEREKRLEKEISRDirtireaalsslLNHPHICRLRDF-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 sadlCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKI 428
Cdd:cd14077    82 ----LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNS--IVHRDLKIENILIS-KSGNIKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLATL-KNKSFAKSVIGTPEFMAPEMYE-EMY-DESVDVYAFGMCLLEMVTGEYPYSECMNPAtIYRKVISGV--KP 503
Cdd:cd14077   155 IDFGLSNLyDPRRLLRTFCGSLYFAAPELLQaQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPA-LHAKIKKGKveYP 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  504 ECFSRipaqypEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14077   234 SYLSS------ECKSLISRMLVVDPKKRATLEQVL 262
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
287-484 4.68e-19

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: 90.35  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDTETGVAVawcelqesKLNKTERQRFREEAE--------MLKDLQHPNIVRFYDYWESADlcgkr 356
Cdd:cd05570     3 LGKGSFGKVMlaERKKTDELYAI--------KVLKKEVIIEDDDVEctmtekrvLALANRHPFLTGLHACFQTED----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLAT- 435
Cdd:cd05570    70 -RLYFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERG--IIYRDLKLDNVLLDAE-GHIKIADFGMCKe 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  436 -LKNKSFAKSVIGTPEFMAPEM-YEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05570   146 gIWGGNTTSTFCGTPDYIAPEIlREQDYGFSVDWWALGVLLYEMLAGQSPF 196
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
287-538 5.70e-19

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: 88.74  E-value: 5.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRgldTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLvtELM 366
Cdd:cd14087     9 IGRGSFSRVVR---VEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKE----RVYMVM--ELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLkmylkrFKRINIK----------VLKswcrQILKGLSFLHTRNppVIHRDLKCDNIFI--TGTTGSVKIGDLGLA 434
Cdd:cd14087    80 TGGEL------FDRIIAKgsfterdatrVLQ----MVLDGVKYLHGLG--ITHRDLKPENLLYyhPGPDSKIMITDFGLA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLKNKS---FAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVkpecFSRIP 510
Cdd:cd14087   148 STRKKGpncLMKTTCGTPEYIAPEiLLRKPYTQSVDMWAVGVIAYILLSGTMPFDD-DNRTRLYRQILRAK----YSYSG 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  511 AQYPEI----REIIDRCIRVRREERSTVKQLL 538
Cdd:cd14087   223 EPWPSVsnlaKDFIDRLLTVNPGERLSATQAL 254
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
285-538 5.87e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 94.03  E-value: 5.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWesADLCGKRKYIVLvtE 364
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRF--LNKANQKLYILM--E 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTL-----KMYlKRFKRINIKVLKSWCRQILKGLSFLHT-RNPP----VIHRDLKCDNIF----------ITGTTG 424
Cdd:PTZ00266   95 FCDAGDLsrniqKCY-KMFGKIEEHAIVDITRQLLHALAYCHNlKDGPngerVLHRDLKPQNIFlstgirhigkITAQAN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  425 SV------KIGDLGLAtlKN---KSFAKSVIGTPEFMAPEMY---EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNpat 492
Cdd:PTZ00266  174 NLngrpiaKIGDFGLS--KNigiESMAHSCVGTPYYWSPELLlheTKSYDDKSDMWALGCIIYELCSGKTPFHKANN--- 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 392899979  493 iYRKVISGVKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:PTZ00266  249 -FSQLISELKRGPDLPIKGKSKELNILIKNLLNLSAKERPSALQCL 293
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
286-537 6.38e-19

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: 88.05  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesADLCGKRKYIvlVTE 364
Cdd:cd14203     2 KLGQGCFGEVWMGTwNGTTKVAI-----KTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLY-----AVVSEEPIYI--VTE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKV--LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL--KNKS 440
Cdd:cd14203    70 FMSKGSLLDFLKDGEGKYLKLpqLVDMAAQIASGMAYIERMN--YIHRDLRAANILV-GDNLVCKIADFGLARLieDNEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPaqyPEI 516
Cdd:cd14203   147 TARQGAKFPiKWTAPEaaLYGRFTIKS-DVWSFGILLTELVTkGRVPYPG-MNNREVLEQVERGYRMPCPPGCP---ESL 221
                         250       260
                  ....*....|....*....|.
gi 392899979  517 REIIDRCIRVRREERSTVKQL 537
Cdd:cd14203   222 HELMCQCWRKDPEERPTFEYL 242
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
286-543 8.11e-19

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: 88.06  E-value: 8.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER----QRFREEAEMLK---DLQHPNIVRFYDYWESADlcgkrkY 358
Cdd:cd14005     7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMingpVPVPLEIALLLkasKPGVPGVIRLLDWYERPD------G 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSG-TLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLATLK 437
Cdd:cd14005    81 FLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRG--VLHRDIKDENLLINLRTGEVKLIDFGCGALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPY---SECMNPATIYRKVISgvkPECfsripaq 512
Cdd:cd14005   159 KDSVYTDFDGTRVYSPPEwiRHGRYHGRPATVWSLGILLYDMLCGDIPFendEQILRGNVLFRPRLS---KEC------- 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 392899979  513 ypeiREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14005   229 ----CDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
287-500 8.51e-19

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: 89.03  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGvavAWCELQesKLNKTERQRFRE------EAEMLKDLQHPNIVRFydYWESADlcgkRKYIV 360
Cdd:cd05612     9 IGTGTFGRVHLVRDRISE---HYYALK--VMAIPEVIRLKQeqhvhnEKRVLKEVSHPFIIRL--FWTEHD----QRFLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNK 439
Cdd:cd05612    78 MLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKE--IVYRDLKPENILLD-KEGHIKLTDFGFAKkLRDR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  440 SFakSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG 500
Cdd:cd05612   155 TW--TLCGTPEYLAPEVIQSKgHNKAVDWWALGILIYEMLVGYPPFFD-DNPFGIYEKILAG 213
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
287-538 1.30e-18

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: 87.86  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDT--------ETGVAVAwcELQESKLNKtERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrKY 358
Cdd:cd05044     3 LGSGAFGEVFEGTAKdilgdgsgETKVAVK--TLRKGATDQ-EKAEFLKEAHLMSNFKHPNILKLLGVCLDNDP----QY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLvtELMTSGTLKMYLKRFK-------RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS---VKI 428
Cdd:cd05044    76 IIL--ELMEGGDLLSYLRAARptaftppLLTLKDLLSICVDVAKGCVYLEDMH--FVHRDLAARNCLVSSKDYRervVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLA--TLKNKSFAKSVIGT-P-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYsecmnPATIYRKVISGVK 502
Cdd:cd05044   152 GDFGLArdIYKNDYYRKEGEGLlPvRWMAPEsLVDGVFTTQSDVWAFGVLMWEILTlGQQPY-----PARNNLEVLHFVR 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 392899979  503 PE-CFSRiPAQYPE-IREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05044   227 AGgRLDQ-PDNCPDdLYELMLRCWSTDPEERPSFARIL 263
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
287-543 1.32e-18

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: 89.65  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd05573     9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDmLKREQIAHVRAERDILADADSPWIVRLHYAFQDED------HLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKS----- 440
Cdd:cd05573    83 MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLH--KLGFIHRDIKPDNILLD-ADGHIKLADFGLCTKMNKSgdres 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 --------------------------FAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYP-YSEcmNPAT 492
Cdd:cd05573   160 ylndsvntlfqdnvlarrrphkqrrvRAYSAVGTPDYIAPEVLRGTgYGPECDWWSLGVILYEMLYGFPPfYSD--SLVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  493 IYRKVISGVKPECFSRIPAQYPEIREIIDRCIRvRREER-STVKQLLVDDFF 543
Cdd:cd05573   238 TYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLC-DPEDRlGSAEEIKAHPFF 288
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
281-544 1.36e-18

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: 88.20  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesadLCGKRKYI 359
Cdd:cd05069    14 LRLDVKLGQGCFGEVWMGTwNGTTKVAI-----KTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLY-------AVVSEEPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKR--FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL- 436
Cdd:cd05069    82 YIVTEFMGKGSLLDFLKEgdGKYLKLPQLVDMAAQIADGMAYIERMN--YIHRDLRAANILV-GDNLVCKIADFGLARLi 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYsecmnPATIYRKVISGVKPECFSRIPA 511
Cdd:cd05069   159 eDNEYTARQGAKFPiKWTAPEaaLYGRFTIKS-DVWSFGILLTELVTkGRVPY-----PGMVNREVLEQVERGYRMPCPQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  512 QYPE-IREIIDRCIRVRREERSTVK--QLLVDDFFT 544
Cdd:cd05069   233 GCPEsLHELMKLCWKKDPDERPTFEyiQSFLEDYFT 268
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
285-481 1.43e-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: 88.20  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgKRKyIVLVTE 364
Cdd:cd07847     7 SKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRR-----KRK-LHLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGlatlknksFAKS 444
Cdd:cd07847    81 YCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHN--CIHRDVKPENILIT-KQGQIKLCDFG--------FARI 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  445 VIGTPE----------FMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07847   150 LTGPGDdytdyvatrwYRAPELLvgDTQYGPPVDVWAIGCVFAELLTGQ 198
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
285-497 1.57e-18

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-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: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 87.40  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL-DTETG----VAVAwCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyi 359
Cdd:cd05040     1 EKLGDGSFGVVRRGEwTTPSGkviqVAVK-CLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPL------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL--ATL 436
Cdd:cd05040    73 MMVTELAPLGSLLDRLRKDQgHFLISTLCDYAVQIANGMAYLESKR--FIHRDLAARNILLA-SKDKVKIGDFGLmrALP 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNK-----SFAKSVigtP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECmNPATIYRKV 497
Cdd:cd05040   150 QNEdhyvmQEHRKV---PfAWCAPEsLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGL-NGSQILEKI 214
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
281-484 1.57e-18

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: 88.01  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKT-ERQR-FREEAEMLKDLQHPNIVRFYdyweSADLCGKRky 358
Cdd:cd06619     3 IQYQEILGHGNGGTVYKAYHLLTRRILA---VKVIPLDITvELQKqIMSELEILYKCDSPYIIGFY----GAFFVENR-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYlkrfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd06619    74 ISICTEFMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLK--ILHRDVKPSNMLVN-TRGQVKLCDFGVSTQLV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  439 KSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd06619   147 NSIAKTYVGTNAYMAPErISGEQYGIHSDVWSLGISFMELALGRFPY 193
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
284-537 1.70e-18

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: 87.48  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGL-----DTETGVAVAWCElqeSKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkY 358
Cdd:cd05056    11 GRCIGEGQFGDVYQGVymspeNEKIAVAVKTCK---NCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPV-----W 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLvtELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT-L 436
Cdd:cd05056    83 IVM--ELAPLGELRSYLQVNKySLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSSPD-CVKLGDFGLSRyM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGT-P-EFMAPEMYE-EMYDESVDVYAFGMCLLE-MVTGEYPYSECMNpatiyRKVIS----GVKPECFSR 508
Cdd:cd05056   158 EDESYYKASKGKlPiKWMAPESINfRRFTSASDVWMFGVCMWEiLMLGVKPFQGVKN-----NDVIGrienGERLPMPPN 232
                         250       260
                  ....*....|....*....|....*....
gi 392899979  509 IPaqyPEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05056   233 CP---PTLYSLMTKCWAYDPSKRPRFTEL 258
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
281-544 1.82e-18

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: 87.81  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKlNKTERQRFREEAE-MLKDLQHPNIVRFYDYWesadlcgKRKYI 359
Cdd:cd06618    17 LENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSG-NKEENKRILMDLDvVLKSHDCPYIVKCYGYF-------ITDSD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLV-TELMTSGTLKMyLKRFKR-INIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLATLK 437
Cdd:cd06618    89 VFIcMELMSTCLDKL-LKRIQGpIPEDILGKMTVSIVKALHYLKEKHG-VIHRDVKPSNILLD-ESGNVKLCDFGISGRL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKS-VIGTPEFMAPEMYE----EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKP-----ECFS 507
Cdd:cd06618   166 VDSKAKTrSAGCAAYMAPERIDppdnPKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPslppnEGFS 245
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  508 ripaqyPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd06618   246 ------PDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
285-485 1.94e-18

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: 87.69  E-value: 1.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKterqrfREEAE-MLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVT 363
Cdd:cd14091     6 EEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDP------SEEIEiLLRYGQHPNIITLRDVYDDG------NSVYLVT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTL--KMYLKRF--KRINIKVLKSwcrqILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIGDLGlatl 436
Cdd:cd14091    74 ELLRGGELldRILRQKFfsEREASAVMKT----LTKTVEYLHSQG--VVHRDLKPSNILYadeSGDPESLRICDFG---- 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 knksFAKS------VIGTP----EFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:cd14091   144 ----FAKQlraengLLMTPcytaNFVAPEVLKKQgYDAACDIWSLGVLLYTMLAGYTPFA 199
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
281-544 2.73e-18

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing 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 with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src 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: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 87.05  E-value: 2.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGL-DTETGVAVawcelQESKLNKTERQRFREEAEMLKDLQHPNIVRFYdywesadLCGKRKYI 359
Cdd:cd05071    11 LRLEVKLGQGCFGEVWMGTwNGTTRVAI-----KTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY-------AVVSEEPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL- 436
Cdd:cd05071    79 YIVTEYMSKGSLLDFLKgeMGKYLRLPQLVDMAAQIASGMAYVERMN--YVHRDLRAANILV-GENLVCKVADFGLARLi 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 -KNKSFAKSVIGTP-EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYsecmnPATIYRKVISGVKPECFSRIPA 511
Cdd:cd05071   156 eDNEYTARQGAKFPiKWTAPEaaLYGRFTIKS-DVWSFGILLTELTTkGRVPY-----PGMVNREVLDQVERGYRMPCPP 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  512 QYPE-IREIIDRCIRVRREERSTVK--QLLVDDFFT 544
Cdd:cd05071   230 ECPEsLHDLMCQCWRKEPEERPTFEylQAFLEDYFT 265
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
287-478 2.83e-18

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: 86.38  E-value: 2.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNkTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIVLVTELM 366
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMA---LKMNTLS-SNRANMLREVQLMNRLSHPNILRFMG------VCVHQGQLHALTEYI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVK--IGDLGLA----TLKNKS 440
Cdd:cd14155    71 NGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKG--IFHRDLTSKNCLIKRDENGYTavVGDFGLAekipDYSDGK 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392899979  441 FAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMV 478
Cdd:cd14155   149 EKLAVVGSPYWMAPEVLRgEPYNEKADVFSYGIILCEII 187
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
285-479 2.99e-18

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: 86.96  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTerqRFREEAE-----------MLKDLQHPNIVRFYDYWESadlc 353
Cdd:cd07835     5 EKIGEGTYGVVYKARDKLTGEIVA--------LKKI---RLETEDEgvpstaireisLLKELNHPNIVRLLDVVHS---- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYivLVTELMTSgTLKMYLKRFKRINI--KVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDL 431
Cdd:cd07835    70 ENKLY--LVFEFLDL-DLKKYMDSSPLTGLdpPLIKSYLYQLLQGIAFCHSHR--VLHRDLKPQNLLID-TEGALKLADF 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  432 GLA---TLKNKSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07835   144 GLArafGVPVRTYTHEVV-TLWYRAPEILlgSKHYSTPVDIWSVGCIFAEMVT 195
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
286-548 3.30e-18

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: 87.80  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd06650    12 ELGAGNGGVVFKVSHKPSGLVMAR-KLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDG------EISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKSV 445
Cdd:cd06650    85 MDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHK-IMHRDVKPSNILVN-SRGEIKLCDFGVSGQLIDSMANSF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  446 IGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYP---------------------YSECMNPATIYRKVIS---G 500
Cdd:cd06650   163 VGTRSYMSPERLQgTHYSVQSDIWSMGLSLVEMAVGRYPipppdakelelmfgcqvegdaAETPPRPRTPGRPLSSygmD 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  501 VKP-----ECFSRI----PAQYP------EIREIIDRCIRVRREERSTVKQLLVDDFFTPEDL 548
Cdd:cd06650   243 SRPpmaifELLDYIvnepPPKLPsgvfslEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDA 305
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
285-531 3.37e-18

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: 86.38  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKL---NKTERQRFrEEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVL 361
Cdd:cd05611     2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMiakNQVTNVKA-ERAIMMIQGESPYVAKLYYSFQSKD------YLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL--ATLKNK 439
Cdd:cd05611    75 VMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRG--IIHRDIKPENLLID-QTGHLKLTDFGLsrNGLEKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SfAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYPYSECMNPATIYRKVISGVKPECFSRIPAQYPEIRE 518
Cdd:cd05611   152 H-NKKFVGTPDYLAPETILGVgDDKMSDWWSLGCVIFEFLFG-YPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVD 229
                         250
                  ....*....|...
gi 392899979  519 IIDRCIRVRREER 531
Cdd:cd05611   230 LINRLLCMDPAKR 242
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
280-480 3.99e-18

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: 86.99  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEeLGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYdywesaDLCGKRK 357
Cdd:cd07871     7 YVKLDK-LGEGTYATVFKGRSKLTENLVA---LKEIRLEHEEGAPCTaiREVSLLKNLKHANIVTLH------DIIHTER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSgTLKMYLKRFKRI----NIKVlksWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGL 433
Cdd:cd07871    77 CLTLVFEYLDS-DLKQYLDNCGNLmsmhNVKI---FMFQLLRGLSYCHKRK--ILHRDLKPQNLLIN-EKGELKLADFGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  434 ATLKN---KSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07871   150 ARAKSvptKTYSNEVV-TLWYRPPDVLlgSTEYSTPIDMWGVGCILYEMATG 200
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
283-484 3.99e-18

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: 86.45  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYivLV 362
Cdd:cd14097     5 FGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETP----KRMY--LV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG------SVKIGDLGLATL 436
Cdd:cd14097    79 MELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKND--IVHRDLKLENILVKSSIIdnndklNIKVTDFGLSVQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  437 K---NKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14097   157 KyglGEDMLQETCGTPIYMAPEvISAHGYSQQCDIWSIGVIMYMLLCGEPPF 208
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
281-522 4.28e-18

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: 86.75  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG-----LDTETGVAVAWCELQESKLNKTeRQRFREEAEMLKDLQHPNIVRFYdywesaDLCGK 355
Cdd:cd05049     7 IVLKRELGEGAFGKVFLGecynlEPEQDKMLVAVKTLKDASSPDA-RKDFEREAELLTNLQHENIVKFY------GVCTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRF--------------KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItG 421
Cdd:cd05049    80 GDPLLMVFEYMEHGDLNKFLRSHgpdaaflasedsapGELTLSQLLHIAVQIASGMVYLASQH--FVHRDLATRNCLV-G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  422 TTGSVKIGDLGLATLKNKSFAKSVIGTP----EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMN----- 489
Cdd:cd05049   157 TNLVVKIGDFGMSRDIYSTDYYRVGGHTmlpiRWMPPEsiLYRKFTTES-DVWSFGVVLWEIFTyGKQPWFQLSNtevie 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  490 --------------PATIYRkVISGvkpeCFSRIPAQYPEIREIIDR 522
Cdd:cd05049   236 citqgrllqrprtcPSEVYA-VMLG----CWKREPQQRLNIKDIHKR 277
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
280-484 5.57e-18

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: 85.72  E-value: 5.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAwCELQESKLNKteRQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYI 359
Cdd:cd14108     3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFA-AKFIPVRAKK--KTSARRELALLAELDHKSIVRFHDAFE------KRRVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINIKVlKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT-GTTGSVKIGDLGLA-TLK 437
Cdd:cd14108    74 IIVTELCHEELLERITKRPTVCESEV-RSYMRQLLEGIEYLHQND--VLHLDLKPENLLMAdQKTDQVRICDFGNAqELT 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  438 NKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14108   151 PNEPQYCKYGTPEFVAPEIVNQSpVSKVTDIWPVGVIAYLCLTGISPF 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
284-543 5.84e-18

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: 85.79  E-value: 5.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKT-VFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEmlkdlqHPNIVRFYDYWESADLCgkrkYIVLv 362
Cdd:cd13982     6 PKVLGYGSEGTiVFRGTFDGRPVAVKRLLPEFFDFADREVQLLRESDE------HPNVIRYFCTEKDRQFL----YIAL- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 tELMTSgTLKMYLKR------FKRINIkVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT----GTTGSVKIGDLG 432
Cdd:cd13982    75 -ELCAA-SLQDLVESpresklFLRPGL-EPVRLLRQIASGLAHLHSLN--IVHRDLKPQNILIStpnaHGNVRAMISDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LAtlKNKSFAKS-------VIGTPEFMAPEMYEEMYDE----SVDVYAFGmCLLemvtgEYPYSECMNP--------ATI 493
Cdd:cd13982   150 LC--KKLDVGRSsfsrrsgVAGTSGWIAPEMLSGSTKRrqtrAVDIFSLG-CVF-----YYVLSGGSHPfgdklereANI 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  494 YRKVISGVKPEcfsRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd13982   222 LKGKYSLDKLL---SLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPFF 268
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
287-484 6.03e-18

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: 86.98  E-value: 6.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCEL-QESKLNKTERQRFREEAEMLKDLQHPNIVRF-YDYWESADLCgkrkyivLVTE 364
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILrKEVIIAKDEVAHTVTESRVLQNTRHPFLTALkYAFQTHDRLC-------FVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05595    76 YANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRD--VVYRDIKLENLMLD-KDGHIKITDFGLCKegITDGATM 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05595   153 KTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
285-490 8.52e-18

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I 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: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 85.79  E-value: 8.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVawcelqeSKLNKTERQRFREEAEM--LKDLQHPNIVRFY--DYWeSADLCGKrkyIV 360
Cdd:cd14056     1 KTIGKGRYGEVWLGKYRGEKVAV-------KIFSSRDEDSWFRETEIyqTVMLRHENILGFIaaDIK-STGSWTQ---LW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHT------RNPPVIHRDLKCDNIFITGtTGSVKIGDLGLA 434
Cdd:cd14056    70 LITEYHEHGSLYDYLQR-NTLDTEEALRLAYSAASGLAHLHTeivgtqGKPAIAHRDLKSKNILVKR-DGTCCIADLGLA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TLknKSFAKSVI--------GTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEM-----VTG---EY--PYSECMN 489
Cdd:cd14056   148 VR--YDSDTNTIdippnprvGTKRYMAPEVLDDSINPKsfesfkmADIYSFGLVLWEIarrceIGGiaeEYqlPYFGMVP 225

                  .
gi 392899979  490 P 490
Cdd:cd14056   226 S 226
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
283-500 9.33e-18

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: 85.81  E-value: 9.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLnkTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLV 362
Cdd:cd14166     7 FMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPL--SRDSSLENEIAVLKRIKHENIVTLEDIYES------TTHYYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLkmylkrFKRI------NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI-FITGTTGS-VKIGDLGLA 434
Cdd:cd14166    79 MQLVSGGEL------FDRIlergvyTEKDASRVINQVLSAVKYLHENG--IVHRDLKPENLlYLTPDENSkIMITDFGLS 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  435 TLKNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG 500
Cdd:cd14166   151 KMEQNGIMSTACGTPGYVAPEvLAQKPYSKAVDCWSIGVITYILLCGYPPFYE-ETESRLFEKIKEG 216
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
287-500 1.05e-17

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: 84.87  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrKYiVLVTE 364
Cdd:cd14070    10 LGEGSFAKVREGLHAVTGekVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETEN-----SY-YLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNiFITGTTGSVKIGDLGLA-TLKNKSFAK 443
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAG--VVHRDLKIEN-LLLDENDNIKLIDFGLSnCAGILGYSD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  444 SVI---GTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYS-ECMNPATIYRKVISG 500
Cdd:cd14070   161 PFStqcGSPAYAAPELLaRKKYGPKVDVWSIGVNMYAMLTGTLPFTvEPFSLRALHQKMVDK 222
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
286-489 1.06e-17

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: 85.03  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwCELQESKLNKteRQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrKYIvLVTEL 365
Cdd:cd14113    14 ELGRGRFSVVKKCDQRGTKRAVA-TKFVNKKLMK--RDQVTHELGVLQSLQHPQLVGLLDTFETPT-----SYI-LVLEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFI--TGTTGSVKIGDLGLATLKNKS-FA 442
Cdd:cd14113    85 ADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLH--NCRIAHLDLKPENILVdqSLSKPTIKLADFGDAVQLNTTyYI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392899979  443 KSVIGTPEFMAPEM-YEEMYDESVDVYAFGMCLLEMVTGEYPYSE------CMN 489
Cdd:cd14113   163 HQLLGSPEFAAPEIiLGNPVSLTSDLWSIGVLTYVLLSGVSPFLDesveetCLN 216
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
281-538 1.06e-17

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: 84.91  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGlDTETGVAVAWCELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYDywesadLCGKRKYIV 360
Cdd:cd05114     6 LTFMKELGSGLFGVVRLG-KWRAQYKVAIKAIREGAMSEED---FIEEAKVMMKLTHPKLVQLYG------VCTQQKPIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLK-RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA--TLK 437
Cdd:cd05114    76 IVTEFMENGCLLNYLRqRRGKLSRDMLLSMCQDVCEGMEYLERNN--FIHRDLAARNCLVN-DTGVVKVSDFGMTryVLD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTP-EFMAPEMYE-EMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISG---VKPECFSRIpa 511
Cdd:cd05114   153 DQYTSSSGAKFPvKWSPPEVFNySKFSSKSDVWSFGVLMWEVFTeGKMPFESKSN-YEVVEMVSRGhrlYRPKLASKS-- 229
                         250       260
                  ....*....|....*....|....*..
gi 392899979  512 qypeIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05114   230 ----VYEVMYSCWHEKPEGRPTFADLL 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
285-539 1.12e-17

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: 84.60  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGL--DTETGVAVAWCElqeSKLNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLV 362
Cdd:cd05084     2 ERIGRGNFGEVFSGRlrADNTPVAVKSCR---ETLPPDLKAKFLQEARILKQYSHPNIVRL------IGVCTQKQPIYIV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLK-RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSF 441
Cdd:cd05084    73 MELVQGGDFLTFLRtEGPRLKVKELIRMVENAAAGMEYLESKH--CIHRDLAARNCLVT-EKNVLKISDFGMSREEEDGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPE----FMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATiyRKVIS-GVKPECfsriPAQY 513
Cdd:cd05084   150 YAATGGMKQipvkWTAPEAlnYGRYSSES-DVWSFGILLWETFSlGAVPYANLSNQQT--REAVEqGVRLPC----PENC 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  514 P-EIREIIDRCIRV---RREERSTVKQLLV 539
Cdd:cd05084   223 PdEVYRLMEQCWEYdprKRPSFSTVHQDLQ 252
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
284-484 1.20e-17

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: 84.97  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQRFREEA----EMLKDLQHPNIVRFYDYWESadlcgkRKYI 359
Cdd:cd14193     9 EEILGGGRFGQVHKCEEKSSGLKLA------AKIIKARSQKEKEEVkneiEVMNQLNHANLIQLYDAFES------RNDI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLkmylkrFKRI---NIKVLK----SWCRQILKGLSFLHTRNppVIHRDLKCDNIF-ITGTTGSVKIGDL 431
Cdd:cd14193    77 VLVMEYVDGGEL------FDRIideNYNLTEldtiLFIKQICEGIQYMHQMY--ILHLDLKPENILcVSREANQVKIIDF 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  432 GLA-TLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14193   149 GLArRYKPREKLRVNFGTPEFLAPEVVNyEFVSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
282-537 1.29e-17

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: 84.65  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRFREeaemlKDLQHPNIVRFYDYWESAdlcgkrKYI 359
Cdd:cd14665     3 ELVKDIGSGNFGVARLMRDKQTKelVAVKYIERGEKIDENVQREIINH-----RSLRHPNIVRFKEVILTP------THL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG-SVKIGDLGLATLKN 438
Cdd:cd14665    72 AIVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQ--ICHRDLKLENTLLDGSPApRLKICDFGYSKSSV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 -KSFAKSVIGTPEFMAPE-MYEEMYDESV-DVYAFGMCLLEMVTGEYPYSECMNPATiYRKVISGVKPECFSrIPAQY-- 513
Cdd:cd14665   150 lHSQPKSTVGTPAYIAPEvLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRN-FRKTIQRILSVQYS-IPDYVhi 227
                         250       260
                  ....*....|....*....|....*
gi 392899979  514 -PEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd14665   228 sPECRHLISRIFVADPATRITIPEI 252
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
286-477 1.37e-17

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: 85.40  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTER----QRFREEAeMLKDLQ---HPNIVRFYDYWESADLCGKRKy 358
Cdd:cd07863     7 EIGVGAYGTVYKARDPHSGHFVA---LKSVRVQTNEDglplSTVREVA-LLKRLEafdHPNIVRLMDVCATSRTDRETK- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSgTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd07863    82 VTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANC--IVHRDLKPENILVT-SGGQVKLADFGLARI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  437 KNKSFA-KSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEM 477
Cdd:cd07863   158 YSCQMAlTPVVVTLWYRAPEvLLQSTYATPVDMWSVGCIFAEM 200
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
285-538 1.60e-17

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: 85.07  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSF----KTVFRGLDTETGVAVawcelqeskLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIV 360
Cdd:cd14178     9 EDIGIGSYsvckRCVHKATSTEYAVKI---------IDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDG------KFVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIGDLGLAtlK 437
Cdd:cd14178    74 LVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQG--VVHRDLKPSNILYmdeSGNPESIRICDFGFA--K 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTP----EFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMN--PATIYRKVISGVKPECFSRIP 510
Cdd:cd14178   150 QLRAENGLLMTPcytaNFVAPEVLKRQgYDAACDIWSLGILLYTMLAGFTPFANGPDdtPEEILARIGSGKYALSGGNWD 229
                         250       260
                  ....*....|....*....|....*...
gi 392899979  511 AQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14178   230 SISDAAKDIVSKMLHVDPHQRLTAPQVL 257
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
284-500 1.62e-17

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: 85.43  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWcelqesklnKTERQRF--REEAEMLKDLQ-HPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14092    11 EEALGDGSFSVCRKCVHKKTGQEFAV---------KIVSRRLdtSREVQLLRLCQgHPNIVKLHEVFQD------ELHTY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGDLGLATLKN 438
Cdd:cd14092    76 LVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKG--VVHRDLKPENLLFTdeDDDAEIKIVDFGFARLKP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  439 KSFAKSvigTPEFM----APEM-----YEEMYDESVDVYAFGMCLLEMVTGEYPY---SECMNPATIYRKVISG 500
Cdd:cd14092   154 ENQPLK---TPCFTlpyaAPEVlkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqspSRNESAAEIMKRIKSG 224
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
287-480 1.70e-17

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: 85.65  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWcelqeSKLNKTER-----QR-FREeAEMLKDLQHPNIVRFYDYWESADLCGKRKyIV 360
Cdd:cd07834     8 IGSGAYGVVCSAYDKRTGRKVAI-----KKISNVFDdlidaKRiLRE-IKILRHLKHENIIGLLDILRPPSPEEFND-VY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSgTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKS 440
Cdd:cd07834    81 IVTELMET-DLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAG--VIHRDLKPSNILVN-SNCDLKICDFGLARGVDPD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392899979  441 FAKsvigtpEFM----------APE---MYEEmYDESVDVYAFGmCLL-EMVTG 480
Cdd:cd07834   157 EDK------GFLteyvvtrwyrAPElllSSKK-YTKAIDIWSVG-CIFaELLTR 202
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
285-538 1.85e-17

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: 85.84  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQRFREEAE-MLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVT 363
Cdd:cd14176    25 EDIGVGSYSVCKRCIHKATNMEFA------VKIIDKSKRDPTEEIEiLLRYGQHPNIITLKDVYDDG------KYVYVVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTG---SVKIGDLGLAtlKNKS 440
Cdd:cd14176    93 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESGnpeSIRICDFGFA--KQLR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTP----EFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcmNPATIYRKVISGVKPECFSRIPAQYPE 515
Cdd:cd14176   169 AENGLLMTPcytaNFVAPEVLERQgYDAACDIWSLGVLLYTMLTGYTPFAN--GPDDTPEEILARIGSGKFSLSGGYWNS 246
                         250       260
                  ....*....|....*....|....*..
gi 392899979  516 I----REIIDRCIRVRREERSTVKQLL 538
Cdd:cd14176   247 VsdtaKDLVSKMLHVDPHQRLTAALVL 273
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
280-480 1.89e-17

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: 85.05  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEeLGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYdywesaDLCGKRK 357
Cdd:cd07873     4 YIKLDK-LGEGTYATVYKGRSKLTDNLVA---LKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLH------DIIHTEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd07873    74 SLTLVFEYLDK-DLKQYLDDCGNsINMHNVKLFLFQLLRGLAYCHRRK--VLHRDLKPQNLLIN-ERGELKLADFGLARA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KN---KSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07873   150 KSiptKTYSNEVV-TLWYRPPDILlgSTDYSTQIDMWGVGCIFYEMSTG 197
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
281-537 2.39e-17

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR 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: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 84.84  E-value: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDywesadLCGK 355
Cdd:cd05055    37 LSFGKTLGAGAFGKVVEatayGLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLG------ACTI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItgTTGSV-KIGDLG 432
Cdd:cd05055   111 GGPILVITEYCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKN--CIHRDLAARNVLL--THGKIvKICDFG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  433 LA-TLKNKS--FAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNPATIYRKVISGVKPECf 506
Cdd:cd05055   187 LArDIMNDSnyVVKGNARLPvKWMAPEsIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMAQ- 265
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  507 sriPAQYP-EIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05055   266 ---PEHAPaEIYDIMKTCWDADPLKRPTFKQI 294
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
284-487 2.52e-17

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: 84.39  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGV--AVAWCELQESKlnktERQRFREEAEMLKDLQ-HPNIVRFYDYWESADlcgkRKYiv 360
Cdd:cd14090     7 GELLGEGAYASVQTCINLYTGKeyAVKIIEKHPGH----SRSRVFREVETLHQCQgHPNILQLIEYFEDDE----RFY-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGDLGLAT-LK 437
Cdd:cd14090    77 LVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKG--IAHRDLKPENILCEsmDKVSPVKICDFDLGSgIK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  438 NKSFAKSVIGTP---------EFMAPEMYEEM------YDESVDVYAFGMCLLEMVTGeYP--YSEC 487
Cdd:cd14090   155 LSSTSMTPVTTPelltpvgsaEYMAPEVVDAFvgealsYDKRCDLWSLGVILYIMLCG-YPpfYGRC 220
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
287-537 3.57e-17

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: 83.62  E-value: 3.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTErqrFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLVTELM 366
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEE---FLKEAAVMKEIKHPNLVQLL------GVCTREPPFYIITEFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLA------TLKN 438
Cdd:cd05052    85 PYGNLLDYLRECNReeLNAVVLLYMATQIASAMEYLEKKN--FIHRDLAARNCLV-GENHLVKVADFGLSrlmtgdTYTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIgtpEFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPaqyPE 515
Cdd:cd05052   162 HAGAKFPI---KWTAPEslAYNKFSIKS-DVWAFGVLLWEIATyGMSPYPG-IDLSQVYELLEKGYRMERPEGCP---PK 233
                         250       260
                  ....*....|....*....|..
gi 392899979  516 IREIIDRCIRVRREERSTVKQL 537
Cdd:cd05052   234 VYELMRACWQWNPSDRPSFAEI 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
323-544 4.24e-17

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: 83.56  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  323 QRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLVTELMTSGTLkMYLKRFKRINIKVLKSWCRQILKGLSFLHT 402
Cdd:cd14118    59 DRVYREIAILKKLDHPNVVKLVEVLDDPN----EDNLYMVFELVDKGAV-MEVPTDNPLSEETARSYFRDIVLGIEYLHY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  403 RNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL--KNKSFAKSVIGTPEFMAPEMYEEMYDE----SVDVYAFGMCLLE 476
Cdd:cd14118   134 QK--IIHRDIKPSNLLL-GDDGHVKIADFGVSNEfeGDDALLSSTAGTPAFMAPEALSESRKKfsgkALDIWAMGVTLYC 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  477 MVTGEYPYSEcMNPATIYRKVISgvKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd14118   211 FVFGRCPFED-DHILGLHEKIKT--DPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
285-538 4.39e-17

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: 83.02  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd14114     8 EELGTGAFGVVHRCTERATGNNFAAKFIMTP--HESDKETVRKEIQIMNQLHHPKLINLHDAFEDDN------EMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTL--KMYLKRFKRINIKVLkSWCRQILKGLSFLHTRNppVIHRDLKCDNI-FITGTTGSVKIGDLGLAT-LKNKS 440
Cdd:cd14114    80 FLSGGELfeRIAAEHYKMSEAEVI-NYMRQVCEGLCHMHENN--IVHLDIKPENImCTTKRSNEVKLIDFGLAThLDPKE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIyRKVIS---GVKPECFSRIPaqyPEI 516
Cdd:cd14114   157 SVKVTTGTAEFAAPEIVErEPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETL-RNVKScdwNFDDSAFSGIS---EEA 232
                         250       260
                  ....*....|....*....|..
gi 392899979  517 REIIDRCIRVRREERSTVKQLL 538
Cdd:cd14114   233 KDFIRKLLLADPNKRMTIHQAL 254
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
285-484 4.55e-17

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: 83.05  E-value: 4.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQesKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVIN--KQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIET------PNEIVLFME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLkmylkrFKRI--------NIKVLkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLAT 435
Cdd:cd14190    82 YVEGGEL------FERIvdedyhltEVDAM-VFVRQICEGIQFMHQMR--VLHLDLKPENILCVNRTGHqVKIIDFGLAR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  436 LKN-KSFAKSVIGTPEFMAPEM--YEEMYDeSVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14190   153 RYNpREKLKVNFGTPEFLSPEVvnYDQVSF-PTDMWSMGVITYMLLSGLSPF 203
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
287-479 4.73e-17

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 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: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 83.97  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG-LDTETG-----VAVAWCELQESKLNKTERQRFREEaemlkDLQHPNIVRFYDYWESADlcGKRKYIV 360
Cdd:cd14055     3 VGKGRFAEVWKAkLKQNASgqyetVAVKIFPYEEYASWKNEKDIFTDA-----SLKHENILQFLTAEERGV--GLDRQYW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHT-RNP------PVIHRDLKCDNIFITgTTGSVKIGDLGL 433
Cdd:cd14055    76 LITAYHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSdRTPcgrpkiPIAHRDLKSSNILVK-NDGTCVLADFGL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 A-----TLKNKSFAKS-VIGTPEFMAPEMYE--------EMYDEsVDVYAFGMCLLEMVT 479
Cdd:cd14055   154 AlrldpSLSVDELANSgQVGTARYMAPEALEsrvnledlESFKQ-IDVYSMALVLWEMAS 212
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
284-543 4.92e-17

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: 83.09  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWcelqesKLNKTERQRFR---EEAEMLKDLQ------HPNIVRFYDYWESadlcg 354
Cdd:cd14133     4 LEVLGKGTFGQVVKCYDLLTGEEVAL------KIIKNNKDYLDqslDEIRLLELLNkkdkadKYHIVRLKDVFYF----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 kRKYIVLVTELMtSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITG-TTGSVKIGDL 431
Cdd:cd14133    73 -KNHLCIVFELL-SQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLG--LIHCDLKPENILLASySRCQIKIIDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLATLKNKSFAkSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYPYSECMNPATIYRKVISGVKPECFSRI- 509
Cdd:cd14133   149 GSSCFLTQRLY-SYIQSRYYRAPEVILGLpYDEKIDMWSLGCILAELYTG-EPLFPGASEVDQLARIIGTIGIPPAHMLd 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  510 --PAQYPEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14133   227 qgKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
287-484 5.54e-17

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: 83.75  E-value: 5.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTerQRFREEAEMLKDLQ-HPNIVRFYDYWESADLcgkrKYIVLVTEL 365
Cdd:cd14132    26 IGRGKYSEVFEGINIGNNEKVV---IKVLKPVKK--KKIKREIKILQNLRgGPNIVKLLDVVKDPQS----KTPSLIFEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKmylKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT--LKNKSFAK 443
Cdd:cd14132    97 VNNTDFK---TLYPTLTDYDIRYYMYELLKALDYCHSKG--IMHRDVKPHNIMIDHEKRKLRLIDWGLAEfyHPGQEYNV 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392899979  444 SViGTPEFMAPEM---YEeMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14132   172 RV-ASRYYKGPELlvdYQ-YYDYSLDMWSLGCMLASMIFRKEPF 213
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
287-515 5.70e-17

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: 82.92  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG-----LDTETGVAVAWCELQESKLNKTERQ-RFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14076     9 LGEGEFGKVKLGwplpkANHRSGVQVAIKLIRRDTQQENCQTsKIMREINILKGLTHPNIVRLLDVLKT------KKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT---LK 437
Cdd:cd14076    83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKG--VVHRDLKLENLLLD-KNRNLVITDFGFANtfdHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTPEFMAPEMY--EEMYDES-VDVYAFGMCLLEMVTGEYPYS------ECMNPATIYRKVISgvkpecfsr 508
Cdd:cd14076   160 NGDLMSTSCGSPCYAAPELVvsDSMYAGRkADIWSCGVILYAMLAGYLPFDddphnpNGDNVPRLYRYICN--------- 230

                  ....*..
gi 392899979  509 IPAQYPE 515
Cdd:cd14076   231 TPLIFPE 237
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
287-537 8.31e-17

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: 82.31  E-value: 8.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCElqesklNKTERQRFREEAEMLKDLQHPNIVRFydywesadLCGKRKYIVLVTELM 366
Cdd:cd14068     2 LGDGGFGSVYRAVYRGEDVAVKIFN------KHTSFRLLRQELVVLSHLHHPSLVAL--------LAAGTAPRMLVMELA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTrnPPVIHRDLKCDNIFI----TGTTGSVKIGDLGLATLKNKSF 441
Cdd:cd14068    68 PKGSLDALLQQDNaSLTRTLQHRIALHVADGLRYLHS--AMIIYRDLKPHNVLLftlyPNCAIIAKIADYGIAQYCCRMG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSVIGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPYSECMN-PATIYRKVISGVKPECFSRIP-AQYPEIR 517
Cdd:cd14068   146 IKTSEGTPGFRAPEVARGnvIYNQQADVYSFGLLLYDILTCGERIVEGLKfPNEFDELAIQGKLPDPVKEYGcAPWPGVE 225
                         250       260
                  ....*....|....*....|
gi 392899979  518 EIIDRCIRVRREERSTVKQL 537
Cdd:cd14068   226 ALIKDCLKENPQCRPTSAQV 245
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
273-536 8.31e-17

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: 82.38  E-value: 8.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  273 DKSKNGRFLKFDEelgrgsFKTVFRGLDTETGvAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadl 352
Cdd:cd14088     1 DRYDLGQVIKTEE------FCEIFRAKDKTTG-KLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFET--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 cgkRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVK--IGD 430
Cdd:cd14088    71 ---RKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLK--IVHRNLKLENLVYYNRLKNSKivISD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLATLKNkSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNP-------ATIYRKVISG-- 500
Cdd:cd14088   146 FHLAKLEN-GLIKEPCGTPEYLAPEVVgRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEddyenhdKNLFRKILAGdy 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  501 -VKPECFSRIPaqyPEIREIIDRCIRVRREERSTVKQ 536
Cdd:cd14088   225 eFDSPYWDDIS---QAAKDLVTRLMEVEQDQRITAEE 258
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
283-538 8.85e-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: 82.60  E-value: 8.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLV 362
Cdd:cd14104     4 IAEELGRGQFGIVHRCVETSSKKTYM---AKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHE------ELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMtSGtlkmyLKRFKRINIKVLK-------SWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLA 434
Cdd:cd14104    75 FEFI-SG-----VDIFERITTARFElnereivSYVRQVCEALEFLHSKN--IGHFDIRPENIIYCTRRGSyIKIIEFGQS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 -TLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATI--YRKVISGVKPECFSRIP 510
Cdd:cd14104   147 rQLKPGDKFRLQYTSAEFYAPEVHQhESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIenIRNAEYAFDDEAFKNIS 226
                         250       260
                  ....*....|....*....|....*...
gi 392899979  511 AqypEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14104   227 I---EALDFVDRLLVKERKSRMTAQEAL 251
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
318-538 9.50e-17

Catalytic domain of an unknown subfamily of 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. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). 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: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 82.18  E-value: 9.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  318 NKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLVTELMTSGTLKMYLKRfkrinIKVLKSWcRQ----- 392
Cdd:cd14156    28 NDVDQHKIVREISLLQKLSHPNIVRYL------GICVKDEKLHPILEYVSGGCLEELLAR-----EELPLSW-REkvela 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  393 --ILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVK--IGDLGLA------TLKNKSFAKSVIGTPEFMAPEMYE-EMY 461
Cdd:cd14156    96 cdISRGMVYLHSKN--IYHRDLNSKNCLIRVTPRGREavVTDFGLArevgemPANDPERKLSLVGSAFWMAPEMLRgEPY 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  462 DESVDVYAFGMCLLEMVtGEYPysecMNPATIYRKVISGVKPECF-SRIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14156   174 DRKVDVFSFGIVLCEIL-ARIP----ADPEVLPRTGDFGLDVQAFkEMVPGCPEPFLDLAASCCRMDAFKRPSFAELL 246
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
285-479 1.06e-16

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: 82.47  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREeAEMLKDLQHPNIVRFYD--YWESadlcgkRKYivL 361
Cdd:cd07861     6 EKIGEGTYGVVYKGRNKKTGQIVAMKKIRlESEEEGVPSTAIRE-ISLLKELQHPNIVCLEDvlMQEN------RLY--L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMtSGTLKMYL---KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAtlkn 438
Cdd:cd07861    77 VFEFL-SMDLKKYLdslPKGKYMDAELVKSYLYQILQGILFCHSRR--VLHRDLKPQNLLID-NKGVIKLADFGLA---- 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  439 KSFAKSV------IGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07861   149 RAFGIPVrvytheVVTLWYRAPEvlLGSPRYSTPVDIWSIGTIFAEMAT 197
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
285-514 1.10e-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: 82.16  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVF--RGLDTETgvavaWCELQESKL---NKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCgkRKYI 359
Cdd:cd14025     2 EKVGSGGFGQVYkvRHKHWKT-----WLAIKCPPSlhvDDSERMELLEEAKKMEMAKFRHILPVYG------IC--SEPV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLK--------MYLKRFKRINikvlkswcrQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTgSVKIGDL 431
Cdd:cd14025    69 GLVMEYMETGSLEkllaseplPWELRFRIIH---------ETAVGMNFLHCMKPPLLHLDLKPANILLDAHY-HVKISDF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLATLKNKSFAK-----SVIGTPEFMAPEMYEE---MYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKP 503
Cdd:cd14025   139 GLAKWNGLSHSHdlsrdGLRGTIAYLPPERFKEknrCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRP 218
                         250
                  ....*....|.
gi 392899979  504 EcFSRIPAQYP 514
Cdd:cd14025   219 S-LSPIPRQRP 228
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
287-512 1.14e-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: 83.55  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07877    25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 tsGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVi 446
Cdd:cd07877   105 --GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSAD--IIHRDLKPSNLAVNEDC-ELKILDFGLARHTDDEMTGYV- 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  447 GTPEFMAPE-MYEEM-YDESVDVYAFGMCLLEMVTGE--YPYSECMNPATIYRKVISGVKPECFSRIPAQ 512
Cdd:cd07877   179 ATRWYRAPEiMLNWMhYNQTVDIWSVGCIMAELLTGRtlFPGTDHIDQLKLILRLVGTPGAELLKKISSE 248
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
284-500 1.15e-16

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: 83.17  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWCELQEsklnKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVT 363
Cdd:cd14179    12 DKPLGEGSFSICRKCLHKKTNQEYAVKIVSK----RMEANTQREIAALKLCEGHPNIVKLHEVYHD------QLHTFLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITGTTGS--VKIGDLGLATLK--NK 439
Cdd:cd14179    82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMH--DVGVVHRDLKPENLLFTDESDNseIKIIDFGFARLKppDN 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  440 SFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYS------ECMNPATIYRKVISG 500
Cdd:cd14179   160 QPLKTPCFTLHYAAPELLNYNgYDESCDLWSLGVILYTMLSGQVPFQchdkslTCTSAEEIMKKIKQG 227
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
285-547 1.25e-16

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: 82.76  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTErqrfreEAEMLKDL-QHPNIVRFYDYWESAdlcgkrKYIVLVT 363
Cdd:cd14177    10 EDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVYDDG------RYVYLVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIGDLGlatlknks 440
Cdd:cd14177    78 ELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQG--VVHRDLKPSNILYmddSANADSIRICDFG-------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSVIG----------TPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMN--PATIYRKVISGVkpecFS 507
Cdd:cd14177   148 FAKQLRGengllltpcyTANFVAPEvLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNdtPEEILLRIGSGK----FS 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 392899979  508 RIPAQYPEI----REIIDRCIRVRREERSTVKQLLVDDFFTPED 547
Cdd:cd14177   224 LSGGNWDTVsdaaKDLLSHMLHVDPHQRYTAEQVLKHSWIACRD 267
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
285-489 1.41e-16

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: 81.55  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKT----ERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIV 360
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLA------AKIIKVkgakEREEVKNEINIMNQLNHVNLIQLYDAFES------KTNLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLkmylkrFKRI-----NIKVLKS--WCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLG 432
Cdd:cd14192    78 LIMEYVDGGEL------FDRItdesyQLTELDAilFTRQICEGVHYLHQHY--ILHLDLKPENILCVNSTGNqIKIIDFG 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  433 LA-TLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY-----SECMN 489
Cdd:cd14192   150 LArRYKPREKLKVNFGTPEFLAPEVVNyDFVSFPTDMWSVGVITYMLLSGLSPFlgetdAETMN 213
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
325-531 1.57e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. 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 LRRK1 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: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 81.93  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  325 FREEAEMLKDLQHPNIVRFYDYwESADLCgkrkyivLVTELMTSGTLKMYLKR------FKRINIKVLKSWCRQILKGLS 398
Cdd:cd14067    57 FRQEASMLHSLQHPCIVYLIGI-SIHPLC-------FALELAPLGSLNTVLEEnhkgssFMPLGHMLTFKIAYQIAAGLA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  399 FLHTRNppVIHRDLKCDNIFI----TGTTGSVKIGDLGLATLKNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMC 473
Cdd:cd14067   129 YLHKKN--IIFCDLKSDNILVwsldVQEHINIKLSDYGISRQSFHEGALGVEGTPGYQAPEIRPRIvYDEKVDMFSYGMV 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  474 LLEMVTGEYPySECMNPATIYRKVISGVKPECFSRIPAQYPEIREIIDRCIRVRREER 531
Cdd:cd14067   207 LYELLSGQRP-SLGHHQLQIAKKLSKGIRPVLGQPEEVQFFRLQALMMECWDTKPEKR 263
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
287-481 1.79e-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: 83.11  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07851    23 VGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEDFQDVYLVTHLM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSgTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVi 446
Cdd:cd07851   103 GA-DLNNIVKC-QKLSDDHIQFLVYQILRGLKYIHSAG--IIHRDLKPSNLAVNEDC-ELKILDFGLARHTDDEMTGYV- 176
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 392899979  447 GTPEFMAPE-MYEEM-YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07851   177 ATRWYRAPEiMLNWMhYNQTVDIWSVGCIMAELLTGK 213
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
287-496 1.80e-16

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: 82.18  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCElQESKLN-KTERQRFREEAEMLKDLQHPNIVRFYDYwesadlCGKRKYIVLVTEL 365
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTEYAVKRLK-EDSELDwSVVKNSFLTEVEKLSRFRHPNIVDLAGY------SAQQGNYCLIYVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKR---------FKRINIKVLKSwcrqilKGLSFLHTRNPPVIHRDLKCDNIFItGTTGSVKIGDLGLATL 436
Cdd:cd14159    74 LPNGSLEDRLHCqvscpclswSQRLHVLLGTA------RAIQYLHSDSPSLIHGDVKSSNILL-DAALNPKLGDFGLARF 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  437 --------KNKSFAK--SVIGTPEFMaPEMYEEMYDESV--DVYAFGMCLLEMVTGEYPYSECMNPATIYRK 496
Cdd:cd14159   147 srrpkqpgMSSTLARtqTVRGTLAYL-PEEYVKTGTLSVeiDVYSFGVVLLELLTGRRAMEVDSCSPTKYLK 217
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
285-479 1.92e-16

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 81.79  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTE 364
Cdd:PLN00009    8 EKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHS------EKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LmtsgtLKMYLKR-------FKRiNIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT-- 435
Cdd:PLN00009   82 Y-----LDLDLKKhmdsspdFAK-NPRLIKTYLYQILRGIAYCHSHR--VLHRDLKPQNLLIDRRTNALKLADFGLARaf 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  436 -LKNKSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVT 479
Cdd:PLN00009  154 gIPVRTFTHEVV-TLWYRAPEILlgSRHYSTPVDIWSVGCIFAEMVN 199
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
285-543 2.02e-16

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: 81.50  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTET--GVAVAWCELQESKLNKTER-QRFRE----EAEMLKDLQ-HPNIVRFYDYWESadlcgkR 356
Cdd:cd14182     9 EILGRGVSSVVRRCIHKPTrqEYAVKIIDITGGGSFSPEEvQELREatlkEIDILRKVSgHPNIIQLKDTYET------N 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT- 435
Cdd:cd14182    83 TFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLN--IVHRDLKPENILLDDDM-NIKLTDFGFSCq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAKSVIGTPEFMAPEMYE-------EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG----VKPE 504
Cdd:cd14182   160 LDPGEKLREVCGTPGYLAPEIIEcsmddnhPGYGKEVDMWSTGVIMYTLLAGSPPFWH-RKQMLMLRMIMSGnyqfGSPE 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  505 CFSRIPAqypeIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14182   239 WDDRSDT----VKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
287-495 2.29e-16

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: 80.83  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDLQ-HPNIVRFYD-YWESADlcgkrkYIVLVTE 364
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMA---LKFVPKPSTKLKDFLREYNISLELSvHPHIIKTYDvAFETED------YYVFAQE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI-TGTTGSVKIGDLGLaTLKNKSFAK 443
Cdd:cd13987    72 YAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKN--LVHRDIKPENVLLfDKDCRRVKLCDFGL-TRRVGSTVK 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  444 SVIGTPEFMAPEMYE----EMY--DESVDVYAFGMCLLEMVTGEYPYSECMNPATIYR 495
Cdd:cd13987   149 RVSGTIPYTAPEVCEakknEGFvvDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYE 206
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
271-503 3.20e-16

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: 81.99  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  271 PIDKSKNGRFLKFdeeLGRGSFKTVF--RGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWE 348
Cdd:cd05602     2 PHAKPSDFHFLKV---IGKGSFGKVLlaRHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  349 SADlcgkRKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKI 428
Cdd:cd05602    79 TTD----KLYFVL--DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLN--IVYRDLKPENILLD-SQGHIVL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  429 GDLGLA--TLKNKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISgvKP 503
Cdd:cd05602   150 TDFGLCkeNIEPNGTTSTFCGTPEYLAPEvLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYS-RNTAEMYDNILN--KP 224
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
287-542 4.24e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 81.79  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREeAEMLKDLQHPNIVRFYDYWESAdlcGKrkyIVLVTELM 366
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICRE-IEILRDVNHPNVVKCHDMFDHN---GE---IQVLLEFM 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMylkrfKRINIK-VLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSF--AK 443
Cdd:PLN00034  155 DGGSLEG-----THIADEqFLADVARQILSGIAYLHRRH--IVHRDIKPSNLLIN-SAKNVKIADFGVSRILAQTMdpCN 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPE-----MYEEMYDESV-DVYAFGMCLLEMVTGEYPY--SECMNPATIYRKVISGVKPECfsrIPAQYPE 515
Cdd:PLN00034  227 SSVGTIAYMSPErintdLNHGAYDGYAgDIWSLGVSILEFYLGRFPFgvGRQGDWASLMCAICMSQPPEA---PATASRE 303
                         250       260
                  ....*....|....*....|....*..
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLVDDF 542
Cdd:PLN00034  304 FRHFISCCLQREPAKRWSAMQLLQHPF 330
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
287-491 4.34e-16

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: 79.88  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAV------AWCelqesklNKTERQRFREEAEMLKDLQHPNIVRFYdyweSADLCGKRKYiV 360
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKIVAIkryranTYC-------SKSDVDMFCREVSILCRLNHPCVIQFV----GACLDDPSQF-A 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTGSVKIGDLG----LAT 435
Cdd:cd14064    69 IVTQYVSGGSLFSLLHEQKRvIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLY-EDGHAVVADFGesrfLQS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  436 LKNKSFAKSViGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPYSEcMNPA 491
Cdd:cd14064   148 LDEDNMTKQP-GNLRWMAPEVFTQctRYSIKADVFSYALCLWELLTGEIPFAH-LKPA 203
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
287-498 4.93e-16

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: 81.55  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAE-MLKDLQHPNIVRFYDYWESADlcgkRKYIVLvtE 364
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKViLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTD----KLYFVL--D 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05604    78 FVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSIN--IVYRDLKPENILLD-SQGHIVLTDFGLCKegISNSDTT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  443 KSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVI 498
Cdd:cd05604   155 TTFCGTPEYLAPEvIRKQPYDNTVDWWCLGSVLYEMLYGLPPFY-CRDTAEMYENIL 210
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
285-543 5.20e-16

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: 80.39  E-value: 5.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLV 362
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVA---LKVISMKTEEGVPFTaiREASLLKGLKHANIVLLHDIIHT------KETLTFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSgTLKMYLKR----FKRINIKVlksWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd07870    77 FEYMHT-DLAQYMIQhpggLHPYNVRL---FMFQLLRGLAYIHGQH--ILHRDLKPQNLLIS-YLGELKLADFGLARAKS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 ---KSFAKSVIgTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKV--ISGVKPE----CFS 507
Cdd:cd07870   150 ipsQTYSSEVV-TLWYRPPDvlLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIwtVLGVPTEdtwpGVS 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  508 RIPAQYPEI---------REIIDRCIRVRREE-------------RSTVKQLLVDDFF 543
Cdd:cd07870   229 KLPNYKPEWflpckpqqlRVVWKRLSRPPKAEdlasqmlmmfpkdRISAQDALLHPYF 286
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
288-498 5.83e-16

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: 81.12  E-value: 5.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTELM 366
Cdd:cd05599    10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSEmLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEE------NLYLIMEFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKSFAKSV 445
Cdd:cd05599    84 PGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLG--YIHRDIKPDNLLLD-ARGHIKLSDFGLCTgLKKSHLAYST 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  446 IGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYP--YSEcmNPATIYRKVI 498
Cdd:cd05599   161 VGTPDYIAPEVFLQKgYGKECDWWSLGVIMYEMLIG-YPpfCSD--DPQETCRKIM 213
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
282-538 6.34e-16

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: 79.69  E-value: 6.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVL 361
Cdd:cd14184     4 KIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTP------AELYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIGDLGLATLKN 438
Cdd:cd14184    77 VMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLC--IVHRDIKPENLLVceyPDGTKSLKLGDFGLATVVE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAkSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY-SECMNPATIYRKVISGvKPEcfsrIPAQY--- 513
Cdd:cd14184   155 GPLY-TVCGTPTYVAPEIIAETgYGLKVDIWAAGVITYILLCGFPPFrSENNLQEDLFDQILLG-KLE----FPSPYwdn 228
                         250       260
                  ....*....|....*....|....*..
gi 392899979  514 --PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14184   229 itDSAKELISHMLQVNVEARYTAEQIL 255
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
323-544 6.97e-16

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: 79.99  E-value: 6.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  323 QRFREEAEMLKDLQHPNIVRFYDYWESAdlcgKRKYIVLVTELMTSGTLkMYLKRFKRINIKVLKSWCRQILKGLSFLHT 402
Cdd:cd14200    68 ERVYQEIAILKKLDHVNIVKLIEVLDDP----AEDNLYMVFDLLRKGPV-MEVPSDKPFSEDQARLYFRDIVLGIEYLHY 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  403 RNppVIHRDLKCDNIFItGTTGSVKIGDLGLATL--KNKSFAKSVIGTPEFMAPEMYEE----MYDESVDVYAFGMCLLE 476
Cdd:cd14200   143 QK--IVHRDIKPSNLLL-GDDGHVKIADFGVSNQfeGNDALLSSTAGTPAFMAPETLSDsgqsFSGKALDVWAMGVTLYC 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  477 MVTGEYPYSECMnPATIYRKVISgvKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd14200   220 FVYGKCPFIDEF-ILALHNKIKN--KPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
280-498 7.03e-16

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: 80.25  E-value: 7.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAwcelqESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKY 358
Cdd:cd14085     4 FFEIESELGRGATSVVYRCRQKGTQKPYA-----VKKLKKTvDKKIVRTEIGVLLRLSHPNIIKLKEIFETP------TE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLkmylkrFKRINIKVLKS------WCRQILKGLSFLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGD 430
Cdd:cd14085    73 ISLVLELVTGGEL------FDRIVEKGYYSerdaadAVKQILEAVAYLHENG--IVHRDLKPENLLYAtpAPDAPLKIAD 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLAT-LKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVI 498
Cdd:cd14085   145 FGLSKiVDQQVTMKTVCGTPGYCAPEILRgCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRIL 214
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
285-483 7.09e-16

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: 79.69  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGvavawcELQESKLNKTER----QRFREEAEMLKDLQHPNIVRFYDYWesadLCGKRKYIV 360
Cdd:cd06646    15 QRVGSGTYGDVYKARNLHTG------ELAAVKIIKLEPgddfSLIQQEIFMVKECKHCNIVAYFGSY----LSREKLWIC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpvIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKS 440
Cdd:cd06646    85 M--EYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGK--MHRDIKGANILLT-DNGDVKLADFGVAAKITAT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  441 FA--KSVIGTPEFMAPEMY----EEMYDESVDVYAFGMCLLEMVTGEYP 483
Cdd:cd06646   160 IAkrKSFIGTPYWMAPEVAavekNGGYNQLCDIWAVGITAIELAELQPP 208
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
332-543 8.50e-16

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: 79.35  E-value: 8.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  332 LKDLQHPNIVRFYDYWESADlcgkrkYIVLVTELMTSGT-LKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHR 410
Cdd:cd14004    62 LNKRSHPNIVKLLDFFEDDE------FYYLVMEKHGSGMdLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQG--IVHR 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  411 DLKCDNIFITGtTGSVKIGDLGLAT-LKNKSFaKSVIGTPEFMAPEMYE-EMYD-ESVDVYAFGMCLLEMVTGEYPYSEc 487
Cdd:cd14004   134 DIKDENVILDG-NGTIKLIDFGSAAyIKSGPF-DTFVGTIDYAAPEVLRgNPYGgKEQDIWALGVLLYTLVFKENPFYN- 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  488 mnpatiyrkVISGVKPEcfSRIPAQYPE-----IREIIDRCIrvrrEERSTVKQLLVDDFF 543
Cdd:cd14004   211 ---------IEEILEAD--LRIPYAVSEdlidlISRMLNRDV----GDRPTIEELLTDPWL 256
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
282-480 8.62e-16

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: 80.44  E-value: 8.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELqeskLNKTERQRF----REEAEMLKDLQHPNIVRFYD--YWESADLCGK 355
Cdd:cd07866    11 EILGKLGEGTFGEVYKARQIKTGRVVALKKI----LMHNEKDGFpitaLREIKILKKLKHPNVVPLIDmaVERPDKSKRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMT---SGTLKMylkrfKRINIKV--LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGD 430
Cdd:cd07866    87 RGSVYMVTPYMDhdlSGLLEN-----PSVKLTEsqIKCYMLQLLEGINYLHENH--ILHRDIKAANILID-NQGILKIAD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  431 LGLA--------TLKNKSFA-----KSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07866   159 FGLArpydgpppNPKGGGGGgtrkyTNLVVTRWYRPPEllLGERRYTTAVDIWGIGCVFAEMFTR 223
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
323-544 9.32e-16

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: 79.62  E-value: 9.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  323 QRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLVTELMTSGTLkMYLKRFKRINIKVLKSWCRQILKGLSFLHT 402
Cdd:cd14199    70 ERVYQEIAILKKLDHPNVVKLVEVLDDPS----EDHLYMVFELVKQGPV-MEVPTLKPLSEDQARFYFQDLIKGIEYLHY 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  403 RNppVIHRDLKCDNIFItGTTGSVKIGDLGLA-TLK-NKSFAKSVIGTPEFMAPEMYEEMYD----ESVDVYAFGMCLLE 476
Cdd:cd14199   145 QK--IIHRDVKPSNLLV-GEDGHIKIADFGVSnEFEgSDALLTNTVGTPAFMAPETLSETRKifsgKALDVWAMGVTLYC 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  477 MVTGEYPYSEcMNPATIYRKVISgvKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFT 544
Cdd:cd14199   222 FVFGQCPFMD-ERILSLHSKIKT--QPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
287-480 1.05e-15

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: 80.34  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG---VAVawcelqesKL---NKTERQRFREEAEMLKDLQH--PN----IVRFYDYWEsadlcg 354
Cdd:cd14135     8 LGKGVFSNVVRARDLARGnqeVAI--------KIirnNELMHKAGLKELEILKKLNDadPDdkkhCIRLLRHFE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMtSGTLKMYLKRFKR---INIKVLKSWCRQILKGLSflHTRNPPVIHRDLKCDNIFITGTTGSVKIGDL 431
Cdd:cd14135    74 HKNHLCLVFESL-SMNLREVLKKYGKnvgLNIKAVRSYAQQLFLALK--HLKKCNILHADIKPDNILVNEKKNTLKLCDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  432 GLAtlknkSFAKSVIGTPE-----FMAPEMYEEM-YDESVDVYAFGMCLLEMVTG 480
Cdd:cd14135   151 GSA-----SDIGENEITPYlvsrfYRAPEIILGLpYDYPIDMWSVGCTLYELYTG 200
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
281-500 1.12e-15

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: 79.10  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIV 360
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFP---AKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITP------RYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYL-KRFKRINIKVLkSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNK 439
Cdd:cd14111    76 LIAEFCSGKELLHSLiDRFRYSEDDVV-GYLVQILQGLEYLHGRR--VLHLDIKPDNIMVTNLN-AIKIVDFGSAQSFNP 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  440 SFAKSV---IGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISG 500
Cdd:cd14111   152 LSLRQLgrrTGTLEYMAPEMVKgEPVGPPADIWSIGVLTYIMLSGRSPFED-QDPQETEAKILVA 215
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
278-480 1.27e-15

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: 80.21  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  278 GRFLKFdEELGRGSFKTVFRGLDTETGVAVAwcelqESKLNKTERQRFRE---EAEMLKDLQHPNIVRFYDYW--ESADL 352
Cdd:cd07854     5 SRYMDL-RPLGCGSNGLVFSAVDSDCDKRVA-----VKKIVLTDPQSVKHalrEIKIIRRLDHDNIVKVYEVLgpSGSDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CGKRKYIV------LVTELMTSgTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSV 426
Cdd:cd07854    79 TEDVGSLTelnsvyIVQEYMET-DLANVLEQ-GPLSEEHARLFMYQLLRGLKYIHSAN--VLHRDLKPANVFINTEDLVL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  427 KIGDLGLATL-----KNKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07854   155 KIGDFGLARIvdphySHKGYLSEGLVTKWYRSPRllLSPNNYTKAIDMWAAGCIFAEMLTG 215
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
307-536 1.29e-15

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 78.97  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  307 VAWCELQESKL-NKTERQRFREeaemLKDLQHPNIVRFYDywesadLCGKRKYIVLVTELMTSGTLK-MYLKRFKRINIK 384
Cdd:cd13992    28 VAIKHITFSRTeKRTILQELNQ----LKELVHDNLNKFIG------ICINPPNIAVVTEYCTRGSLQdVLLNREIKMDWM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  385 VLKSWCRQILKGLSFLHTrNPPVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVIGTPE-----FMAPEMYEE 459
Cdd:cd13992    98 FKSSFIKDIVKGMNYLHS-SSIGYHGRLKSSNCLVDSRW-VVKLTDFGLRNLLEEQTNHQLDEDAQhkkllWTAPELLRG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  460 mYDESV------DVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGVK----PECFSRIPAQYPEIREIIDRCIRVRRE 529
Cdd:cd13992   176 -SLLEVrgtqkgDVYSFAIILYEILFRSDPFAL-EREVAIVEKVISGGNkpfrPELAVLLDEFPPRLVLLVKQCWAENPE 253

                  ....*..
gi 392899979  530 ERSTVKQ 536
Cdd:cd13992   254 KRPSFKQ 260
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
286-537 1.29e-15

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: 79.24  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRG-----LDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIV 360
Cdd:cd05092    12 ELGEGAFGKVFLAechnlLPEQDKMLVAVKALKEA--TESARQDFQREAELLTVLQHQHIVRFY------GVCTEGEPLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKR---------------FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGS 425
Cdd:cd05092    84 MVFEYMRHGDLNRFLRShgpdakildggegqaPGQLTLGQMLQIASQIASGMVYLASLH--FVHRDLATRNCLV-GQGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  426 VKIGDLGLATLKNKSFAKSVIGTP----EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATIyrkvi 498
Cdd:cd05092   161 VKIGDFGMSRDIYSTDYYRVGGRTmlpiRWMPPEsiLYRKFTTES-DIWSFGVVLWEIFTyGKQPWYQLSNTEAI----- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  499 sgvkpECFS------RIPAQYPEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05092   235 -----ECITqgreleRPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
285-480 1.36e-15

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: 79.65  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLV 362
Cdd:cd07872    12 EKLGEGTYATVFKGRSKLTENLVA---LKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLH------DIVHTDKSLTLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSgTLKMYLKRFKRI-NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN--- 438
Cdd:cd07872    83 FEYLDK-DLKQYMDDCGNImSMHNVKIFLYQILRGLAYCHRRK--VLHRDLKPQNLLIN-ERGELKLADFGLARAKSvpt 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392899979  439 KSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07872   159 KTYSNEVV-TLWYRPPDVLlgSSEYSTQIDMWGVGCIFFEMASG 201
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
326-479 1.36e-15

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: 79.64  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  326 REEAeMLKDLQHPNIVRfydywesadlcgkrkyivLVTELMTSGTLKMYL------------------KRFKRINIKVLK 387
Cdd:cd07842    51 REIA-LLRELKHENVVS------------------LVEVFLEHADKSVYLlfdyaehdlwqiikfhrqAKRVSIPPSMVK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  388 SWCRQILKGLSFLHTRNppVIHRDLKCDNIFITG---TTGSVKIGDLGLATLKN---KSFAKS--VIGTPEFMAPE--MY 457
Cdd:cd07842   112 SLLWQILNGIHYLHSNW--VLHRDLKPANILVMGegpERGVVKIGDLGLARLFNaplKPLADLdpVVVTIWYRAPEllLG 189
                         170       180
                  ....*....|....*....|..
gi 392899979  458 EEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07842   190 ARHYTKAIDIWAIGCIFAELLT 211
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
287-484 1.82e-15

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: 79.57  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVAWCE----LQESKLNKTerqrFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIV 360
Cdd:cd05590     3 LGKGSFGKVMLARLKESGrlYAVKVLKkdviLQDDDVECT----MTEKRILSLARNHPFLTQLYCCFQTPD------RLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKN 438
Cdd:cd05590    73 FVMEFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKG--IIYRDLKLDNVLLD-HEGHCKLADFGMCKegIFN 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05590   150 GKTTSTFCGTPDYIAPEILQEMlYGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
287-543 2.32e-15

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: 78.28  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRF-REEAEMLKDLQHPNIVRFYDYWESADlcgkrKYIVLVTEL 365
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFlPRELEILARLNHKSIIKTYEIFETSD-----GKVYIVMEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKS----- 440
Cdd:cd14165    84 GVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELD--IVHRDLKCENLLLDKDF-NIKLTDFGFSKRCLRDengri 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 -FAKSVIGTPEFMAPEMYEEM-YDESV-DVYAFGMCLLEMVTGEYPYSEcmnpaTIYRKVISGVKPE--CFSRIPAQYPE 515
Cdd:cd14165   161 vLSKTFCGSAAYAAPEVLQGIpYDPRIyDIWSLGVILYIMVCGSMPYDD-----SNVKKMLKIQKEHrvRFPRSKNLTSE 235
                         250       260
                  ....*....|....*....|....*...
gi 392899979  516 IREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14165   236 CKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
287-484 2.35e-15

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: 77.69  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwCELQESKLNKTERQRfrEEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVTELM 366
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVA-VKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESP------TSYILVLELM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFITGT--TGSVKIGDLGLAT-LKNKSFAK 443
Cdd:cd14115    72 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLH--NCRVAHLDIKPENLLIDLRipVPRVKLIDLEDAVqISGHRHVH 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 392899979  444 SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14115   150 HLLGNPEFAAPEVIQGTpVSLATDIWSIGVLTYVMLSGVSPF 191
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
286-557 2.35e-15

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: 77.89  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKT--VFRGLDTETGVAVAWCElqesKLNKTERQRFREEAEMlKDLQHPNIVRFydywesADLCGKRKYIVLVT 363
Cdd:cd14662     7 DIGSGNFGVarLMRNKETKELVAVKYIE----RGLKIDENVQREIINH-RSLRHPNIIRF------KEVVLTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGS-VKIGDLGLAtlKNK--- 439
Cdd:cd14662    76 EYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQ--ICHRDLKLENTLLDGSPAPrLKICDFGYS--KSSvlh 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMY-EEMYD-ESVDVYAFGMCLLEMVTGEYPYSECMNPATIyRKVISGVkpecfsrIPAQYPeir 517
Cdd:cd14662   152 SQPKSTVGTPAYIAPEVLsRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDDPKNF-RKTIQRI-------MSVQYK--- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  518 eiIDRCIRVRREERSTVKQLLVDDfftPEDLIGIRvEIKN 557
Cdd:cd14662   221 --IPDYVRVSQDCRHLLSRIFVAN---PAKRITIP-EIKN 254
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
287-484 2.39e-15

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: 79.24  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR--FREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLvtE 364
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhiMAERNVLLKNLKHPFLVGLHYSFQTSE----KLYFVL--D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05603    77 YVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLN--IIYRDLKPENILLD-CQGHVVLTDFGLCKegMEPEETT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  443 KSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05603   154 STFCGTPEYLAPEvLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
281-538 2.86e-15

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK 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: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 78.32  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCEL--QESKLNKTERQrfreEAEMLKDLQ-HPNIVRFYDYW-----ESADL 352
Cdd:cd14036     2 LRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLlsNEEEKNKAIIQ----EINFMKKLSgHPNIVQFCSAAsigkeESDQG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CGKrkyIVLVTELmTSGTLkmyLKRFKRINIKVLKSwCRQILK-------GLSFLHTRNPPVIHRDLKCDNIFItGTTGS 425
Cdd:cd14036    78 QAE---YLLLTEL-CKGQL---VDFVKKVEAPGPFS-PDTVLKifyqtcrAVQHMHKQSPPIIHRDLKIENLLI-GNQGQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  426 VKIGDLGLATL-----------KNKSFAKSVI---GTPEFMAPEMYeEMY-----DESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14036   149 IKLCDFGSATTeahypdyswsaQKRSLVEDEItrnTTPMYRTPEMI-DLYsnypiGEKQDIWALGCILYLLCFRKHPFED 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  487 CMNPATIYRKVIsgvkpecFSRIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14036   228 GAKLRIINAKYT-------IPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
pknD PRK13184
serine/threonine-protein kinase PknD;
287-540 3.36e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.74  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyiVLVTEL 365
Cdd:PRK13184   10 IGKGGMGEVYLAYDPVCSRRVALKKIREDLSeNPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDP-------VYYTMP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSG-TLKMYLKRF-----------KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGL 433
Cdd:PRK13184   83 YIEGyTLKSLLKSVwqkeslskelaEKTSVGAFLSIFHKICATIEYVHSKG--VLHRDLKPDNILL-GLFGEVVILDWGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 ATLKNK--------SFAKS------------VIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPAT 492
Cdd:PRK13184  160 AIFKKLeeedlldiDVDERnicyssmtipgkIVGTPDYMAPErLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  493 IYRKVISG---VKPecFSRIPaqyPEIREIIDRCIRVRREER-STVKQLLVD 540
Cdd:PRK13184  240 SYRDVILSpieVAP--YREIP---PFLSQIAMKALAVDPAERySSVQELKQD 286
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
285-498 3.72e-15

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: 77.62  E-value: 3.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTErQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVTE 364
Cdd:cd14169     9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESP------THLYLAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLkmylkrFKRI------NIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDN-IFITGTTGS-VKIGDLGLATL 436
Cdd:cd14169    82 LVTGGEL------FDRIiergsyTEKDASQLIGQVLQAVKYLH--QLGIVHRDLKPENlLYATPFEDSkIMISDFGLSKI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYP--YSEcmNPATIYRKVI 498
Cdd:cd14169   154 EAQGMLSTACGTPGYVAPELLEQKpYGKAVDVWAIGVISYILLCG-YPpfYDE--NDSELFNQIL 215
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
356-484 4.14e-15

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: 78.45  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLA- 434
Cdd:cd05620    68 KEHLFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKG--IIYRDLKLDNVMLDRD-GHIKIADFGMCk 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  435 -TLKNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05620   145 eNVFGDNRASTFCGTPDYIAPEILQGLkYTFSVDWWSFGVLLYEMLIGQSPF 196
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
287-481 4.95e-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: 78.38  E-value: 4.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkRKYIVLVTELM 366
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISP-----LEDIYFVTELL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 tsGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVi 446
Cdd:cd07856    93 --GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAG--VIHRDLKPSNILVNENC-DLKICDFGLARIQDPQMTGYV- 166
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 392899979  447 GTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07856   167 STRYYRAPEimLTWQKYDVEVDIWSAGCIFAEMLEGK 203
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
393-504 5.04e-15

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: 77.15  E-value: 5.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  393 ILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAtlKNKSF-AKSVIGTPEFMAPEMYEEMYDESVDVYAFG 471
Cdd:cd13975   111 VVEGIRFLHSQG--LVHRDIKLKNVLLD-KKNRAKITDLGFC--KPEAMmSGSIVGTPIHMAPELFSGKYDNSVDVYAFG 185
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392899979  472 MCLLEMVTGE----YPYSECMNPATIYRKVISGVKPE 504
Cdd:cd13975   186 ILFWYLCAGHvklpEAFEQCASKDHLWNNVRKGVRPE 222
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
283-498 5.52e-15

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: 76.99  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  283 FDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLV 362
Cdd:cd14167     7 FREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETS-IENEIAVLHKIKHPNIVALDDIYES------GGHLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLkmylkrFKRINIKVLKS------WCRQILKGLSFLHTRNppVIHRDLKCDNI--FITGTTGSVKIGDLGLA 434
Cdd:cd14167    80 MQLVSGGEL------FDRIVEKGFYTerdaskLIFQILDAVKYLHDMG--IVHRDLKPENLlyYSLDEDSKIMISDFGLS 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  435 TLKNK-SFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGeYP--YSEcmNPATIYRKVI 498
Cdd:cd14167   152 KIEGSgSVMSTACGTPGYVAPEvLAQKPYSKAVDCWSIGVIAYILLCG-YPpfYDE--NDAKLFEQIL 216
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
287-484 6.44e-15

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: 78.20  E-value: 6.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREEAEMLKDLQHPNIVRF-YDYWESADLCgkrkyivLVTE 364
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKILKkEVIIAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQTKDRLC-------FVME 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05593    96 YVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLD-KDGHIKITDFGLCKegITDAATM 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05593   173 KTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPF 215
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
266-543 6.96e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 79.68  E-value: 6.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  266 DAQEKPIDKSKNGRFLKFDEELGRGSFKTVF---RGLDTETGVAVAWCELQEsklnktERQRF--REEAEMLKDLQHPNI 340
Cdd:PTZ00267   54 EGEEVPESNNPREHMYVLTTLVGRNPTTAAFvatRGSDPKEKVVAKFVMLND------ERQAAyaRSELHCLAACDHFGI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  341 VRFYDYWESADlcgkrkYIVLVTELMTSGTLKMYLKR-------FKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLK 413
Cdd:PTZ00267  128 VKHFDDFKSDD------KLLLIMEYGSGGDLNKQIKQrlkehlpFQEYEVGLL---FYQIVLALDEVHSRK--MMHRDLK 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  414 CDNIFITgTTGSVKIGDLGLATLKNKSF----AKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSecm 488
Cdd:PTZ00267  197 SANIFLM-PTGIIKLGDFGFSKQYSDSVsldvASSFCGTPYYLAPELWErKRYSKKADMWSLGVILYELLTLHRPFK--- 272
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  489 NPAT--IYRKVISGVKPECFSRIPAQypeIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:PTZ00267  273 GPSQreIMQQVLYGKYDPFPCPVSSG---MKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
287-481 7.35e-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: 77.41  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTERQRFRE--------EAEMLKDLQHPNIVRFYDYwesadLCGKR-K 357
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVA--------LKKVRMDNERDgipisslrEITLLLNLRHPNIVELKEV-----VVGKHlD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSgTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLA-- 434
Cdd:cd07845    82 SIFLVMEYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENF--IIHRDLKVSNLLLTD-KGCLKIADFGLArt 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 -TLKNKSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07845   158 yGLPAKPMTPKVV-TLWYRAPELLlgCTTYTTAIDMWAVGCILAELLAHK 206
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
281-484 7.55e-15

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 77.41  E-value: 7.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETG----VAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDYWESADlcgkr 356
Cdd:cd05110     9 LKRVKVLGSGAFGTVYKGIWVPEGetvkIPVAIKILNETTGPKANVE-FMDEALIMASMDHPHLVRLLGVCLSPT----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kyIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT 435
Cdd:cd05110    83 --IQLVTQLMPHGCLLDYVHEHKdNIGSQLLLNWCVQIAKGMMYLEERR--LVHRDLAARNVLVK-SPNHVKITDFGLAR 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  436 L---KNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPY 484
Cdd:cd05110   158 LlegDEKEYNADGGKMPiKWMALEcIHYRKFTHQSDVWSYGVTIWELMTfGGKPY 212
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
285-483 7.77e-15

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: 76.62  E-value: 7.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGvavawcELQESKLNKTERQR----FREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYIV 360
Cdd:cd06645    17 QRIGSGTYGDVYKARNVNTG------ELAAIKVIKLEPGEdfavVQQEIIMMKDCKHSNIVAYFGSYL------RRDKLW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpvIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKS 440
Cdd:cd06645    85 ICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGK--MHRDIKGANILLT-DNGHVKLADFGVSAQITAT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  441 FA--KSVIGTPEFMAPEM----YEEMYDESVDVYAFGMCLLEMVTGEYP 483
Cdd:cd06645   162 IAkrKSFIGTPYWMAPEVaaveRKGGYNQLCDIWAVGITAIELAELQPP 210
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
336-484 8.39e-15

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: 77.66  E-value: 8.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  336 QHPNIVRFYDYWESadlcgkRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCD 415
Cdd:cd05619    64 EHPFLTHLFCTFQT------KENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKG--IVYRDLKLD 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  416 NIFITgTTGSVKIGDLGLATLKNKSFAKS--VIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05619   136 NILLD-KDGHIKIADFGMCKENMLGDAKTstFCGTPDYIAPEiLLGQKYNTSVDWWSFGVLLYEMLIGQSPF 206
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
262-483 8.74e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.92  E-value: 8.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  262 EDDFDAQEKPIDKSKNgRFLKFDEELGRGSFKTVFRG--LDTETGVAVAWCeLQESklnkterQRFREEAEMLKDLQHPN 339
Cdd:PTZ00036   50 EDEEKMIDNDINRSPN-KSYKLGNIIGNGSFGVVYEAicIDTSEKVAIKKV-LQDP-------QYKNRELLIMKNLNHIN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  340 IVRFYDYWESADLCGKRKYIVL--VTELMTSgTLKMYLKRFKRIN----IKVLKSWCRQILKGLSFLHTRNppVIHRDLK 413
Cdd:PTZ00036  121 IIFLKDYYYTECFKKNEKNIFLnvVMEFIPQ-TVHKYMKHYARNNhalpLFLVKLYSYQLCRALAYIHSKF--ICHRDLK 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  414 CDNIFITGTTGSVKIGDLGLA-TLKNKSFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGeYP 483
Cdd:PTZ00036  198 PQNLLIDPNTHTLKLCDFGSAkNLLAGQRSVSYICSRFYRAPELMlgATNYTTHIDLWSLGCIIAEMILG-YP 269
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
264-478 8.81e-15

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: 77.79  E-value: 8.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  264 DFDAQEKPIdkskngrflkfdEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRF 343
Cdd:cd07855     2 DVGDRYEPI------------ETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  344 YDYWESADLCGKRKYIVLVTELM---------TSGTLKMYLKRFkrinikvlksWCRQILKGLSFLHTRNppVIHRDLKC 414
Cdd:cd07855    70 RDILRPKVPYADFKDVYVVLDLMesdlhhiihSDQPLTLEHIRY----------FLYQLLRGLKYIHSAN--VIHRDLKP 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  415 DNIFITGtTGSVKIGDLGLA------TLKNKSFAKSVIGTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMV 478
Cdd:cd07855   138 SNLLVNE-NCELKIGDFGMArglctsPEEHKYFMTEYVATRWYRAPELMLSLpeYTQAIDMWSVGCIFAEML 208
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
285-509 9.16e-15

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: 76.50  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQRFREEAEMLKDL-------QHPNIVRFYDYWESADlcgkrk 357
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYA------AKFLKKRRRGQDCRAEILHEIavlelakSNPRVVNLHEVYETTS------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYL--KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGL 433
Cdd:cd14198    82 EIILILEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNN--IVHLDLKPQNILLSSIYplGDIKIVDFGM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 A-TLKNKSFAKSVIGTPEFMAPEM--YEEMyDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRkvISGVK----PECF 506
Cdd:cd14198   160 SrKIGHACELREIMGTPEYLAPEIlnYDPI-TTATDMWNIGVIAYMLLTHESPFVGEDNQETFLN--ISQVNvdysEETF 236

                  ...
gi 392899979  507 SRI 509
Cdd:cd14198   237 SSV 239
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
287-542 1.09e-14

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 76.60  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG----VAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDywesadLCgKRKYIVLV 362
Cdd:cd05109    15 LGSGAFGTVYKGIWIPDGenvkIPVAIKVLRENTSPKANKE-ILDEAYVMAGVGSPYVCRLLG------IC-LTSTVQLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL---KN 438
Cdd:cd05109    87 TQLMPYGCLLDYVRENKdRIGSQDLLNWCVQIAKGMSYLEEVR--LVHRDLAARNVLVKSPN-HVKITDFGLARLldiDE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECmnPATIYRKVISgvKPECFSRIPAQYPE 515
Cdd:cd05109   164 TEYHADGGKVPiKWMALEsILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGI--PAREIPDLLE--KGERLPQPPICTID 239
                         250       260
                  ....*....|....*....|....*..
gi 392899979  516 IREIIDRCIRVRREERSTVKQlLVDDF 542
Cdd:cd05109   240 VYMIMVKCWMIDSECRPRFRE-LVDEF 265
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
287-493 1.09e-14

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 76.53  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAE-MLK--DLQHPNIVRFYDYWESADLcgkrkyiVLVT 363
Cdd:cd05111    15 LGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDhMLAigSLDHAYIVRLLGICPGASL-------QLVT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL---KNK 439
Cdd:cd05111    88 QLLPLGSLLDHVRQHRgSLGPQLLLNWCVQIAKGMYYLEEHR--MVHRNLAARNVLLKSPS-QVQVADFGVADLlypDDK 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  440 SFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATI 493
Cdd:cd05111   165 KYFYSEAKTPiKWMALEsIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAG-MRLAEV 220
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
287-557 1.12e-14

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: 77.23  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIVLVteL 365
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIvSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPE----KLYLVLA--F 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL--KNKSFAK 443
Cdd:cd05585    76 INGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFN--VIYRDLKPENILLD-YTGHIALCDFGLCKLnmKDDDKTN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  444 SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVISGvkpecfsriPAQYPEireiidr 522
Cdd:cd05585   153 TFCGTPEYLAPELLLGHgYTKAVDWWTLGVLLYEMLTGLPPFYD-ENTNEMYRKILQE---------PLRFPD------- 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 392899979  523 ciRVRREERSTVKQLLVDDfftPEDLIGIR--VEIKN 557
Cdd:cd05585   216 --GFDRDAKDLLIGLLNRD---PTKRLGYNgaQEIKN 247
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
287-486 1.29e-14

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: 76.48  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFRE-EAEMLKDLQHPNIVRF-YDYWESADLCgkrkyivLVTE 364
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLaYAFETKTHLC-------LVMS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRF--KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKNKSF 441
Cdd:cd05607    83 LMNGGDLKYHIYNVgeRGIEMERVIFYSAQITCGILHLHSLK--IVYRDMKPENVLLD-DNGNCRLSDLGLAVeVKEGKP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392899979  442 AKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd05607   160 ITQRAGTNGYMAPEiLKEESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
287-481 1.40e-14

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: 76.96  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWcelqeSKLNKTERQ----RFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKyIVLV 362
Cdd:cd07849    13 IGEGAYGMVCSAVHKPTGQKVAI-----KKISPFEHQtyclRTLREIKILLRFKHENIIGILDIQRPPTFESFKD-VYIV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSgtlKMYlkrfkriniKVLKS----------WCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG 432
Cdd:cd07849    87 QELMET---DLY---------KLIKTqhlsndhiqyFLYQILRGLKYIHSAN--VLHRDLKPSNLLLN-TNCDLKICDFG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  433 LATL-----KNKSFAKSVIGTPEFMAPEMyeeM-----YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07849   152 LARIadpehDHTGFLTEYVATRWYRAPEI---MlnskgYTKAIDIWSVGCILAEMLSNR 207
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
287-489 1.53e-14

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: 76.67  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF-----RGLDTETGVAVAwcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcGKrkyIVL 361
Cdd:cd05582     3 LGQGSFGKVFlvrkiTGPDAGTLYAMK--VLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTE---GK---LYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLkmylkrFKRINIKVL------KSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLA- 434
Cdd:cd05582    75 ILDFLRGGDL------FTRLSKEVMfteedvKFYLAELALALDHLHSLG--IIYRDLKPENILLDED-GHIKLTDFGLSk 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  435 -TLKNKSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY-----SECMN 489
Cdd:cd05582   146 eSIDHEKKAYSFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGSLPFqgkdrKETMT 207
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
285-480 1.63e-14

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: 76.27  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR--EEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIVLV 362
Cdd:cd07869    11 EKLGEGSYATVYKGKSKVNGKLVA---LKVIRLQEEEGTPFTaiREASLLKGLKHANIVLLH------DIIHTKETLTLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLK---NK 439
Cdd:cd07869    82 FEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRY--ILHRDLKPQNLLIS-DTGELKLADFGLARAKsvpSH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  440 SFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07869   159 TYSNEVV-TLWYRPPDVLlgSTEYSTCLDMWGVGCIFVEMIQG 200
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
287-484 2.61e-14

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: 76.61  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQ-ESKLNKTERQRFREEAEMLKDLQHPNIVRF-YDYWESADLCgkrkyivLVTE 364
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKkEVIVAKDEVAHTLTENRVLQNSRHPFLTALkYSFQTHDRLC-------FVME 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05594   106 YANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKN-VVYRDLKLENLMLD-KDGHIKITDFGLCKegIKDGATM 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392899979  443 KSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05594   184 KTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPF 226
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
286-477 2.70e-14

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: 75.45  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETG---VAVAWCELQESKlNKTERQRFREEAEM--LKDLQHPNIVRFYDYWeSADLCGKRKYIV 360
Cdd:cd07862     8 EIGEGAYGKVFKARDLKNGgrfVALKRVRVQTGE-EGMPLSTIREVAVLrhLETFEHPNVVRLFDVC-TVSRTDRETKLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSgTLKMYLKRFKRINI--KVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKN 438
Cdd:cd07862    86 LVFEHVDQ-DLTTYLDKVPEPGVptETIKDMMFQLLRGLDFLHSHR--VVHRDLKPQNILVT-SSGQIKLADFGLARIYS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392899979  439 KSFA-KSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEM 477
Cdd:cd07862   162 FQMAlTSVVVTLWYRAPEvLLQSSYATPVDLWSVGCIFAEM 202
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
286-483 2.74e-14

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: 76.24  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd06649    12 ELGAGNGGVVTKVQHKPSGLIMAR-KLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDG------EISICMEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPpVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKSV 445
Cdd:cd06649    85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQ-IMHRDVKPSNILVN-SRGEIKLCDFGVSGQLIDSMANSF 162
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392899979  446 IGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYP 483
Cdd:cd06649   163 VGTRSYMSPERLQgTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
285-477 2.81e-14

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 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: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 75.56  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQEsklnktERQRFREeAEMLKD--LQHPNIVRFYdyweSADL--CGKRKYIV 360
Cdd:cd14143     1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSRE------ERSWFRE-AEIYQTvmLRHENILGFI----AADNkdNGTWTQLW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFkRINIKVLKSWCRQILKGLSFLH-----TRNPPVI-HRDLKCDNIFITgTTGSVKIGDLGLA 434
Cdd:cd14143    70 LVSDYHEHGSLFDYLNRY-TVTVEGMIKLALSIASGLAHLHmeivgTQGKPAIaHRDLKSKNILVK-KNGTCCIADLGLA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  435 tLKNKSFAKSV-------IGTPEFMAPEMYEEMYD-------ESVDVYAFGMCLLEM 477
Cdd:cd14143   148 -VRHDSATDTIdiapnhrVGTKRYMAPEVLDDTINmkhfesfKRADIYALGLVFWEI 203
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
286-531 2.96e-14

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk 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: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 74.61  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRG----LDTETGVAVAWceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgkrkyiVL 361
Cdd:cd05116     2 ELGSGNFGTVKKGyyqmKKVVKTVAVKI--LKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESW-------ML 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL----K 437
Cdd:cd05116    73 VMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESN--FVHRDLAARNVLLV-TQHYAKISDFGLSKAlradE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPaqyP 514
Cdd:cd05116   150 NYYKAQTHGKWPvKWYAPEcMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKG-MKGNEVTQMIEKGERMECPAGCP---P 225
                         250
                  ....*....|....*..
gi 392899979  515 EIREIIDRCIRVRREER 531
Cdd:cd05116   226 EMYDLMKLCWTYDVDER 242
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
281-538 3.04e-14

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 75.04  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGlDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIV 360
Cdd:cd14153     2 LEIGELIGKGRFGQVYHG-RWHGEVAIRLIDIERD--NEEQLKAFKREVMAYRQTRHENVVLF------MGACMSPPHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRI-NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgtTGSVKIGDLGLATL--- 436
Cdd:cd14153    73 IITSLCKGRTLYSVVRDAKVVlDVNKTRQIAQEIVKGMGYLHAKG--ILHKDLKSKNVFYD--NGKVVITDFGLFTIsgv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 ----KNKSFAKSVIGTPEFMAPEMYEEM----------YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrKVISGVK 502
Cdd:cd14153   149 lqagRREDKLRIQSGWLCHLAPEIIRQLspeteedklpFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIW-QVGSGMK 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  503 PEcFSRIpAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14153   228 PN-LSQI-GMGKEISDILLFCWAYEQEERPTFSKLM 261
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
287-538 3.04e-14

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: 74.62  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTERQRFREEAEMLKDLQHP--------------NIVRFYDYWESAD- 351
Cdd:cd14100     8 LGSGGFGSVYSGIRVADGAPVA--------IKHVEKDRVSEWGELPNGTRVPmeivllkkvgsgfrGVIRLLDWFERPDs 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  352 --LCGKRKYIV--LVTELMTSGTLKMYLKRfkrinikvlkSWCRQILKGLSflHTRNPPVIHRDLKCDNIFITGTTGSVK 427
Cdd:cd14100    80 fvLVLERPEPVqdLFDFITERGALPEELAR----------SFFRQVLEAVR--HCHNCGVLHRDIKDENILIDLNTGELK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  428 IGDLGLATLKNKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPY---SECMNPATIYRKVISgvk 502
Cdd:cd14100   148 LIDFGSGALLKDTVYTDFDGTRVYSPPEwiRFHRYHGRSAAVWSLGILLYDMVCGDIPFehdEEIIRGQVFFRQRVS--- 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  503 PECfsripaqypeiREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14100   225 SEC-----------QHLIKWCLALRPSDRPSFEDIQ 249
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
279-538 3.13e-14

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: 75.02  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFlKFDEELGRGSFKTVFRGLDTETGVAVAW----CELQESklnkteRQRFREEAEMLKDLQHPNIVRFYDYwESADLCG 354
Cdd:cd13986     1 RY-RIQRLLGEGGFSFVYLVEDLSTGRLYALkkilCHSKED------VKEAMREIENYRLFNHPNILRLLDS-QIVKEAG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKMYLKRFK----RINIKVLKSWCRQILKGLSFLHTRNP-PVIHRDLKCDNIFITGTTGSVkIG 429
Cdd:cd13986    73 GKKEVYLLLPYYKRGSLQDEIERRLvkgtFFPEDRILHIFLGICRGLKAMHEPELvPYAHRDIKPGNVLLSEDDEPI-LM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  430 DLGLAT-----LKNKSFAKSVI------GTPEFMAPEMYE----EMYDESVDVYAFGMCLLEMVTGEYPYS-ECMNPATI 493
Cdd:cd13986   152 DLGSMNparieIEGRREALALQdwaaehCTMPYRAPELFDvkshCTIDEKTDIWSLGCTLYALMYGESPFErIFQKGDSL 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  494 YRKVISGVKPecFSRIPAQYPEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd13986   232 ALAVLSGNYS--FPDNSRYSEELHQLVKSMLVVNPAERPSIDDLL 274
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
285-478 4.10e-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: 74.87  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTER----QRFREEAEMLKDLQHPNIVRFYDYwESADLCGKrKYIV 360
Cdd:cd07837     7 EKIGEGTYGKVYKARDKNTGKLVA---LKKTRLEMEEEgvpsTALREVSLLQMLSQSIYIVRLLDV-EHVEENGK-PLLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSgTLKMYLKRFKR-----INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLA- 434
Cdd:cd07837    82 LVFEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHG--VMHRDLKPQNLLVDKQKGLLKIADLGLGr 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  435 --TLKNKSFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMV 478
Cdd:cd07837   159 afTIPIKSYTHEIV-TLWYRAPEVLlgSTHYSTPVDMWSVGCIFAEMS 205
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
279-538 4.30e-14

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: 74.94  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTV----FRGLDTETGVAVAWCELQeSKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcG 354
Cdd:cd05080     4 RYLKKIRDLGEGHFGKVslycYDPTNDGTGEMVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSE----Q 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKMYLKRFKrINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLA 434
Cdd:cd05080    79 GGKSLQLIMEYVPLGSLRDYLPKHS-IGLAQLLLFAQQICEGMAYLHSQH--YIHRDLAARNVLLDNDR-LVKIGDFGLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TL---KNKSFAKSVIG-TPEF-MAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYsecMNPATIYRKVIsGVKPECFSR 508
Cdd:cd05080   155 KAvpeGHEYYRVREDGdSPVFwYAPEcLKEYKFYYASDVWSFGVTLYELLTHCDSS---QSPPTKFLEMI-GIAQGQMTV 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  509 I--------------PAQYP-EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05080   231 VrliellergerlpcPDKCPqEVYHLMKNCWETEASFRPTFENLI 275
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
286-478 5.43e-14

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: 75.29  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFR-EEAEMLKDLQ--HPNIVRFYD----------------- 345
Cdd:cd13977     7 EVGRGSYGVVYEAVVRRTGARVA---VKKIRCNAPENVELAlREFWALSSIQrqHPNVIQLEEcvlqrdglaqrmshgss 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  346 ----YWESADLCGKRK---------YIVLVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHtRNPpVIHRDL 412
Cdd:cd13977    84 ksdlYLLLVETSLKGErcfdprsacYLWFVMEFCDGGDMNEYLLS-RRPDRQTNTSFMLQLSSALAFLH-RNQ-IVHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  413 KCDNIFITGTTGS--VKIGDLGLATL-------------KNKSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEM 477
Cdd:cd13977   161 KPDNILISHKRGEpiLKVADFGLSKVcsgsglnpeepanVNKHFLSSACGSDFYMAPEVWEGHYTAKADIFALGIIIWAM 240

                  .
gi 392899979  478 V 478
Cdd:cd13977   241 V 241
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
315-486 5.44e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 74.74  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  315 SKLNKTER----QRFREEAEMLKDLQHPNIVRFYDYWESAD--LCGKRKYivLVTELMTSGTLKMYLKRFKRINIKVLK- 387
Cdd:cd14001    38 SKCDKGQRslyqERLKEEAKILKSLNHPNIVGFRAFTKSEDgsLCLAMEY--GGKSLNDLIEERYEAGLGPFPAATILKv 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  388 SWcrQILKGLSFLHTrNPPVIHRDLKCDNIFITGTTGSVKIGDLGLA-TLKNKSFAKS-----VIGTPEFMAPEMYEEMY 461
Cdd:cd14001   116 AL--SIARALEYLHN-EKKILHGDIKSGNVLIKGDFESVKLCDFGVSlPLTENLEVDSdpkaqYVGTEPWKAKEALEEGG 192
                         170       180
                  ....*....|....*....|....*..
gi 392899979  462 DES--VDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd14001   193 VITdkADIFAYGLVLWEMMTLSVPHLN 219
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
284-484 5.71e-14

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: 74.68  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAwCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESaDLCgkrkyIVLVT 363
Cdd:cd14174     7 DELLGEGAYAKVQGCVSLQNGKEYA-VKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFED-DTR-----FYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGT--TGSVKIGDLGLATLKNKSF 441
Cdd:cd14174    80 EKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKG--IAHRDLKPENILCESPdkVSPVKICDFDLGSGVKLNS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  442 AKSVIGTPE---------FMAPEMYE------EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14174   158 ACTPITTPElttpcgsaeYMAPEVVEvftdeaTFYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
287-523 5.78e-14

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: 74.08  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTERQRFR-EEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVTEL 365
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCA--------VKKVRLEVFRaEELMACAGLTSPRVVPLYGAVREG------PWVNIFMDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLA-TLKNKSFAKS 444
Cdd:cd13991    80 KEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRK--ILHGDVKADNVLLSSDGSDAFLCDFGHAeCLDPDGLGKS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  445 VI------GTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSECMNpatiyrkvisgvKPECFsRIPAQYPEIR 517
Cdd:cd13991   158 LFtgdyipGTETHMAPEVVLgKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYS------------GPLCL-KIANEPPPLR 224

                  ....*.
gi 392899979  518 EIIDRC 523
Cdd:cd13991   225 EIPPSC 230
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
287-538 5.90e-14

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: 73.83  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLnKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELM 366
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKL-KGKEDMIESEILIIKSLSHPNIVKLFEVYET------EKEIYLILEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLK---RFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITGT---TGSVKIGDLGLATLKNKS 440
Cdd:cd14185    81 RGGDLFDAIIesvKFTEHDAALM---IIDLCEALVYIHSKH--IVHRDLKPENLLVQHNpdkSTTLKLADFGLAKYVTGP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAkSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY-SECMNPATIYRKVISG---VKPECFSRIPAqypE 515
Cdd:cd14185   156 IF-TVCGTPTYVAPEILSEKgYGLEVDMWAAGVILYILLCGFPPFrSPERDQEELFQIIQLGhyeFLPPYWDNISE---A 231
                         250       260
                  ....*....|....*....|...
gi 392899979  516 IREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14185   232 AKDLISRLLVVDPEKRYTAKQVL 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
321-485 6.47e-14

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: 73.86  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  321 ERQRFREEAEM-LKDLQHPNIVRFYDYWESADlcGKRKYIVLVTELMTSGTLkmylkrFKRINIKVLKSWC--------R 391
Cdd:cd14089    36 DNPKARREVELhWRASGCPHIVRIIDVYENTY--QGRKCLLVVMECMEGGEL------FSRIQERADSAFTereaaeimR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  392 QILKGLSFLHTRNppVIHRDLKCDNIFITGTT--GSVKIGDLGlatlknksFAKSVIG---------TPEFMAPEMYE-E 459
Cdd:cd14089   108 QIGSAVAHLHSMN--IAHRDLKPENLLYSSKGpnAILKLTDFG--------FAKETTTkkslqtpcyTPYYVAPEVLGpE 177
                         170       180
                  ....*....|....*....|....*...
gi 392899979  460 MYDESVDVYAFGMCLLEMVTGeYP--YS 485
Cdd:cd14089   178 KYDKSCDMWSLGVIMYILLCG-YPpfYS 204
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
328-510 7.57e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 75.30  E-value: 7.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  328 EAEMLKDLQHPNIVRFYDYWESADLcgkrkyIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppV 407
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAI------TCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQR--I 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  408 IHRDLKCDNIFITgTTGSVKIGDLGLATLK-NKSFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTgeYPYS 485
Cdd:PHA03209  179 IHRDVKTENIFIN-DVDQVCIGDLGAAQFPvVAPAFLGLAGTVETNAPEvLARDKYNSKADIWSAGIVLFEMLA--YPST 255
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392899979  486 ECMNPATI-----------YRKVIS--GVKPECFSRIP 510
Cdd:PHA03209  256 IFEDPPSTpeeyvkschshLLKIIStlKVHPEEFPRDP 293
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
338-484 8.58e-14

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: 74.65  E-value: 8.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  338 PNIVRFYDYWESADlcgkRKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI 417
Cdd:cd05616    61 PFLTQLHSCFQTMD----RLYFVM--EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKG--IIYRDLKLDNV 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 FITgTTGSVKIGDLGLA--TLKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05616   133 MLD-SEGHIKIADFGMCkeNIWDGVTTKTFCGTPDYIAPEIIAyQPYGKSVDWWAFGVLLYEMLAGQAPF 201
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
281-484 9.64e-14

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 73.84  E-value: 9.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTE-------TGVAVawcELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLC 353
Cdd:cd05045     2 LVLGKTLGEGEFGKVVKATAFRlkgragyTTVAV---KMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYG------AC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLKRFKRI------------------------NIKVLKSWCRQILKGLSFLHTRNppVIH 409
Cdd:cd05045    73 SQDGPLLLIVEYAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnpderalTMGDLISFAWQISRGMQYLAEMK--LVH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  410 RDLKCDNIFItGTTGSVKIGDLGLA--TLKNKSFAKSVIG-TP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYP 483
Cdd:cd05045   151 RDLAARNVLV-AEGRKMKISDFGLSrdVYEEDSYVKRSKGrIPvKWMAIEsLFDHIYTTQSDVWSFGVLLWEIVTlGGNP 229

                  .
gi 392899979  484 Y 484
Cdd:cd05045   230 Y 230
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
279-498 1.08e-13

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: 73.93  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLnKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkY 358
Cdd:cd14168    10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAL-KGKESSIENEIAVLRKIKHENIVALEDIYESPN------H 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLkmylkrFKRI------NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI--FITGTTGSVKIGD 430
Cdd:cd14168    83 LYLVMQLVSGGEL------FDRIvekgfyTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLlyFSQDEESKIMISD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLATLKNK-SFAKSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYRKVI 498
Cdd:cd14168   155 FGLSKMEGKgDVMSTACGTPGYVAPEvLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEQIL 223
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
287-484 1.18e-13

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: 73.54  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwCElqesKLNKTERQRFREEA------EMLKDLQHPNIVRFYDYWESAD-LCgkrkyi 359
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYA-CK----KLEKKRIKKRKGEAmalnekQILEKVNSRFVVSLAYAYETKDaLC------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 vLVTELMTSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-L 436
Cdd:cd05605    77 -LVLTIMNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSER--IVYRDLKPENILLD-DHGHVRISDLGLAVeI 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05605   153 PEGETIRGRVGTVGYMAPEVVKnERYTFSPDWWGLGCLIYEMIEGQAPF 201
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
287-484 1.19e-13

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: 74.26  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGvavawcELQESKLNKTERQRFREEAEML----------KDLQHPNIVRFYDYWESADlcgkr 356
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTG------ELFAIKALKKGDIIARDEVESLmcekrifetvNSARHPFLVNLFACFQTPE----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kYIVLVTELMTSGTLKMYLKR--FKRINiKVLKSWCrqILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA 434
Cdd:cd05589    76 -HVCFVMEYAAGGDLMMHIHEdvFSEPR-AVFYAAC--VVLGLQFLHEHK--IVYRDLKLDNLLLD-TEGYVKIADFGLC 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  435 ------TLKNKSFAksviGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05589   149 kegmgfGDRTSTFC----GTPEFLAPEvLTDTSYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
285-481 1.26e-13

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: 74.22  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTE 364
Cdd:cd07880    21 KQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFYLVMP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMtsGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKS 444
Cdd:cd07880   101 FM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAG--IIHRDLKPGNLAVNEDC-ELKILDFGLARQTDSEMTGY 175
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392899979  445 VIgTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07880   176 VV-TRWYRAPEVILNWmhYTQTVDIWSVGCIMAEMLTGK 213
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
287-522 1.46e-13

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: 73.19  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGL-------DTETGVAVAwcELQESKLNKTERQrFREEAEMLKDLQHPNIVRFydywesADLCGKRK-- 357
Cdd:cd05036    14 LGQGAFGEVYEGTvsgmpgdPSPLQVAVK--TLPELCSEQDEMD-FLMEALIMSKFNHPNIVRC------IGVCFQRLpr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLvtELMTSGTLKMYLK-------RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGS---VK 427
Cdd:cd05036    85 FILL--ELMAGGDLKSFLRenrprpeQPSSLTMLDLLQLAQDVAKGCRYLEENH--FIHRDIAARNCLLT-CKGPgrvAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  428 IGDLGLA-TLKNKSF----AKSVIgtP-EFMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPY-----SECMN----- 489
Cdd:cd05036   160 IGDFGMArDIYRADYyrkgGKAML--PvKWMPPEAFLDgIFTSKTDVWSFGVLLWEIFSlGYMPYpgksnQEVMEfvtsg 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392899979  490 ---------PATIYRkvisgVKPECFSRIPAQYPEIREIIDR 522
Cdd:cd05036   238 grmdppkncPGPVYR-----IMTQCWQHIPEDRPNFSTILER 274
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
285-486 2.03e-13

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 72.62  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGlDTETGVAVAWC---ELQESKlNKTERQRFREEAEMLKDLQHPNIVrfydywESADLCGKRKYIVL 361
Cdd:cd05042     1 QEIGNGWFGKVLLG-EIYSGTSVAQVvvkELKASA-NPKEQDTFLKEGQPYRILQHPNIL------QCLGQCVEAIPYLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLkRFKRI------NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT 435
Cdd:cd05042    73 VMEFCDLGDLKAYL-RSEREhergdsDTRTLQRMACEVAAGLAHLHKLN--FVHSDLALRNCLLTSDL-TVKIGDYGLAH 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  436 LKNKsfaKSVIGTPE-------FMAPEMYEEMYD--------ESVDVYAFGMCLLEMVT-GEYPYSE 486
Cdd:cd05042   149 SRYK---EDYIETDDklwfplrWTAPELVTEFHDrllvvdqtKYSNIWSLGVTLWELFEnGAQPYSN 212
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
277-537 2.27e-13

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: 71.94  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLKFDEELGRGSFKTVFRGLDTETGVAVAWCElqesklNKTERQRFREEAEMLKDLQHPNIVRFYDYwesadLCGKR 356
Cdd:cd05082     4 NMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIK------NDATAQAFLAEASVMTQLRHSNLVQLLGV-----IVEEK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTELMTSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA 434
Cdd:cd05082    73 GGLYIVTEYMAKGSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNN--FVHRDLAARNVLVS-EDNVAKVSDFGLT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 tlKNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVISGVKPECFSRIPa 511
Cdd:cd05082   150 --KEASSTQDTGKLPvKWTAPEaLREKKFSTKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPRVEKGYKMDAPDGCP- 225
                         250       260
                  ....*....|....*....|....*.
gi 392899979  512 qyPEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05082   226 --PAVYDVMKNCWHLDAAMRPSFLQL 249
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
290-481 2.31e-13

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: 72.64  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  290 GSFKTVFRGLDTETGVAVAwceLQESKLNKtERQRF-----REeAEMLKDLQHPNIVRFYDYwesadLCGKR-KYIVLVT 363
Cdd:cd07843    16 GTYGVVYRARDKKTGEIVA---LKKLKMEK-EKEGFpitslRE-INILLKLQHPNIVTVKEV-----VVGSNlDKIYMVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSgTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL---KNK 439
Cdd:cd07843    86 EYVEH-DLKSLMETMKqPFLQSEVKCLMLQLLSGVAHLHDNW--ILHRDLKTSNLLLN-NRGILKICDFGLAREygsPLK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392899979  440 SFAKSVIgTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07843   162 PYTQLVV-TLWYRAPELLlgAKEYSTAIDMWSVGCIFAELLTKK 204
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
282-452 2.33e-13

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: 72.10  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETG--VAVawcelqesKL--NKTERQRFREEAEMLKDLQ-HPNIVRFYDYWESADlcgkr 356
Cdd:cd14016     3 KLVKKIGSGSFGEVYLGIDLKTGeeVAI--------KIekKDSKHPQLEYEAKVYKLLQgGPGIPRLYWFGQEGD----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 kYIVLVTELMtsGT-----LKMYLKRFkrinikVLKSWCR---QILKGLSFLHTRNppVIHRDLKCDNiFITGTTGSVK- 427
Cdd:cd14016    70 -YNVMVMDLL--GPsledlFNKCGRKF------SLKTVLMladQMISRLEYLHSKG--YIHRDIKPEN-FLMGLGKNSNk 137
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 392899979  428 --IGDLGLA-------TLKNKSFA--KSVIGTPEFM 452
Cdd:cd14016   138 vyLIDFGLAkkyrdprTGKHIPYRegKSLTGTARYA 173
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
288-543 2.53e-13

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: 72.35  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  288 GRGSFKTVFRGLDTETG--VAVAWCEL-QESKLNKTERQRF----REEAEMLKDLQHPNIVRFYDYWESADLCgkrkyIV 360
Cdd:cd14011     5 GPGLPWKIYNGSKKSTKqeVSVFVFEKkQLEEYSKRDREQIlellKRGVKQLTRLRHPRILTVQHPLEESRES-----LA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTsGTLKMYLKrfKRINIKVLKSWCR--------------QILKGLSFLHTRNpPVIHRDLKCDNIFITgTTGSV 426
Cdd:cd14011    80 FATEPVF-ASLANVLG--ERDNMPSPPPELQdyklydveikygllQISEALSFLHNDV-KLVHGNICPESVVIN-SNGEW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  427 KIGDLGLAtLKNKSFAK--------------SVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPA 491
Cdd:cd14011   155 KLAGFDFC-ISSEQATDqfpyfreydpnlppLAQPNLNYLAPEyILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNL 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  492 TIYRKVISGV---KPECFSRIPAqypEIREIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14011   234 LSYKKNSNQLrqlSLSLLEKVPE---ELRDHVKTLLNVTPEVRPDAEQLSKIPFF 285
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
287-513 2.59e-13

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: 73.54  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIENFNEVYLVTNLM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 tsGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVi 446
Cdd:cd07878   103 --GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAG--IIHRDLKPSNVAVNEDC-ELRILDFGLARQADDEMTGYV- 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  447 GTPEFMAPE-MYEEM-YDESVDVYAFGMCLLEMVTGE--YPYSECMNPATIYRKVISGVKPECFSRIPAQY 513
Cdd:cd07878   177 ATRWYRAPEiMLNWMhYNQTVDIWSVGCIMAELLKGKalFPGNDYIDQLKRIMEVVGTPSPEVLKKISSEH 247
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
281-538 2.69e-13

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 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: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 72.31  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGlDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIV 360
Cdd:cd14152     2 IELGELIGQGRWGKVHRG-RWHGEVAIRLLEIDGN--NQDHLKLFKKEVMNYRQTRHENVVLF------MGACMHPPHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgtTGSVKIGDLGLATL--- 436
Cdd:cd14152    73 IITSFCKGRTLYSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLFGIsgv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 ----KNKSFAKSVIGTPEFMAPEMYEEM----------YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYrKVISGvk 502
Cdd:cd14152   149 vqegRRENELKLPHDWLCYLAPEIVREMtpgkdedclpFSKAADVYAFGTIWYELQARDWPLKNQPAEALIW-QIGSG-- 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  503 pECFSRIPAQYP---EIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14152   226 -EGMKQVLTTISlgkEVTEILSACWAFDLEERPSFTLLM 263
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
285-477 3.19e-13

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 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: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 72.47  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVawcelqesKL--NKTERQRFREeAEMLKD--LQHPNIVRFYdyweSADLCGKRK--Y 358
Cdd:cd14142    11 ECIGKGRYGEVWRGQWQGESVAV--------KIfsSRDEKSWFRE-TEIYNTvlLRHENILGFI----ASDMTSRNSctQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTR------NPPVIHRDLKCDNIFITGtTGSVKIGDLG 432
Cdd:cd14142    78 LWLITHYHENGSLYDYLQR-TTLDHQEMLRLALSAASGLVHLHTEifgtqgKPAIAHRDLKSKNILVKS-NGQCCIADLG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  433 LATLKNKSFAK------SVIGTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEM 477
Cdd:cd14142   156 LAVTHSQETNQldvgnnPRVGTKRYMAPEVLDETINTDcfesykrVDIYAFGLVLWEV 213
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
287-489 3.28e-13

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). 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. 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 EphA2 subfamily 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).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 71.93  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR--FREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTE 364
Cdd:cd05063    13 IGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRqdFLSEASIMGQFSHHNIIRL------EGVVTKFKPAMIITE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLK----RFKRINikvLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATL---- 436
Cdd:cd05063    87 YMENGALDKYLRdhdgEFSSYQ---LVGMLRGIAAGMKYLSDMN--YVHRDLAARNILVNSNL-ECKVSDFGLSRVledd 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  437 KNKSFAKSVIGTP-EFMAPEM--YEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMN 489
Cdd:cd05063   161 PEGTYTTSGGKIPiRWTAPEAiaYRKFTSAS-DVWSFGIVMWEVMSfGERPYWDMSN 216
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
279-519 3.33e-13

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC 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 TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 72.35  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTVFRG-----LDTETGVAVAWCELQESKLnkTERQRFREEAEMLKDLQHPNIVRFYdywesaDLC 353
Cdd:cd05094     5 RDIVLKRELGEGAFGKVFLAecynlSPTKDKMLVAVKTLKDPTL--AARKDFQREAELLTNLQHDHIVKFY------GVC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLKRF----------------KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI 417
Cdd:cd05094    77 GDGDPLIMVFEYMKHGDLNKFLRAHgpdamilvdgqprqakGELGLSQMLHIATQIASGMVYLASQH--FVHRDLATRNC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 FItGTTGSVKIGDLGLATLKNKSFAKSVIGTP----EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPY------ 484
Cdd:cd05094   155 LV-GANLLVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMYRKFTTES-DVWSFGVILWEIFTyGKQPWfqlsnt 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 392899979  485 --SECMNPATIYR------KVISGVKPECFSRIPAQYPEIREI 519
Cdd:cd05094   233 evIECITQGRVLErprvcpKEVYDIMLGCWQREPQQRLNIKEI 275
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
278-475 3.70e-13

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: 71.93  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  278 GRF-LKFDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLN-KTERQRFREEAEMLKDLQ-HPNIVRFYDYweSADLCG 354
Cdd:cd14037     1 GSHhVTIEKYLAEGGFAHVYLVKTSNGGNRAA---LKRVYVNdEHDLNVCKREIEIMKRLSgHKNIVGYIDS--SANRSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLV-TELMTSGTLKMYLKrfKRINIK-----VLKSWCrQILKGLSFLHTRNPPVIHRDLKCDNIFITgTTGSVKI 428
Cdd:cd14037    76 NGVYEVLLlMEYCKGGGVIDLMN--QRLQTGlteseILKIFC-DVCEAVAAMHYLKPPLIHRDLKVENVLIS-DSGNYKL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  429 GDLGLATLKNKS--------FAKSVI---GTPEFMAPEMYE----EMYDESVDVYAFGmCLL 475
Cdd:cd14037   152 CDFGSATTKILPpqtkqgvtYVEEDIkkyTTLQYRAPEMIDlyrgKPITEKSDIWALG-CLL 212
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
264-501 3.79e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 72.71  E-value: 3.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  264 DFDAQEKPIDKSK-NGRFLKFDEELGRGSF-KTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNI 340
Cdd:PTZ00426   14 DSDSTKEPKRKNKmKYEDFNFIRTLGTGSFgRVILATYKNEDFPPVAIKRFEKSKIIKQKQvDHVFSERKILNYINHPFC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  341 VRFYDYWESadlcgkRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT 420
Cdd:PTZ00426   94 VNLYGSFKD------ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLN--IVYRDLKPENLLLD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  421 gTTGSVKIGDLGLATLKNkSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSeCMNPATIYRKVIS 499
Cdd:PTZ00426  166 -KDGFIKMTDFGFAKVVD-TRTYTLCGTPEYIAPEILLNVgHGKAADWWTLGIFIYEILVGCPPFY-ANEPLLIYQKILE 242

                  ..
gi 392899979  500 GV 501
Cdd:PTZ00426  243 GI 244
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
281-538 3.91e-13

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. 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. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR 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: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 71.63  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR--FREEAEMLKDLQHPNIVRFYdywesaDLCGKRKY 358
Cdd:cd05033     6 VTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRldFLTEASIMGQFDHPNVIRLE------GVVTKSRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLA-TL 436
Cdd:cd05033    80 VMIVTEYMENGSLDKFLRENDgKFTVTQLVGMLRGIASGMKYLSEMN--YVHRDLAARNILVNSDL-VCKVSDFGLSrRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIG--TP-EFMAPEMYE-EMYDESVDVYAFGMCLLE-MVTGEYPYSECMNpatiyRKVISGVkpECFSRIPA 511
Cdd:cd05033   157 EDSEATYTTKGgkIPiRWTAPEAIAyRKFTSASDVWSFGIVMWEvMSYGERPYWDMSN-----QDVIKAV--EDGYRLPP 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  512 qyPE-----IREIIDRCIRVRREERSTVKQLL 538
Cdd:cd05033   230 --PMdcpsaLYQLMLDCWQKDRNERPTFSQIV 259
PHA02988 PHA02988
hypothetical protein; Provisional
325-538 3.94e-13

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 71.70  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  325 FREEAEMLKDLQHPNIVRFYDYWesADLCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTR- 403
Cdd:PHA02988   65 TENEIKNLRRIDSNNILKIYGFI--IDIVDDLPRLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYKYt 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  404 NPPviHRDLKCDNIFITGTtGSVKIGDLGL-ATLKNKSFAKsvIGTPEFMAPEMYEEM---YDESVDVYAFGMCLLEMVT 479
Cdd:PHA02988  143 NKP--YKNLTSVSFLVTEN-YKLKIICHGLeKILSSPPFKN--VNFMVYFSYKMLNDIfseYTIKDDIYSLGVVLWEIFT 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  480 GEYPYsECMNPATIYRKVISGVKPEcfsRIPAQYP-EIREIIDRCIRVRREERSTVKQLL 538
Cdd:PHA02988  218 GKIPF-ENLTTKEIYDLIINKNNSL---KLPLDCPlEIKCIVEACTSHDSIKRPNIKEIL 273
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
323-505 4.25e-13

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: 71.18  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  323 QRF-REEAEMLKDLQHPNIVRFYDYWESADlcGKrkyIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLH 401
Cdd:cd14163    44 QRFlPRELQIVERLDHKNIIHVYEMLESAD--GK---IYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  402 TRNppVIHRDLKCDNIFITGTTgsVKIGDLGLATL---KNKSFAKSVIGTPEFMAPEMYEEMYDESV--DVYAFGMCLLE 476
Cdd:cd14163   119 GCG--VAHRDLKCENALLQGFT--LKLTDFGFAKQlpkGGRELSQTFCGSTAYAAPEVLQGVPHDSRkgDIWSMGVVLYV 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 392899979  477 MVTGEYPYSECMNPATIY--RKVIS-----GVKPEC 505
Cdd:cd14163   195 MLCAQLPFDDTDIPKMLCqqQKGVSlpghlGVSRTC 230
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
284-484 4.40e-13

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: 71.98  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFR--GLDTETGVAVAWCELQESKLnkteRQRFREEAEMLKDLQ-HPNIVRFYDYWESADlcgkRKYiv 360
Cdd:cd14173     7 EEVLGEGAYARVQTciNLITNKEYAVKIIEKRPGHS----RSRVFREVEMLYQCQgHRNVLELIEFFEEED----KFY-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNIFI--TGTTGSVKIGDLGLATLKN 438
Cdd:cd14173    77 LVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLH--NKGIAHRDLKPENILCehPNQVSPVKICDFDLGSGIK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899979  439 KSFAKSVIGTPE---------FMAPEMYE------EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14173   155 LNSDCSPISTPElltpcgsaeYMAPEVVEafneeaSIYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
287-552 6.65e-13

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: 72.73  E-value: 6.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFK--TVFRGLDTETGVAVAWCELQEsKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd05624    80 IGRGAFGevAVVKMKNTERIYAMKILNKWE-MLKRAETACFREERNVLVNGDCQWITTLHYAFQDEN------YLYLVMD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG--LATLKNKSF 441
Cdd:cd05624   153 YYVGGDLLTLLSKFEdKLPEDMARFYIGEMVLAIHSIHQLH--YVHRDIKPDNVLLD-MNGHIRLADFGscLKMNDDGTV 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  442 AKSV-IGTPEFMAPEMYEEM------YDESVDVYAFGMCLLEMVTGEYP-YSECMnpATIYRKVISGVKPECF-SRIPAQ 512
Cdd:cd05624   230 QSSVaVGTPDYISPEILQAMedgmgkYGPECDWWSLGVCMYEMLYGETPfYAESL--VETYGKIMNHEERFQFpSHVTDV 307
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 392899979  513 YPEIREIIDR--CIRVRREERSTVKQLLVDDFFTPEDLIGIR 552
Cdd:cd05624   308 SEEAKDLIQRliCSRERRLGQNGIEDFKKHAFFEGLNWENIR 349
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
287-484 6.87e-13

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: 71.75  E-value: 6.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTV----FRGLDTETGVAVAWCE--LQESKLNKTerqrFREEAEMLKDLQHPNIVRFYDYWESADlcgkRKYIV 360
Cdd:cd05591     3 LGKGSFGKVmlaeRKGTDEVYAIKVLKKDviLQDDDVDCT----MTEKRILALAAKHPFLTALHSCFQTKD----RLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKN 438
Cdd:cd05591    75 M--EYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHG--VIYRDLKLDNILLD-AEGHCKLADFGMCKegILN 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  439 KSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05591   150 GKTTTTFCGTPDYIAPEILQELeYGPSVDWWALGVLMYEMMAGQPPF 196
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
287-502 7.52e-13

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: 71.75  E-value: 7.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQE-SKLNKTERQRfrEEAEMLKDLQHPNIVRFYDYWEsaDLCGKRKyiVLVTEL 365
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDVQM--REFEVLKKLNHKNIVKLFAIEE--ELTTRHK--VLVMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRIN-------IKVLkswcRQILKGLSflHTRNPPVIHRDLKCDNI--FITGTTGSV-KIGDLGLAT 435
Cdd:cd13988    75 CPCGSLYTVLEEPSNAYglpesefLIVL----RDVVAGMN--HLRENGIVHRDIKPGNImrVIGEDGQSVyKLTDFGAAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 --LKNKSFAkSVIGTPEFMAPEMYE---------EMYDESVDVYAFGMCLLEMVTGEYPYSEC----MNPATIYR----- 495
Cdd:cd13988   149 elEDDEQFV-SLYGTEEYLHPDMYEravlrkdhqKKYGATVDLWSIGVTFYHAATGSLPFRPFegprRNKEVMYKiitgk 227

                  ....*....
gi 392899979  496 --KVISGVK 502
Cdd:cd13988   228 psGAISGVQ 236
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
302-481 8.60e-13

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 74.11  E-value: 8.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   302 ETGVAVAWCELQESKLNKT-ERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrKYIVLVTELMTSGTLKMYLKRFKR 380
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEhQRARFRRETALCARLYHPNIVALLDSGEAPP-----GLLFAVFEYVPGRTLREVLAADGA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979   381 INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI--TGTTGSVKIGDLGLATL---------KNKSFAKSVIGTP 449
Cdd:TIGR03903   76 LPAGETGRLMLQVLDALACAHNQG--IVHRDLKPQNIMVsqTGVRPHAKVLDFGIGTLlpgvrdadvATLTRTTEVLGTP 153
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 392899979   450 EFMAPemyEEMYDESV----DVYAFGMCLLEMVTGE 481
Cdd:TIGR03903  154 TYCAP---EQLRGEPVtpnsDLYAWGLIFLECLTGQ 186
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
281-521 9.30e-13

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They 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, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. 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. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 70.91  E-value: 9.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLDTETGVAVAwCELQESKLNKTERQ--RFREEAEMLKDL-QHPNIVRFYDywesadLC 353
Cdd:cd05053    14 LTLGKPLGEGAFGQVVKaeavGLDNKPNEVVT-VAVKMLKDDATEKDlsDLVSEMEMMKMIgKHKNIINLLG------AC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLKR----------------FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI 417
Cdd:cd05053    87 TQDGPLYVVVEYASKGNLREFLRArrppgeeaspddprvpEEQLTQKDLVSFAYQVARGMEYLASKK--CIHRDLAARNV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 FITgtTGSV-KIGDLGLA--TLKNKSFAKSVIGT-P-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPY------ 484
Cdd:cd05053   165 LVT--EDNVmKIADFGLArdIHHIDYYRKTTNGRlPvKWMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlGGSPYpgipve 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  485 --------SECMNPATIYRKVISGVKPECFSRIPAQYPEIREIID 521
Cdd:cd05053   243 elfkllkeGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
281-540 1.54e-12

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: 69.87  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG---LDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRK 357
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAqlkQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLNKPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYL--KRF----KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDL 431
Cdd:cd05035    81 SPMVILPFMKHGDLHSYLlySRLgglpEKLPLQTLLKFMVDIAKGMEYLSNRN--FIHRDLAARNCMLDENM-TVCVADF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLA-TLKNKSFAKS--VIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISGVK--- 502
Cdd:cd05035   158 GLSrKIYSGDYYRQgrISKMPvKWIALEsLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVEN-HEIYDYLRNGNRlkq 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392899979  503 -PECFSripaqypEIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:cd05035   237 pEDCLD-------EVYFLMYFCWTVDPKDRPTFTKLREV 268
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
287-489 1.71e-12

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: 70.86  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgKRKY--IVLVTE 364
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPH---REAFndVYIVYE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGtlkmyLKRFKRINIKVLKSWCR----QILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA--TLKN 438
Cdd:cd07858    90 LMDTD-----LHQIIRSSQTLSDDHCQyflyQLLRGLKYIHSAN--VLHRDLKPSNLLLN-ANCDLKICDFGLArtTSEK 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  439 KSFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE--YPYSECMN 489
Cdd:cd07858   162 GDFMTEYVVTRWYRAPELLlnCSEYTTAIDVWSVGCIFAELLGRKplFPGKDYVH 216
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
273-484 1.82e-12

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: 69.64  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  273 DKSKNGRFLkfdeelGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYdywESADL 352
Cdd:cd14183     6 ERYKVGRTI------GDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLI---EEMDM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CGKrkyIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI---TGTTGSVKIG 429
Cdd:cd14183    76 PTE---LYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLN--IVHRDIKPENLLVyehQDGSKSLKLG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  430 DLGLATLKNKSFAkSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14183   151 DFGLATVVDGPLY-TVCGTPTYVAPEIIAETgYGLKVDIWAAGVITYILLCGFPPF 205
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
287-479 1.86e-12

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: 69.99  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwCelqesklnKTERQRFR--EEAEMLKDLQ-------HPNIVRF----YDywesadlc 353
Cdd:cd07831     7 IGEGTFSEVLKAQSRKTGKYYA-I--------KCMKKHFKslEQVNNLREIQalrrlspHPNILRLievlFD-------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgsVKIGDLG- 432
Cdd:cd07831    70 RKTGRLALVFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNG--IFHRDIKPENILIKDDI--LKLADFGs 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  433 LATLKNKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07831   146 CRGIYSKPPYTEYISTRWYRAPEclLTDGYYGPKMDIWAVGCVFFEILS 194
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
287-489 2.10e-12

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: 70.28  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR-FREEAeMLKDL-QHPNIVRFYDYWESADlcgkRKYIVLVTE 364
Cdd:cd07852    15 LGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRtFREIM-FLQELnDHPNIIKLLNVIRAEN----DKDIYLVFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGtlkmyLKRFKRINIkvLKSWCR-----QILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAtlknK 439
Cdd:cd07852    90 YMETD-----LHAVIRANI--LEDIHKqyimyQLLKALKYLHSGG--VIHRDLKPSNILLNSDC-RVKLADFGLA----R 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  440 SFAKSV-----------IGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGE--YPYSECMN 489
Cdd:cd07852   156 SLSQLEeddenpvltdyVATRWYRAPEILlgSTRYTKGVDMWSVGCILGEMLLGKplFPGTSTLN 220
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
316-531 2.16e-12

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: 69.74  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  316 KLNK------TERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSW 389
Cdd:cd05609    32 KINKqnlilrNQIQQVFVERDILTFAENPFVVSMYCSFET------KRHLCMVMEYVEGGDCATLLKNIGPLPVDMARMY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  390 CRQILKGLSFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA-----------------KSVIGTPEFM 452
Cdd:cd05609   106 FAETVLALEYLH--SYGIVHRDLKPDNLLIT-SMGHIKLTDFGLSKIGLMSLTtnlyeghiekdtrefldKQVCGTPEYI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  453 APE-MYEEMYDESVDVYAFGMCLLEMVTGEYP-YSEcmNPATIYRKVISG--VKPECFSRIPaqyPEIREIIDRCIRVRR 528
Cdd:cd05609   183 APEvILRQGYGKPVDWWAMGIILYEFLVGCVPfFGD--TPEELFGQVISDeiEWPEGDDALP---DDAQDLITRLLQQNP 257

                  ...
gi 392899979  529 EER 531
Cdd:cd05609   258 LER 260
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
392-484 2.23e-12

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: 70.11  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  392 QILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFAKSVIGTPEFMAPEM--YEEmYDESVDV 467
Cdd:cd05587   105 EIAVGLFFLHSKG--IIYRDLKLDNVMLD-AEGHIKIADFGMCKegIFGGKTTRTFCGTPDYIAPEIiaYQP-YGKSVDW 180
                          90
                  ....*....|....*..
gi 392899979  468 YAFGMCLLEMVTGEYPY 484
Cdd:cd05587   181 WAYGVLLYEMLAGQPPF 197
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
282-485 2.25e-12

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: 69.18  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAwceLQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVL 361
Cdd:cd14110     6 AFQTEINRGRFSVVRQCEEKRSGQMLA---AKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSP------RHLVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSf 441
Cdd:cd14110    77 IEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRR--ILHLDLRSENMIITEKN-LLKIVDLGNAQPFNQG- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  442 akSVIGTPEF------MAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYS 485
Cdd:cd14110   153 --KVLMTDKKgdyvetMAPELLEGQgAGPQTDIWAIGVTAFIMLSADYPVS 201
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
287-480 2.33e-12

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: 70.44  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07876    29 IGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELM 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKS-V 445
Cdd:cd07876   109 DANLCQVIHMELDHERMSYL---LYQMLCGIKHLHSAG--IIHRDLKPSNIVVK-SDCTLKILDFGLARTACTNFMMTpY 182
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 392899979  446 IGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTG 480
Cdd:cd07876   183 VVTRYYRAPEVILGMgYKENVDIWSVGCIMGELVKG 218
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
287-486 2.44e-12

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: 70.48  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDTETGVAVAWCELQESKLNKTERQRFREEA--EMLKDLQHPNIVRF-YDYWESADLCgkrkyivL 361
Cdd:cd05633    13 IGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMtYAFHTPDKLC-------F 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSF 441
Cdd:cd05633    86 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHVRISDLGLACDFSKKK 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  442 AKSVIGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd05633   163 PHASVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRQ 209
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
287-481 2.56e-12

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: 70.32  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQDFYLVMPYM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNKSFAKSVI 446
Cdd:cd07879   103 QTDLQKIMGHPLSEDKVQYL---VYQMLCGLKYIHSAG--IIHRDLKPGNLAVNEDC-ELKILDFGLARHADAEMTGYVV 176
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 392899979  447 gTPEFMAPEMYEEM--YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07879   177 -TRWYRAPEVILNWmhYNQTVDIWSVGCIMAEMLTGK 212
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
282-481 2.57e-12

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: 70.20  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgKRKY--I 359
Cdd:cd07859     3 KIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPS---RREFkdI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSgTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIfITGTTGSVKIGDLGLATLK-N 438
Cdd:cd07859    80 YVVFELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTAN--VFHRDLKPKNI-LANADCKLKICDFGLARVAfN 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 KS----FAKSVIGTPEFMAPEM---YEEMYDESVDVYAFGMCLLEMVTGE 481
Cdd:cd07859   156 DTptaiFWTDYVATRWYRAPELcgsFFSKYTPAIDIWSIGCIFAEVLTGK 205
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
280-493 2.59e-12

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They 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. The EphB 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: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 69.13  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQR--FREEAEMLKDLQHPNIVRFydywesADLCGKRK 357
Cdd:cd05065     5 CVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRrdFLSEASIMGQFDHPNIIHL------EGVVTKSR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMTSGTLKMYLK----RFKRINikvLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGL 433
Cdd:cd05065    79 PVMIITEFMENGALDSFLRqndgQFTVIQ---LVGMLRGIAAGMKYLSEMN--YVHRDLAARNILVNSNL-VCKVSDFGL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  434 ATL-----KNKSFAKSVIGT-P-EFMAPEMYE-EMYDESVDVYAFGMCLLE-MVTGEYPYSECMNPATI 493
Cdd:cd05065   153 SRFleddtSDPTYTSSLGGKiPiRWTAPEAIAyRKFTSASDVWSYGIVMWEvMSYGERPYWDMSNQDVI 221
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
281-531 2.88e-12

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 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: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 69.20  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDE-ELGRGSF----KTVFRGLDTETGVAVAWCELQESKlnkTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcgk 355
Cdd:cd05115     5 LLIDEvELGSGNFgcvkKGVYKMRKKQIDVAIKVLKQGNEK---AVRDEMMREAQIMHQLDNPYIVRMIGVCEAEAL--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 rkyiVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLA 434
Cdd:cd05115    79 ----MLVMEMASGGPLNKFLSGKKdEITVSNVVELMHQVSMGMKYLEEKN--FVHRDLAARNVLLVNQH-YAKISDFGLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 T--------LKNKSFAKSVIgtpEFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATIyRKVISGVKP 503
Cdd:cd05115   152 KalgaddsyYKARSAGKWPL---KWYAPEciNFRKFSSRS-DVWSYGVTMWEAFSyGQKPYKKMKGPEVM-SFIEQGKRM 226
                         250       260
                  ....*....|....*....|....*...
gi 392899979  504 ECFSRIPaqyPEIREIIDRCIRVRREER 531
Cdd:cd05115   227 DCPAECP---PEMYALMSDCWIYKWEDR 251
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
281-537 3.07e-12

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: 68.75  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAVawcelQESKLNKTErQRFREEAEMLKDLQHPNIVRfydywesadLCGK--RKY 358
Cdd:cd05083     8 LTLGEIIGEGEFGAVLQGEYMGQKVAV-----KNIKCDVTA-QAFLEETAVMTKLQHKNLVR---------LLGVilHNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKR--INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd05083    73 LYIVMELMSKGNLVNFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKK--LVHRDLAARNILVS-EDGVAKISDFGLAKV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSVIGTpEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYsecmnPATIYRKVISGVKPECFSRIPAQYP 514
Cdd:cd05083   150 GSMGVDNSRLPV-KWTAPEaLKNKKFSSKSDVWSYGVLLWEVFSyGRAPY-----PKMSVKEVKEAVEKGYRMEPPEGCP 223
                         250       260
                  ....*....|....*....|....
gi 392899979  515 -EIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05083   224 pDVYSIMTSCWEAEPGKRPSFKKL 247
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
287-498 3.69e-12

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: 69.65  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEML-KDLQHPNIVRFYDYWESADlcgkRKYIVLvtE 364
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAiLKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKD----KLYFVL--D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFA 442
Cdd:cd05575    77 YVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLN--IIYRDLKPENILLD-SQGHVVLTDFGLCKegIEPSDTT 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  443 KSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGEYP-YSEcmNPATIYRKVI 498
Cdd:cd05575   154 STFCGTPEYLAPEvLRKQPYDRTVDWWCLGAVLYEMLYGLPPfYSR--DTAEMYDNIL 209
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
287-484 4.36e-12

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: 68.62  E-value: 4.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDTETGVAVAWCELQESKLNKTERQRFREEAeMLKDLQH----PNIVRFYDYWESAD-LCgkrkyi 359
Cdd:cd05606     2 IGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERI-MLSLVSTggdcPFIVCMTYAFQTPDkLC------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 vLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK 439
Cdd:cd05606    75 -FILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRF--IVYRDLKPANILLD-EHGHVRISDLGLACDFSK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  440 SFAKSVIGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05606   151 KKPHASVGTHGYMAPEVLQKgvAYDSSADWFSLGCMLYKLLKGHSPF 197
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
277-481 4.66e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 69.27  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFLkFDEELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQrFREEAE----MLKDL-QHP-----NIVRFYDY 346
Cdd:cd14226    12 MDRYE-IDSLIGKGSFGQVVKAYDHVEQEWVA------IKIIKNKKA-FLNQAQievrLLELMnKHDtenkyYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  347 WESadlcgkRKYIVLVTELMtSGTLKMYLKR--FKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTG 424
Cdd:cd14226    84 FMF------RNHLCLVFELL-SYNLYDLLRNtnFRGVSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLCNPKR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  425 S-VKIGDLGLATLKNKSFAKsVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd14226   157 SaIKIIDFGSSCQLGQRIYQ-YIQSRFYRSPEVLLGLpYDLAIDMWSLGCILVEMHTGE 214
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
287-528 5.01e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 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: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 68.66  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVawcelqESKLNKTERQRFREeAEMLKD--LQHPNIVRFYdyweSADLCGKRKY--IVLV 362
Cdd:cd14144     3 VGKGRYGEVWKGKWRGEKVAV------KIFFTTEEASWFRE-TEIYQTvlMRHENILGFI----AADIKGTGSWtqLYLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLkRFKRINIKVLKSWCRQILKGLSFLHTR------NPPVIHRDLKCDNIFITgTTGSVKIGDLGLAtL 436
Cdd:cd14144    72 TDYHENGSLYDFL-RGNTLDTQSMLKLAYSAACGLAHLHTEifgtqgKPAIAHRDIKSKNILVK-KNGTCCIADLGLA-V 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  437 KNKSFAKSV-------IGTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEMVtgeypysecmnpatiyRKVIS-GV 501
Cdd:cd14144   149 KFISETNEVdlppntrVGTKRYMAPEVLDESLNRNhfdaykmADMYSFGLVLWEIA----------------RRCISgGI 212
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  502 KPEC----FSRIPA--QYPEIREIIdrCIRVRR 528
Cdd:cd14144   213 VEEYqlpyYDAVPSdpSYEDMRRVV--CVERRR 243
OSR1_C pfam12202
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
569-633 5.08e-12

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


Pssm-ID: 463491  Cd Length: 62  Bit Score: 62.67  E-value: 5.08e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979   569 IQMQLRVYDEKKRKQyrfKENEGLQFAFDIENDSPDEVVQQMIEQQHIPDEDTRMITKLIKDKVD 633
Cdd:pfam12202    1 INLVLRVRDPKKKKH---KELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
286-481 5.51e-12

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: 69.13  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETG--VAVawcelqesKLNKTErQRFRE----EAEMLKDLQH------PNIVRFYDYWEsadlc 353
Cdd:cd14134    19 LLGEGTFGKVLECWDRKRKryVAV--------KIIRNV-EKYREaakiEIDVLETLAEkdpngkSHCVQLRDWFD----- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gKRKYIVLVTELMTSgTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI-FITGTT------- 423
Cdd:cd14134    85 -YRGHMCIVFELLGP-SLYDFLKknNYGPFPLEHVQHIAKQLLEAVAFLHDLK--LTHTDLKPENIlLVDSDYvkvynpk 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  424 ----------GSVKIGDLGLATLKNKSFAkSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGE 481
Cdd:cd14134   161 kkrqirvpksTDIKLIDFGSATFDDEYHS-SIVSTRHYRAPEVILGLgWSYPCDVWSIGCILVELYTGE 228
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
317-552 7.57e-12

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: 68.53  E-value: 7.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  317 LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILK 395
Cdd:cd05597    40 LKRAETACFREERDVLVNGDRRWITKLHYAFQD------ENYLYLVMDYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  396 GLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLG--LATLKNKSFAKSV-IGTPEFMAPEMYEEM------YDESVD 466
Cdd:cd05597   114 AIDSIHQLG--YVHRDIKPDNVLL-DRNGHIRLADFGscLKLREDGTVQSSVaVGTPDYISPEILQAMedgkgrYGPECD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  467 VYAFGMCLLEMVTGEYP-YSECMnpATIYRKVISgvKPECFSrIPAQYPEI----REIIDR--CIRVRREERSTVKQLLV 539
Cdd:cd05597   191 WWSLGVCMYEMLYGETPfYAESL--VETYGKIMN--HKEHFS-FPDDEDDVseeaKDLIRRliCSRERRLGQNGIDDFKK 265
                         250
                  ....*....|...
gi 392899979  540 DDFFTPEDLIGIR 552
Cdd:cd05597   266 HPFFEGIDWDNIR 278
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
287-484 7.80e-12

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: 68.36  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQEsklnKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcgkRKYIVLVTELM 366
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISR----RMEANTQREVAALRLCQSHPNIVALHEVLHD------QYHTYLVMELL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFIT--GTTGSVKIGDLGLATLKNKSFAKs 444
Cdd:cd14180    84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAG--VVHRDLKPENILYAdeSDGAVLKVIDFGFARLRPQGSRP- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392899979  445 vIGTP----EFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14180   161 -LQTPcftlQYAAPELFSNQgYDESCDLWSLGVILYTMLSGQVPF 204
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
281-539 7.92e-12

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: 68.10  E-value: 7.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGVAV-AWCELQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDywesadLCGKRKY 358
Cdd:cd05089     4 IKFEDVIGEGNFGQVIKAMIKKDGLKMnAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLG------ACENRGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKR---------FKR-------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGT 422
Cdd:cd05089    78 LYIAIEYAPYGNLLDFLRKsrvletdpaFAKehgtastLTSQQLLQFASDVAKGMQYLSEKQ--FIHRDLAARNVLV-GE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  423 TGSVKIGDLGLATLKNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVIS 499
Cdd:cd05089   155 NLVSKIADFGLSRGEEVYVKKTMGRLPvRWMAIEsLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCG-MTCAELYEKLPQ 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  500 GVKPEcfsRIPAQYPEIREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd05089   234 GYRME---KPRNCDDEVYELMRQCWRDRPYERPPFSQISV 270
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
361-484 8.09e-12

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: 68.60  E-value: 8.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKN 438
Cdd:cd05588    73 FVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKG--IIYRDLKLDNVLLD-SEGHIKLTDYGMCKegLRP 149
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 392899979  439 KSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05588   150 GDTTSTFCGTPNYIAPEILRgEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
287-521 9.11e-12

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: 68.54  E-value: 9.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDTETGVAVAWCELQESKLNKTERQRFREEA--EMLKDLQHPNIVRFYDYWESADlcgkrkYIVLV 362
Cdd:cd14223     8 IGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMSYAFHTPD------KLSFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA 442
Cdd:cd14223    82 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRF--VVYRDLKPANILLD-EFGHVRISDLGLACDFSKKKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  443 KSVIGTPEFMAPEMYEE--MYDESVDVYAFGMCLLEMVTGEYPYSE--CMNPATIYRKVISGVK--PECFSripaqyPEI 516
Cdd:cd14223   159 HASVGTHGYMAPEVLQKgvAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRMTLTMAVelPDSFS------PEL 232

                  ....*
gi 392899979  517 REIID 521
Cdd:cd14223   233 RSLLE 237
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
287-480 1.02e-11

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: 68.21  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07850     8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQDVYLVMELM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSG---TLKMYLKRfKRINIKVLKSWCrqilkGLSFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAK 443
Cdd:cd07850    88 DANlcqVIQMDLDH-ERMSYLLYQMLC-----GIKHLH--SAGIIHRDLKPSNIVVK-SDCTLKILDFGLARTAGTSFMM 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 392899979  444 S--VIgTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTG 480
Cdd:cd07850   159 TpyVV-TRYYRAPEVILGMgYKENVDIWSVGCIMGEMIRG 197
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
321-481 1.03e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 68.87  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  321 ERQRFREEAEMLKDLQHPNIVRF---YDYwesadlcgkRKYIVLVTELMTSgTLKMYLKRFKRINIKVLKSWCRQILKGL 397
Cdd:PHA03212  126 QRGGTATEAHILRAINHPSIIQLkgtFTY---------NKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAI 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  398 SFLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATL-----KNKSFAKSviGTPEFMAPEMY-EEMYDESVDVYAFG 471
Cdd:PHA03212  196 QYLH--ENRIIHRDIKAENIFIN-HPGDVCLGDFGAACFpvdinANKYYGWA--GTIATNAPELLaRDPYGPAVDIWSAG 270
                         170
                  ....*....|
gi 392899979  472 MCLLEMVTGE 481
Cdd:PHA03212  271 IVLFEMATCH 280
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
287-531 1.07e-11

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: 68.20  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVF--RGLDT-ETGVAVAWCELQESKL--NKTERQRFREEAEMLKDLQHPNIVRFYDYWESadlcGKRKYIVL 361
Cdd:cd05584     4 LGKGGYGKVFqvRKTTGsDKGKIFAMKVLKKASIvrNQKDTAHTKAERNILEAVKHPFIVDLHYAFQT----GGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 vtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKIGDLGLA--TLKNK 439
Cdd:cd05584    80 --EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLG--IIYRDLKPENILL-DAQGHVKLTDFGLCkeSIHDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 SFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPYSECMNPATIyRKVISGVkpecFSRIPAQYPEIRE 518
Cdd:cd05584   155 TVTHTFCGTIEYMAPEILTRSgHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTI-DKILKGK----LNLPPYLTNEARD 229
                         250
                  ....*....|...
gi 392899979  519 IIDRCIRVRREER 531
Cdd:cd05584   230 LLKKLLKRNVSSR 242
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
287-484 1.15e-11

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: 68.15  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKKEViIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTND------RLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--LKNKSFAK 443
Cdd:cd05571    77 VNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQG--IVYRDLKLENLLLD-KDGHIKITDFGLCKeeISYGATTK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 392899979  444 SVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05571   154 TFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
286-485 1.17e-11

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: 68.52  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVAWCELQESKLNK-TERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTE 364
Cdd:cd05600    18 QVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKlNEVNHVLTERDILTTTNSPWLVKLLYAFQDPE------NVYLAME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLkrfkrINIKVLKSWC-----RQILKGLSFLHtrNPPVIHRDLKCDNiFITGTTGSVKIGDLGLAT---- 435
Cdd:cd05600    92 YVPGGDFRTLL-----NNSGILSEEHarfyiAEMFAAISSLH--QLGYIHRDLKPEN-FLIDSSGHIKLTDFGLASgtls 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 -----------------------------------LKNKSFAKSVIGTPEFMAPEM-YEEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd05600   164 pkkiesmkirleevkntafleltakerrniyramrKEDQNYANSVVGSPDYMAPEVlRGEGYDLTVDYWSLGCILFECLV 243

                  ....*.
gi 392899979  480 GEYPYS 485
Cdd:cd05600   244 GFPPFS 249
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
287-540 1.21e-11

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: 66.80  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTERQRFRE------------EAEMLKDL----QHPNIVRFYDYWESa 350
Cdd:cd14101     8 LGKGGFGTVYAGHRISDGLQVA--------IKQISRNRVQQwsklpgvnpvpnEVALLQSVgggpGHRGVIRLLDWFEI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  351 dlcgKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGD 430
Cdd:cd14101    79 ----PEGFLLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKG--VVHRDIKDENILVDLRTGDIKLID 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  431 LGLATLKNKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNpatiyrkvISGVKPECFSR 508
Cdd:cd14101   153 FGSGATLKDSMYTDFDGTRVYSPPEwiLYHQYHALPATVWSLGILLYDMVCGDIPFERDTD--------ILKAKPSFNKR 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 392899979  509 IPaqyPEIREIIDRCIRVRREERSTVKQLLVD 540
Cdd:cd14101   225 VS---NDCRSLIRSCLAYNPSDRPSLEQILLH 253
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
286-521 1.30e-11

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 67.30  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGL-------DTETGVAVAwcELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKY 358
Cdd:cd05061    13 ELGQGSFGMVYEGNardiikgEAETRVAVK--TVNESA-SLRERIEFLNEASVMKGFTCHHVVRLLG------VVSKGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKR----------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKI 428
Cdd:cd05061    84 TLVVMELMAHGDLKSYLRSLRPeaennpgrppPTLQEMIQMAAEIADGMAYLNAKK--FVHRDLAARNCMV-AHDFTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLA-----TLKNKSFAKSVIGTpEFMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISG- 500
Cdd:cd05061   161 GDFGMTrdiyeTDYYRKGGKGLLPV-RWMAPESLKDgVFTTSSDMWSFGVVLWEITSlAEQPYQGLSN-EQVLKFVMDGg 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  501 --VKPE------------CFSRIPAQYPEIREIID 521
Cdd:cd05061   239 ylDQPDncpervtdlmrmCWQFNPKMRPTFLEIVN 273
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
337-538 1.39e-11

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: 67.49  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  337 HPNIVRFYD-YWESADLCGK---RKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDL 412
Cdd:cd14171    58 HPNIVQIYDvYANSVQFPGEsspRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLN--IAHRDL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  413 KCDNIFITGTT--GSVKIGDLGLATLKNKSFaKSVIGTPEFMAPEMYEEM------------------YDESVDVYAFGM 472
Cdd:cd14171   136 KPENLLLKDNSedAPIKLCDFGFAKVDQGDL-MTPQFTPYYVAPQVLEAQrrhrkersgiptsptpytYDKSCDMWSLGV 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  473 CLLEMVTGeYP--YSECMN---PATIYRKVISG---VKPECFSRIPAQypeIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14171   215 IIYIMLCG-YPpfYSEHPSrtiTKDMKRKIMTGsyeFPEEEWSQISEM---AKDIVRKLLCVDPEERMTIEEVL 284
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
287-539 1.56e-11

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: 66.99  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAV-AWCELQESKLNKTERQRFREEAEMLKDL-QHPNIVRFYDywesadLCGKRKYIVLVTE 364
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGLRMdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLG------ACEHRGYLYLAIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKR---------FKRINIKVLKSWCRQIL-------KGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKI 428
Cdd:cd05047    77 YAPHGNLLDFLRKsrvletdpaFAIANSTASTLSSQQLLhfaadvaRGMDYLSQKQ--FIHRDLAARNILV-GENYVAKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLATLKNKSFAKSVIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYseC-MNPATIYRKVISGVKPE 504
Cdd:cd05047   154 ADFGLSRGQEVYVKKTMGRLPvRWMAIEsLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY--CgMTCAELYEKLPQGYRLE 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  505 cfsRIPAQYPEIREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd05047   232 ---KPLNCDDEVYDLMRQCWREKPYERPSFAQILV 263
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
359-484 1.57e-11

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: 68.12  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--L 436
Cdd:cd05617    91 LFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERG--IIYRDLKLDNVLLD-ADGHIKLTDYGMCKegL 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05617   168 GPGDTTSTFCGTPNYIAPEILRgEEYGFSVDWWALGVLMFEMMAGRSPF 216
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
281-511 1.67e-11

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: 66.81  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG---LDTETGVAVAwceLQESKLNKTERQR--FREEAEMLKDLQHPNIVRFydywesADLCGK 355
Cdd:cd05066     6 IKIEKVIGAGEFGEVCSGrlkLPGKREIPVA---IKTLKAGYTEKQRrdFLSEASIMGQFDHPNIIHL------EGVVTR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLA 434
Cdd:cd05066    77 SKPVMIVTEYMENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMG--YVHRDLAARNILVNSNL-VCKVSDFGLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TL--KNKSFAKSVIGTP---EFMAPEMYE-EMYDESVDVYAFGMCLLE-MVTGEYPYSECMNpatiyRKVISGVkpECFS 507
Cdd:cd05066   154 RVleDDPEAAYTTRGGKipiRWTAPEAIAyRKFTSASDVWSYGIVMWEvMSYGERPYWEMSN-----QDVIKAI--EEGY 226

                  ....
gi 392899979  508 RIPA 511
Cdd:cd05066   227 RLPA 230
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
338-484 1.71e-11

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: 67.71  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  338 PNIVRFYDYWESADlcgkRKYIVLvtELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI 417
Cdd:cd05615    71 PFLTQLHSCFQTVD----RLYFVM--EYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKG--IIYRDLKLDNV 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 FITgTTGSVKIGDLGLAT--LKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05615   143 MLD-SEGHIKIADFGMCKehMVEGVTTRTFCGTPDYIAPEIIAyQPYGRSVDWWAYGVLLYEMLAGQPPF 211
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
287-538 2.06e-11

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: 66.13  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwcelqeskLNKTERQRFRE-----------EAEMLKDLQHP--NIVRFYDYWESADlc 353
Cdd:cd14102     8 LGSGGFGTVYAGSRIADGLPVA--------VKHVVKERVTEwgtlngvmvplEIVLLKKVGSGfrGVIKLLDWYERPD-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gkrKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSflHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGL 433
Cdd:cd14102    78 ---GFLIVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVR--HCYSCGVVHRDIKDENLLVDLRTGELKLIDFGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  434 ATLKNKSFAKSVIGTPEFMAPE--MYEEMYDESVDVYAFGMCLLEMVTGEYPY---SECMNPATIYRKVISgvkPECfsr 508
Cdd:cd14102   153 GALLKDTVYTDFDGTRVYSPPEwiRYHRYHGRSATVWSLGVLLYDMVCGDIPFeqdEEILRGRLYFRRRVS---PEC--- 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 392899979  509 ipaqypeiREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14102   227 --------QQLIKWCLSLRPSDRPTLEQIF 248
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
287-523 2.24e-11

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: 66.48  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTV---FRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVT 363
Cdd:cd05074    17 LGKGEFGSVreaQLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKGRLPIPMVIL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLkRFKRIN-------IKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT- 435
Cdd:cd05074    97 PFMKHGDLHTFL-LMSRIGeepftlpLQTLVRFMIDIASGMEYLSSKN--FIHRDLAARNCMLNENM-TVCVADFGLSKk 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 ------LKNKSFAKSVIgtpEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISGVK----P 503
Cdd:cd05074   173 iysgdyYRQGCASKLPV---KWLALEsLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVEN-SEIYNYLIKGNRlkqpP 248
                         250       260
                  ....*....|....*....|
gi 392899979  504 ECFSripaqypEIREIIDRC 523
Cdd:cd05074   249 DCLE-------DVYELMCQC 261
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
286-486 2.28e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a 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: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 66.60  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGLDTETGVAVawcelqESKLNKTERQRFRE-EAEMLKDLQHPNIVRFYdyweSADLCGKRKY--IVLV 362
Cdd:cd14220     2 QIGKGRYGEVWMGKWRGEKVAV------KVFFTTEEASWFREtEIYQTVLMRHENILGFI----AADIKGTGSWtqLYLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKrFKRINIKVLKSWCRQILKGLSFLHTR------NPPVIHRDLKCDNIFITgTTGSVKIGDLGLATL 436
Cdd:cd14220    72 TDYHENGSLYDFLK-CTTLDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIK-KNGTCCIADLGLAVK 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  437 KNKSFAK------SVIGTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEM----VTG----EY--PYSE 486
Cdd:cd14220   150 FNSDTNEvdvplnTRVGTKRYMAPEVLDESLNKNhfqayimADIYSFGLIIWEMarrcVTGgiveEYqlPYYD 222
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
287-479 2.77e-11

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: 66.62  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKLNKtERQRFR----EEAEMLKDLQHPNIVRFYD--YWESADLCGKRKYIV 360
Cdd:cd07865    20 IGQGTFGEVFKARHRKTGQIVA---LKKVLMEN-EKEGFPitalREIKILQLLKHENVVNLIEicRTKATPYNRYKGSIY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMT---SGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAtlk 437
Cdd:cd07865    96 LVFEFCEhdlAGLLSNKNVKFTLSEIKKV---MKMLLNGLYYIHRNK--ILHRDMKAANILIT-KDGVLKLADFGLA--- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392899979  438 nKSFAKSVIGTPEFM----------APEMY--EEMYDESVDVYAFGMCLLEMVT 479
Cdd:cd07865   167 -RAFSLAKNSQPNRYtnrvvtlwyrPPELLlgERDYGPPIDMWGAGCIMAEMWT 219
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
281-537 2.90e-11

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: 66.59  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTV---------------FRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYd 345
Cdd:cd05051     7 LEFVEKLGEGQFGEVhlceanglsdltsddFIGNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLL- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  346 ywesaDLCGKRKYIVLVTELMTSGTLKMYLKRF-------KRINIKVLKSWC-----RQILKGLSFLHTRNppVIHRDLK 413
Cdd:cd05051    86 -----GVCTRDEPLCMIVEYMENGDLNQFLQKHeaetqgaSATNSKTLSYGTllymaTQIASGMKYLESLN--FVHRDLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  414 CDNIFItGTTGSVKIGDLGLA-TLKNKSFAK---SVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT--GEYPYSE 486
Cdd:cd05051   159 TRNCLV-GPNYTIKIADFGMSrNLYSGDYYRiegRAVLPIRWMAWEsILLGKFTTKSDVWAFGVTLWEILTlcKEQPYEH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899979  487 CM------NPATIYRKviSGvKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05051   238 LTdeqvieNAGEFFRD--DG-MEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
285-484 4.85e-11

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily 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).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 65.36  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG--LDTETGVAVAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVrfydywESADLCGKRKYIVLV 362
Cdd:cd14206     3 QEIGNGWFGKVILGeiFSDYTPAQVVVKELRVSA-GPLEQRKFISEAQPYRSLQHPNIL------QCLGLCTETIPFLLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRI----------NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLG 432
Cdd:cd14206    76 MEFCQLGDLKRYLRAQRKAdgmtpdlptrDLRTLQRMAYEITLGLLHLHKNN--YIHSDLALRNCLLTSDL-TVRIGDYG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  433 LAtlkNKSFAKSVIGTPE-------FMAPEMYEEMY------DES--VDVYAFGMCLLEMVT-GEYPY 484
Cdd:cd14206   153 LS---HNNYKEDYYLTPDrlwiplrWVAPELLDELHgnlivvDQSkeSNVWSLGVTIWELFEfGAQPY 217
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
264-552 5.05e-11

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: 66.96  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  264 DFDAQEKPI-DKSKNGRFLKFDEEL----GRGSFK--TVFRGLDTETGVAVAWCELQEsKLNKTERQRFREEAEMLKDLQ 336
Cdd:cd05623    52 EYLEWAKPFtSKVKQMRLHKEDFEIlkviGRGAFGevAVVKLKNADKVFAMKILNKWE-MLKRAETACFREERDVLVNGD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  337 HPNIVRF-YDYWESADLcgkrkyiVLVTELMTSGTLKMYLKRFK-RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKC 414
Cdd:cd05623   131 SQWITTLhYAFQDDNNL-------YLVMDYYVGGDLLTLLSKFEdRLPEDMARFYLAEMVLAIDSVHQLH--YVHRDIKP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  415 DNIFITgTTGSVKIGDLG--LATLKNKSFAKSV-IGTPEFMAPEMYEEM------YDESVDVYAFGMCLLEMVTGEYP-Y 484
Cdd:cd05623   202 DNILMD-MNGHIRLADFGscLKLMEDGTVQSSVaVGTPDYISPEILQAMedgkgkYGPECDWWSLGVCMYEMLYGETPfY 280
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  485 SECMnpATIYRKVISgvKPECFsRIPAQYPEIRE----IIDR--CIRVRREERSTVKQLLVDDFFTPEDLIGIR 552
Cdd:cd05623   281 AESL--VETYGKIMN--HKERF-QFPTQVTDVSEnakdLIRRliCSREHRLGQNGIEDFKNHPFFVGIDWDNIR 349
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
281-485 5.48e-11

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: 65.77  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTV----------FRGLD----TETGVAVAWCELQeSKLNKTERQRFREEAEMLKDLQHPNIVRFYDY 346
Cdd:cd05097     7 LRLKEKLGEGQFGEVhlceaeglaeFLGEGapefDGQPVLVAVKMLR-ADVTKTARNDFLKEIKIMSRLKNPNIIRLLGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  347 WESAD-LCgkrkyivLVTELMTSGTLKMYLKR------------FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLK 413
Cdd:cd05097    86 CVSDDpLC-------MITEYMENGDLNQFLSQreiestfthannIPSVSIANLLYMAVQIASGMKYLASLN--FVHRDLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  414 CDNIFItGTTGSVKIGDLGLA-TLKNKSF----AKSVIGTpEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT--GEYPYS 485
Cdd:cd05097   157 TRNCLV-GNHYTIKIADFGMSrNLYSGDYyriqGRAVLPI-RWMAWEsILLGKFTTASDVWAFGVTLWEMFTlcKEQPYS 234
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
281-480 7.41e-11

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 64.58  E-value: 7.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETGvavAWCELQESK-----LNKTER---QRFREEAEMLKDLQHPNIVRFYdyweSADL 352
Cdd:cd05078     1 LIFNESLGQGTFTKIFKGIRREVG---DYGQLHETEvllkvLDKAHRnysESFFEAASMMSQLSHKHLVLNY----GVCV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CGKRKyiVLVTELMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFI-------TGTTG 424
Cdd:cd05078    74 CGDEN--ILVQEYVKFGSLDTYLKKNKNcINILWKLEVAKQLAWAMHFLEEKT--LVHGNVCAKNILLireedrkTGNPP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  425 SVKIGDLGLA-TLKNKSFAKSVIgtpEFMAPEMYEEMYDESV--DVYAFGMCLLEMVTG 480
Cdd:cd05078   150 FIKLSDPGISiTVLPKDILLERI---PWVPPECIENPKNLSLatDKWSFGTTLWEICSG 205
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
285-486 8.80e-11

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 64.50  E-value: 8.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRG-LDTETGVA-VAWCELQESKlNKTERQRFREEAEMLKDLQHPNIVrfydywESADLCGKRKYIVLV 362
Cdd:cd05086     3 QEIGNGWFGKVLLGeIYTGTSVArVVVKELKASA-NPKEQDDFLQQGEPYYILQHPNIL------QCVGQCVEAIPYLLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYL-----KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLK 437
Cdd:cd05086    76 FEFCDLGDLKTYLanqqeKLRGDSQIMLLQRMACEIAAGLAHMHKHN--FLHSDLALRNCYLTSDL-TVKVGDYGIGFSR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  438 NKsfaKSVIGTPE-------FMAPEMYEEMYD--------ESVDVYAFGMCLLEMV-TGEYPYSE 486
Cdd:cd05086   153 YK---EDYIETDDkkyaplrWTAPELVTSFQDgllaaeqtKYSNIWSLGVTLWELFeNAAQPYSD 214
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
282-480 9.80e-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: 9.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTV----FRGLDTETGVAVAWCELQESKLNKTERQrFREeaemLKDLQ----HPNIVRFYDywesADLC 353
Cdd:cd07857     3 ELIKELGQGAYGIVcsarNAETSEEETVAIKKITNVFSKKILAKRA-LRE----LKLLRhfrgHKNITCLYD----MDIV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKY--IVLVTELMTSgTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDL 431
Cdd:cd07857    74 FPGNFneLYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSAN--VLHRDLKPGNLLVN-ADCELKICDF 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  432 GLA------TLKNKSFAKSVIGTPEFMAPEM---YEEmYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07857   150 GLArgfsenPGENAGFMTEYVATRWYRAPEImlsFQS-YTKAIDVWSVGCILAELLGR 206
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
281-537 1.04e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 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 FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 64.99  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLDTETGVAVAWCELQESKLNKTERQ--RFREEAEMLKDL-QHPNIVRFYDywesadLC 353
Cdd:cd05099    14 LVLGKPLGEGCFGQVVRaeayGIDKSRPDQTVTVAVKMLKDNATDKDlaDLISEMELMKLIgKHKNIINLLG------VC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLkRFKR-----------------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDN 416
Cdd:cd05099    88 TQEGPLYVIVEYAAKGNLREFL-RARRppgpdytfditkvpeeqLSFKDLVSCAYQVARGMEYLESRR--CIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  417 IFITgTTGSVKIGDLGLATLKNK--SFAKSVIG-TP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYsecmnP 490
Cdd:cd05099   165 VLVT-EDNVMKIADFGLARGVHDidYYKKTSNGrLPvKWMAPEaLFDRVYTHQSDVWSFGILMWEIFTlGGSPY-----P 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  491 ATIYRKVIS----GVKPECFSRIPAQ-YPEIREiidrCIRVRREERSTVKQL 537
Cdd:cd05099   239 GIPVEELFKllreGHRMDKPSNCTHElYMLMRE----CWHAVPTQRPTFKQL 286
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
284-480 1.06e-10

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: 65.54  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLcGKRKYIVLVT 363
Cdd:cd07853     5 DRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHI-DPFEEIYVVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLkRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLKNksFAK 443
Cdd:cd07853    84 ELMQSDLHKIIV-SPQPLSSDHVKVFLYQILRGLKYLHSAG--ILHRDIKPGNLLVNSNC-VLKICDFGLARVEE--PDE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 392899979  444 SVIGTPE-----FMAPE--MYEEMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd07853   158 SKHMTQEvvtqyYRAPEilMGSRHYTSAVDIWSVGCIFAELLGR 201
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
281-537 1.13e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR 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: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 64.82  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLD-TETGVAVAWCELQESKlNKTERQRFREEAEMLKDL-QHPNIVrfydywesaDLCG 354
Cdd:cd05054     9 LKLGKPLGRGAFGKVIQasafGIDkSATCRTVAVKMLKEGA-TASEHKALMTELKILIHIgHHLNVV---------NLLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 ----KRKYIVLVTELMTSGTLKMYLKRfKR---------------------------INIKVLKSWCRQILKGLSFLHTR 403
Cdd:cd05054    79 actkPGGPLMVIVEFCKFGNLSNYLRS-KReefvpyrdkgardveeeedddelykepLTLEDLICYSFQVARGMEFLASR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  404 NppVIHRDLKCDNIFITgTTGSVKIGDLGLA--TLKNKSFAKSVIGT-P-EFMAPE-MYEEMYDESVDVYAFGMCLLEMV 478
Cdd:cd05054   158 K--CIHRDLAARNILLS-ENNVVKICDFGLArdIYKDPDYVRKGDARlPlKWMAPEsIFDKVYTTQSDVWSFGVLLWEIF 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  479 T-GEYPYSECMNPATIYRKVISGVKpecfSRIPaQY--PEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05054   235 SlGASPYPGVQMDEEFCRRLKEGTR----MRAP-EYttPEIYQIMLDCWHGEPKERPTFSEL 291
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
286-493 1.28e-10

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: 64.29  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRG-----LDTETGVAVAWCELQESklNKTERQRFREEAEMLKDLQHPNIVRFYdywesaDLCGKRKYIV 360
Cdd:cd05093    12 ELGEGAFGKVFLAecynlCPEQDKILVAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFY------GVCVEGDPLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLK-------------RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVK 427
Cdd:cd05093    84 MVFEYMKHGDLNKFLRahgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLV-GENLLVK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  428 IGDLGLATLKNKSFAKSVIGTP----EFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYPYSECMNPATI 493
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSNNEVI 232
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
287-480 1.58e-10

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 64.58  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETG--VAVawcelqesKLNKTERQRFRE---EAEMLKDLQ-------HPNIVRFYDYWESAD-LC 353
Cdd:cd14212     7 LGQGTFGQVVKCQDLKTNklVAV--------KVLKNKPAYFRQamlEIAILTLLNtkydpedKHHIVRLLDHFMHHGhLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 gkrkyivLVTELMtSGTLKMYLK--RFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITG-TTGSVKIGD 430
Cdd:cd14212    79 -------IVFELL-GVNLYELLKqnQFRGLSLQLIRKFLQQLLDALSVLKDAR--IIHCDLKPENILLVNlDSPEIKLID 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  431 LGLATLKNKSFaKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTG 480
Cdd:cd14212   149 FGSACFENYTL-YTYIQSRFYRSPEVLLGLpYSTAIDMWSLGCIAAELFLG 198
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
289-535 1.58e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b 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: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 64.28  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  289 RGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAemlkdLQHPNIVRFYdyweSADLCGK--RKYIVLVTELM 366
Cdd:cd14140     5 RGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPG-----MKHENLLQFI----AAEKRGSnlEMELWLITAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRfkriNIKVLKSWC---RQILKGLSFLHT---------RNPPVIHRDLKCDNIFITGTTGSVkIGDLGLA 434
Cdd:cd14140    76 DKGSLTDYLKG----NIVSWNELChiaETMARGLSYLHEdvprckgegHKPAIAHRDFKSKNVLLKNDLTAV-LADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 TL----KNKSFAKSVIGTPEFMAPEMYEEMYDES------VDVYAFGMCLLEMVT----GEYPYSECMNPatiyrkvisg 500
Cdd:cd14140   151 VRfepgKPPGDTHGQVGTRRYMAPEVLEGAINFQrdsflrIDMYAMGLVLWELVSrckaADGPVDEYMLP---------- 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  501 vkpecFSRIPAQYPEIREIIDrcIRVRREERSTVK 535
Cdd:cd14140   221 -----FEEEIGQHPSLEDLQE--VVVHKKMRPVFK 248
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
408-486 1.80e-10

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: 64.25  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  408 IHRDLKCDNIFITgTTGSVKIGDLGLA---TLKNKSFAKSVIGTPEFMAPEM-------YEEMYDESVDVYAFGMCLLEM 477
Cdd:cd05601   124 VHRDIKPENILID-RTGHIKLADFGSAaklSSDKTVTSKMPVGTPDYIAPEVltsmnggSKGTYGVECDWWSLGIVAYEM 202

                  ....*....
gi 392899979  478 VTGEYPYSE 486
Cdd:cd05601   203 LYGKTPFTE 211
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
279-493 1.91e-10

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: 63.86  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  279 RFLKFDEELGRGSFKTV----------FRG----LDTETG--VAVAwCELQESKLNKTERQRFREEAEMLKDLQHPNIVR 342
Cdd:cd05095     5 KLLTFKEKLGEGQFGEVhlceaegmekFMDkdfaLEVSENqpVLVA-VKMLRADANKNARNDFLKEIKIMSRLKDPNIIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  343 FYDYWESAD-LCgkrkyivLVTELMTSGTLKMYLKRFK------------RINIKVLKSWCRQILKGLSFLHTRNppVIH 409
Cdd:cd05095    84 LLAVCITDDpLC-------MITEYMENGDLNQFLSRQQpegqlalpsnalTVSYSDLRFMAAQIASGMKYLSSLN--FVH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  410 RDLKCDNIFItGTTGSVKIGDLGLA-TLKNKSF----AKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVT--GEY 482
Cdd:cd05095   155 RDLATRNCLV-GKNYTIKIADFGMSrNLYSGDYyriqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQ 233
                         250
                  ....*....|.
gi 392899979  483 PYSECMNPATI 493
Cdd:cd05095   234 PYSQLSDEQVI 244
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
287-526 2.45e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 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 FGFR1 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: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 63.88  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFR----GLDTETGVAVAWCELQESKLNKTER--QRFREEAEMLKDL-QHPNIVRFYDywesadLCGKRKYI 359
Cdd:cd05098    21 LGEGCFGQVVLaeaiGLDKDKPNRVTKVAVKMLKSDATEKdlSDLISEMEMMKMIgKHKNIINLLG------ACTQDGPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  360 VLVTELMTSGTLKMYLkRFKR-----------------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgT 422
Cdd:cd05098    95 YVIVEYASKGNLREYL-QARRppgmeycynpshnpeeqLSSKDLVSCAYQVARGMEYLASKK--CIHRDLAARNVLVT-E 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  423 TGSVKIGDLGLA-TLKNKSFAKSVIG---TPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPY------------ 484
Cdd:cd05098   171 DNVMKIADFGLArDIHHIDYYKKTTNgrlPVKWMAPEaLFDRIYTHQSDVWSFGVLLWEIFTlGGSPYpgvpveelfkll 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  485 ---------SECMNPATIYRKvisgvkpECFSRIPAQYPEIREIIDRCIRV 526
Cdd:cd05098   251 keghrmdkpSNCTNELYMMMR-------DCWHAVPSQRPTFKQLVEDLDRI 294
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
285-484 2.63e-10

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: 63.08  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGlDTETGVAVAWCELQESKLNKT--ERQRFREEAEMLKDLQHPNIVrfydywESADLCGKRKYIVLV 362
Cdd:cd05087     3 KEIGHGWFGKVFLG-EVNSGLSSTQVVVKELKASASvqDQMQFLEEAQPYRALQHTNLL------QCLAQCAEVTPYLLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYLKRFKRI-----NIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLATLK 437
Cdd:cd05087    76 MEFCPLGDLKGYLRSCRAAesmapDPLTLQRMACEVACGLLHLHRNN--FVHSDLALRNCLLTADL-TVKIGDYGLSHCK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  438 NKS---FAKSVIGTP-EFMAPEMYEEMYD--------ESVDVYAFGMCLLEMVT-GEYPY 484
Cdd:cd05087   153 YKEdyfVTADQLWVPlRWIAPELVDEVHGnllvvdqtKQSNVWSLGVTIWELFElGNQPY 212
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
289-529 2.68e-10

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: 63.10  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  289 RGSFKTVFRGLDTETGVAVAwCEL---QESKLNKTERQ-RFReeaemlkdlqHPNIVRFYD--YWESAdlcgkrkyIVLV 362
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMA-CKLipvEQFKPSDVEIQaCFR----------HENIAELYGalLWEET--------VHLF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  363 TELMTSGTLKMYL------KRFKRInikvlksWC-RQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAT 435
Cdd:cd13995    75 MEAGEGGSVLEKLescgpmREFEII-------WVtKHVLKGLDFLHSKN--IIHHDIKPSNIVFMSTKAVLVDFGLSVQM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 LKNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSEcMNPATIYrkvisgvkPECFSRIPAQYP 514
Cdd:cd13995   146 TEDVYVPKDLRGTEIYMSPEVILcRGHNTKADIYSLGATIIHMQTGSPPWVR-RYPRSAY--------PSYLYIIHKQAP 216
                         250
                  ....*....|....*
gi 392899979  515 EIREIIDRCIRVRRE 529
Cdd:cd13995   217 PLEDIAQDCSPAMRE 231
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
287-498 2.76e-10

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: 64.13  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKL-NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVLVTEL 365
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMiNKNMVHQVQAERDALALSKSPFIVHLYYSLQSAN------NVYLVMEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNK------ 439
Cdd:cd05610    86 LIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHG--IIHRDLKPDNMLIS-NEGHIKLTDFGLSKVTLNrelnmm 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  440 ------SFAKS-------------------------------------------VIGTPEFMAPE-MYEEMYDESVDVYA 469
Cdd:cd05610   163 dilttpSMAKPkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPElLLGKPHGPAVDWWA 242
                         250       260
                  ....*....|....*....|....*....
gi 392899979  470 FGMCLLEMVTGEYPYSEcMNPATIYRKVI 498
Cdd:cd05610   243 LGVCLFEFLTGIPPFND-ETPQQVFQNIL 270
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
281-519 2.92e-10

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: 63.11  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG------LDTETGVAVAWCELQESKLNKTErqrFREEAEMLKDLQHPNIV------------- 341
Cdd:cd05090     7 VRFMEELGECAFGKIYKGhlylpgMDHAQLVAIKTLKDYNNPQQWNE---FQQEASLMTELHHPNIVcllgvvtqeqpvc 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  342 RFYDYWESADLcgkRKYIVLVTELM-------TSGTLKMYLKRFKRINIKVlkswcrQILKGLSFLHTRNppVIHRDLKC 414
Cdd:cd05090    84 MLFEFMNQGDL---HEFLIMRSPHSdvgcssdEDGTVKSSLDHGDFLHIAI------QIAAGMEYLSSHF--FVHKDLAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  415 DNIFItGTTGSVKIGDLGLA---------TLKNKSFAKSvigtpEFMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEY 482
Cdd:cd05090   153 RNILV-GEQLHVKISDLGLSreiyssdyyRVQNKSLLPI-----RWMPPEaiMYGKFSSDS-DIWSFGVVLWEIFSfGLQ 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  483 PYSECMNPATI----YRKVIS----------GVKPECFSRIPAQYPEIREI 519
Cdd:cd05090   226 PYYGFSNQEVIemvrKRQLLPcsedcpprmySLMTECWQEIPSRRPRFKDI 276
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
285-525 3.66e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b 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: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 63.14  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVawcelqeSKLNKTERQRFREEAEMLKD--LQHPNIVRFYdyweSADLCGKRKY--IV 360
Cdd:cd14219    11 KQIGKGRYGEVWMGKWRGEKVAV-------KVFFTTEEASWFRETEIYQTvlMRHENILGFI----AADIKGTGSWtqLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTR------NPPVIHRDLKCDNIFITgTTGSVKIGDLGLA 434
Cdd:cd14219    80 LITDYHENGSLYDYLKS-TTLDTKAMLKLAYSSVSGLCHLHTEifstqgKPAIAHRDLKSKNILVK-KNGTCCIADLGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 tLKNKSFAKSV-------IGTPEFMAPEMYEEMYDES-------VDVYAFGMCLLEM----VTG----EY--PYSECMNP 490
Cdd:cd14219   158 -VKFISDTNEVdippntrVGTKRYMPPEVLDESLNRNhfqsyimADMYSFGLILWEVarrcVSGgiveEYqlPYHDLVPS 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  491 ATIYRKVISGVkpeCFSRIPAQYPEiREIIDRCIR 525
Cdd:cd14219   237 DPSYEDMREIV---CIKRLRPSFPN-RWSSDECLR 267
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
285-543 4.38e-10

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: 62.24  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAWCELQES--KLNKTER-QRFREEAEMLKDLQ-HPNIVRFYDYWESADLcgkrkyIV 360
Cdd:cd14019     7 EKIGEGTFSSVYKAEDKLHDLYDRNKGRLVAlkHIYPTSSpSRILNELECLERLGgSNNVSGLITAFRNEDQ------VV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYlkrFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTGSVKIGDLGLAtlKNKS 440
Cdd:cd14019    81 AVLPYIEHDDFRDF---YRKMSLTDIRIYLRNLFKALKHVHSFG--IIHRDVKPGNFLYNRETGKGVLVDFGLA--QREE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  441 FAKSV----IGTPEFMAPEMYEEMYDES--VDVYAFGMCLLEMVTGEYP----YSECMNPATIyrKVISGvKPECFsrip 510
Cdd:cd14019   154 DRPEQraprAGTRGFRAPEVLFKCPHQTtaIDIWSAGVILLSILSGRFPfffsSDDIDALAEI--ATIFG-SDEAY---- 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  511 aqypeirEIIDRCIRVRREERSTVKQLLVDDFF 543
Cdd:cd14019   227 -------DLLDKLLELDPSKRITAEEALKHPFF 252
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
285-556 6.33e-10

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: 62.64  E-value: 6.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGV--AVAWCELQE-SKLNKTERQRFreEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIVL 361
Cdd:cd05574     7 KLLGKGDVGRVYLVRLKGTGKlfAMKVLDKEEmIKRNKVKRVLT--EREILATLDHPFLPTLYASFQTST------HLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  362 VTELMTSGTLKMYLKR--FKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI----------------FITGTT 423
Cdd:cd05574    79 VMDYCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLG--FVYRDLKPENIllhesghimltdfdlsKQSSVT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  424 GSVKIGDL--GLATLKNKS------------FAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPYSecm 488
Cdd:cd05574   157 PPPVRKSLrkGSRRSSVKSieketfvaepsaRSNSFVGTEEYIAPEVIKgDGHGSAVDWWTLGILLYEMLYGTTPFK--- 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  489 npatiyrkviSGVKPECFSRI---PAQYPEIREIIDRCirvrreeRSTVKQLLVDDfftPEDLIGIRV---EIK 556
Cdd:cd05574   234 ----------GSNRDETFSNIlkkELTFPESPPVSSEA-------KDLIRKLLVKD---PSKRLGSKRgasEIK 287
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
359-484 6.65e-10

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: 63.13  E-value: 6.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--L 436
Cdd:cd05618    96 LFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERG--IIYRDLKLDNVLLD-SEGHIKLTDYGMCKegL 172
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392899979  437 KNKSFAKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd05618   173 RPGDTTSTFCGTPNYIAPEILRgEDYGFSVDWWALGVLMFEMMAGRSPF 221
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
281-526 1.07e-09

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: 61.95  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLDTETGVAVAWCELQESKLNKTERQ--RFREEAEMLKDL-QHPNIVRFYDywesadLC 353
Cdd:cd05101    26 LTLGKPLGEGCFGQVVMaeavGIDKDKPKEAVTVAVKMLKDDATEKDlsDLVSEMEMMKMIgKHKNIINLLG------AC 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  354 GKRKYIVLVTELMTSGTLKMYLKRFK----------------RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI 417
Cdd:cd05101   100 TQDGPLYVIVEYASKGNLREYLRARRppgmeysydinrvpeeQMTFKDLVSCTYQLARGMEYLASQK--CIHRDLAARNV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  418 FITgTTGSVKIGDLGLA-TLKNKSFAKSVIG---TPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYS------ 485
Cdd:cd05101   178 LVT-ENNVMKIADFGLArDINNIDYYKKTTNgrlPVKWMAPEaLFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPgipvee 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  486 ---------ECMNPATIYRKVISGVKpECFSRIPAQYPEIREIIDRCIRV 526
Cdd:cd05101   257 lfkllkeghRMDKPANCTNELYMMMR-DCWHAVPSQRPTFKQLVEDLDRI 305
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
408-525 1.09e-09

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: 61.95  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  408 IHRDLKCDNIFItGTTGSVKIGDLGLAT----LKNKSF--AKSVIGTPEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTG 480
Cdd:cd05598   123 IHRDIKPDNILI-DRDGHIKLTDFGLCTgfrwTHDSKYylAHSLVGTPNYIAPEVLLrTGYTQLCDWWSVGVILYEMLVG 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392899979  481 EYPYSEcMNPATIYRKVISGvkpECFSRIPAQ---YPEIREIIDRCIR 525
Cdd:cd05598   202 QPPFLA-QTPAETQLKVINW---RTTLKIPHEanlSPEAKDLILRLCC 245
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
392-539 1.35e-09

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 62.34  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  392 QILKGLSFLHTRNppVIHRDLKCDNIFITgtTGS-VKIGDLGLA--TLKNKSF-AKSVIGTP-EFMAPE-MYEEMYDESV 465
Cdd:cd05107   247 QVANGMEFLASKN--CVHRDLAARNVLIC--EGKlVKICDFGLArdIMRDSNYiSKGSTFLPlKWMAPEsIFNNLYTTLS 322
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899979  466 DVYAFGMCLLEMVT-GEYPYSECMNPATIYRKVISGVKpecFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLV 539
Cdd:cd05107   323 DVWSFGILLWEIFTlGGTPYPELPMNEQFYNAIKRGYR---MAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVH 394
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
287-626 1.37e-09

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: 62.03  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07874    25 IGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKS-V 445
Cdd:cd07874   105 DANLCQVIQMELDHERMSYL---LYQMLCGIKHLHSAG--IIHRDLKPSNIVVK-SDCTLKILDFGLARTAGTSFMMTpY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  446 IGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGE--YPYSECMNPatiYRKVISGVKPECfsripaqyPEIREIIDR 522
Cdd:cd07874   179 VVTRYYRAPEVILGMgYKENVDIWSVGCIMGEMVRHKilFPGRDYIDQ---WNKVIEQLGTPC--------PEFMKKLQP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  523 CIRVRREERSTVKQLLVDDFFtPEDLIgirveikNRDADLNDLNV----EIQMQLRVYDEKKrkqyRFKENEGLQFAF-- 596
Cdd:cd07874   248 TVRNYVENRPKYAGLTFPKLF-PDSLF-------PADSEHNKLKAsqarDLLSKMLVIDPAK----RISVDEALQHPYin 315
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 392899979  597 ------DIENDSPDEVVQQMIEQQHIPDEDTRMITK 626
Cdd:cd07874   316 vwydpaEVEAPPPQIYDKQLDEREHTIEEWKELIYK 351
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
281-522 1.45e-09

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: 61.39  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRG-----LDTETGVAVAWCELQESKLNKTERQrFREEAEMLKDLQHPNIVRFYDywesadLCGK 355
Cdd:cd05050     7 IEYVRDIGQGAFGRVFQArapglLPYEPFTMVAVKMLKEEASADMQAD-FQREAALMAEFDHPNIVKLLG------VCAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  356 RKYIVLVTELMTSGTLKMYLKRFK----------------------RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLK 413
Cdd:cd05050    80 GKPMCLLFEYMAYGDLNEFLRHRSpraqcslshstssarkcglnplPLSCTEQLCIAKQVAAGMAYLSERK--FVHRDLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  414 CDNIFITGTTgSVKIGDLGLAtlkNKSFAKSVIGTPE-------FMAPE--MYEEMYDESvDVYAFGMCLLEMVT-GEYP 483
Cdd:cd05050   158 TRNCLVGENM-VVKIADFGLS---RNIYSADYYKASEndaipirWMPPEsiFYNRYTTES-DVWAYGVVLWEIFSyGMQP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899979  484 YSECMNPATIYR----KVISGvkPE------------CFSRIPAQYP---EIREIIDR 522
Cdd:cd05050   233 YYGMAHEEVIYYvrdgNVLSC--PDncplelynlmrlCWSKLPSDRPsfaSINRILQR 288
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
319-537 1.64e-09

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 61.07  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  319 KTERQRFREEAEMLK------DLQHPNIVRFYdyweSAdlCGKRKYIVLVTELMTSGTLK------------MYlkRFKR 380
Cdd:cd14042    37 KVNKKRIDLTREVLKelkhmrDLQHDNLTRFI----GA--CVDPPNICILTEYCPKGSLQdilenedikldwMF--RYSL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  381 INikvlkswcrQILKGLSFLHtRNPPVIHRDLKCDNIFITGTTgSVKIGDLGLATLKnkSFAKSVIGTPEF------MAP 454
Cdd:cd14042   109 IH---------DIVKGMHYLH-DSEIKSHGNLKSSNCVVDSRF-VLKITDFGLHSFR--SGQEPPDDSHAYyakllwTAP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  455 EMYEEMYDESV-----DVYAFGMCLLEMVTGEYPYSEC---MNPATIY-RKVISGVKP---ECFSRIPAQyPEIREIIDR 522
Cdd:cd14042   176 ELLRDPNPPPPgtqkgDVYSFGIILQEIATRQGPFYEEgpdLSPKEIIkKKVRNGEKPpfrPSLDELECP-DEVLSLMQR 254
                         250
                  ....*....|....*
gi 392899979  523 CIRVRREERSTVKQL 537
Cdd:cd14042   255 CWAEDPEERPDFSTL 269
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
361-503 1.67e-09

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: 61.17  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT---LK 437
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLG--IIYRDIKLENILLD-SSGHVVLTDFGLSKeflLD 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899979  438 NKSFAKSVIGTPEFMAPEMY---EEMYDESVDVYAFGMCLLEMVTGEYPYS---ECMNPATIYRKVISGVKP 503
Cdd:cd05613   159 ENERAYSFCGTIEYMAPEIVrggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILKSEPP 230
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
287-537 2.16e-09

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer 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 Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 60.72  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG-LDTETGVA--VAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVlVT 363
Cdd:cd14204    15 LGEGEFGSVMEGeLQQPDGTNhkVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVGSQRIPKPMV-IL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLKMYLKRF------KRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDLGLAT-- 435
Cdd:cd14204    94 PFMKYGDLHSFLLRSrlgsgpQHVPLQTLLKFMIDIALGMEYLSSRN--FLHRDLAARNCMLRDDM-TVCVADFGLSKki 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 -----LKNKSFAKSVIgtpEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISGVK----PE 504
Cdd:cd14204   171 ysgdyYRQGRIAKMPV---KWIAVEsLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQN-HEIYDYLLHGHRlkqpED 246
                         250       260       270
                  ....*....|....*....|....*....|...
gi 392899979  505 CFSripaqypEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd14204   247 CLD-------ELYDIMYSCWRSDPTDRPTFTQL 272
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
287-552 2.16e-09

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: 61.40  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTER-QRFREEAEMLKDLQHPNIVRFYDYWESAdlcgkrKYIVLVTEL 365
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQlAHVKAERDVLAESDSPWVVSLYYSFQDA------QYLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  366 MTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA----------- 434
Cdd:cd05629    83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLG--FIHRDIKPDNILID-RGGHIKLSDFGLStgfhkqhdsay 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 ---------------------------TLKNKS-----------FAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLL 475
Cdd:cd05629   160 yqkllqgksnknridnrnsvavdsinlTMSSKDqiatwkknrrlMAYSTVGTPDYIAPEIFlQQGYGQECDWWSLGAIMF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  476 EMVTGEYPY-SEcmNPATIYRKVISGVKPECFSRIPAQYPEIREIIDRCI-----RVRREERSTVKQllvDDFFTPEDLI 549
Cdd:cd05629   240 ECLIGWPPFcSE--NSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLItnaenRLGRGGAHEIKS---HPFFRGVDWD 314

                  ...
gi 392899979  550 GIR 552
Cdd:cd05629   315 TIR 317
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
263-489 2.32e-09

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: 61.56  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  263 DDFDAQEK-PIDKSKNGRFLKFDEE----LGRGSFKTV--FRGLDTETGVAVAWCELQEsKLNKTERQRFREEAEMLKDL 335
Cdd:cd05622    52 DNFLSRYKdTINKIRDLRMKAEDYEvvkvIGRGAFGEVqlVRHKSTRKVYAMKLLSKFE-MIKRSDSAFFWEERDIMAFA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  336 QHPNIVR-FYDYWESadlcgkrKYIVLVTELMTSGTLKMYLKrfkriNIKVLKSWCR----QILKGLSFLHTRNppVIHR 410
Cdd:cd05622   131 NSPWVVQlFYAFQDD-------RYLYMVMEYMPGGDLVNLMS-----NYDVPEKWARfytaEVVLALDAIHSMG--FIHR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  411 DLKCDNIFITgTTGSVKIGDLGLATLKNKS---FAKSVIGTPEFMAPEMYEEM-----YDESVDVYAFGMCLLEMVTGEY 482
Cdd:cd05622   197 DVKPDNMLLD-KSGHLKLADFGTCMKMNKEgmvRCDTAVGTPDYISPEVLKSQggdgyYGRECDWWSVGVFLYEMLVGDT 275
                         250
                  ....*....|....*.
gi 392899979  483 P---------YSECMN 489
Cdd:cd05622   276 PfyadslvgtYSKIMN 291
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
261-487 2.41e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 61.23  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  261 VEDDFDAQEKPIDKSKNGRFLKFDEELGRGSFKTVFRGLDTeTGVAVAWCElqesklnkterqrfreEAEMLKDLQHPNI 340
Cdd:cd07868    14 VEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEG-TGISMSACR----------------EIALLRELKHPNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  341 VRFYDYWESAdlcGKRKYIVLVTELMTSGTLKMYLKRFKRINIK-------VLKSWCRQILKGLSFLHTRnpPVIHRDLK 413
Cdd:cd07868    77 ISLQKVFLSH---ADRKVWLLFDYAEHDLWHIIKFHRASKANKKpvqlprgMVKSLLYQILDGIHYLHAN--WVLHRDLK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  414 CDNIFITG---TTGSVKIGDLGLATLKNKSFA-----KSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEyP 483
Cdd:cd07868   152 PANILVMGegpERGRVKIADMGFARLFNSPLKpladlDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCIFAELLTSE-P 230

                  ....
gi 392899979  484 YSEC 487
Cdd:cd07868   231 IFHC 234
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
287-563 4.35e-09

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: 60.46  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVR-FYDYWEsadlcgkRKYIVLVTE 364
Cdd:cd05627    10 IGRGAFGEVRLVQKKDTGHIYAMKILRKADmLEKEQVAHIRAERDILVEADGAWVVKmFYSFQD-------KRNLYLIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKN----- 438
Cdd:cd05627    83 FLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLG--FIHRDIKPDNLLLD-AKGHVKLSDFGLCTgLKKahrte 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 -------------------------------KSFAKSVIGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGeYPYSE 486
Cdd:cd05627   160 fyrnlthnppsdfsfqnmnskrkaetwkknrRQLAYSTVGTPDYIAPEVFMQTgYNKLCDWWSLGVIMYEMLIG-YPPFC 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  487 CMNPATIYRKVISGVKPECFsriPAQYP---EIREIIDR-CIRVR-REERSTVKQLLVDDFFTPEDLIGIR-------VE 554
Cdd:cd05627   239 SETPQETYRKVMNWKETLVF---PPEVPiseKAKDLILRfCTDAEnRIGSNGVEEIKSHPFFEGVDWEHIRerpaaipIE 315

                  ....*....
gi 392899979  555 IKNRDADLN 563
Cdd:cd05627   316 IKSIDDTSN 324
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
336-481 4.51e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 59.34  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  336 QHPNIVRFYDYWESADlcgkrkYIVLVTELMTSGTLKMYLKRFKRINIKV----LKSWCRQILKGLSFLHTRNppVIHRD 411
Cdd:cd14051    58 KHPHVVRYYSAWAEDD------HMIIQNEYCNGGSLADAISENEKAGERFseaeLKDLLLQVAQGLKYIHSQN--LVHMD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  412 LKCDNIFITGTTGSV-----------------------KIGDLGLATLKNKSFAKSviGTPEFMAPEMYEEMYDE--SVD 466
Cdd:cd14051   130 IKPGNIFISRTPNPVsseeeeedfegeednpesnevtyKIGDLGHVTSISNPQVEE--GDCRFLANEILQENYSHlpKAD 207
                         170
                  ....*....|....*
gi 392899979  467 VYAFGMCLLEMVTGE 481
Cdd:cd14051   208 IFALALTVYEAAGGG 222
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
392-531 4.53e-09

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: 59.33  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  392 QILKGLSFLHTRNppVIHRDLKCDNIFITGTtGSVKIGDLGLATL---KNKSFAKSVIGTPEFMAPEMY---EEMYDESV 465
Cdd:cd05583   107 EIVLALEHLHKLG--IIYRDIKLENILLDSE-GHVVLTDFGLSKEflpGENDRAYSFCGTIEYMAPEVVrggSDGHDKAV 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  466 DVYAFGMCLLEMVTGEYPYS---ECMNPATIYRKVISGVKPecfsrIPAQY-PEIREIIDRCIRVRREER 531
Cdd:cd05583   184 DWWSLGVLTYELLTGASPFTvdgERNSQSEISKRILKSHPP-----IPKTFsAEAKDFILKLLEKDPKKR 248
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
392-538 4.96e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 61.04  E-value: 4.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  392 QILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFA----KSVIGTPEFMAPEMYEEM-YDESVD 466
Cdd:PTZ00283  151 QVLLAVHHVHSKH--MIHRDIKSANILLC-SNGLVKLGDFGFSKMYAATVSddvgRTFCGTPYYVAPEIWRRKpYSKKAD 227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392899979  467 VYAFGMCLLEMVTGEYPYsECMNPATIYRKVISGVkpecFSRIPAQY-PEIREIIDRCIRVRREERSTVKQLL 538
Cdd:PTZ00283  228 MFSLGVLLYELLTLKRPF-DGENMEEVMHKTLAGR----YDPLPPSIsPEMQEIVTALLSSDPKRRPSSSKLL 295
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
286-521 5.41e-09

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 59.28  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  286 ELGRGSFKTVFRGL-------DTETGVAVAwcELQESKlNKTERQRFREEAEMLKDLQHPNIVRFYDywesadLCGKRKY 358
Cdd:cd05062    13 ELGQGSFGMVYEGIakgvvkdEPETRVAIK--TVNEAA-SMRERIEFLNEASVMKEFNCHHVVRLLG------VVSQGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKR----------INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItGTTGSVKI 428
Cdd:cd05062    84 TLVIMELMTRGDLKSYLRSLRPemennpvqapPSLKKMIQMAGEIADGMAYLNANK--FVHRDLAARNCMV-AEDFTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLA-----TLKNKSFAKSVIGTpEFMAPEMYEE-MYDESVDVYAFGMCLLEMVT-GEYPYsECMNPATIYRKVISG- 500
Cdd:cd05062   161 GDFGMTrdiyeTDYYRKGGKGLLPV-RWMSPESLKDgVFTTYSDVWSFGVVLWEIATlAEQPY-QGMSNEQVLRFVMEGg 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392899979  501 --VKPE------------CFSRIPAQYPEIREIID 521
Cdd:cd05062   239 llDKPDncpdmlfelmrmCWQYNPKMRPSFLEIIS 273
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
284-538 6.12e-09

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: 58.68  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  284 DEELGRGSFKTVFRGLDTETGVAVAwcelqeSKLNKTERQRFREeAEMLKDLQHPNIVRFYDYWESadlcgKRKYIVLVT 363
Cdd:cd14109     9 EEDEKRAAQGAPFHVTERSTGRNFL------AQLRYGDPFLMRE-VDIHNSLDHPNIVQMHDAYDD-----EKLAVTVID 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  364 ELMTSGTLkmylkrfKRINIKVLKSWC---------RQILKGLSFLHTRNppVIHRDLKCDNIFItgTTGSVKIGDLGLA 434
Cdd:cd14109    77 NLASTIEL-------VRDNLLPGKDYYterqvavfvRQLLLALKHMHDLG--IAHLDLRPEDILL--QDDKLKLADFGQS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  435 -TLKNKSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIyRKVISG---VKPECFSRI 509
Cdd:cd14109   146 rRLLRGKLTTLIYGSPEFVSPEIVnSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETL-TNVRSGkwsFDSSPLGNI 224
                         250       260
                  ....*....|....*....|....*....
gi 392899979  510 PAqypEIREIIDRCIRVRREERSTVKQLL 538
Cdd:cd14109   225 SD---DARDFIKKLLVYIPESRLTVDEAL 250
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
281-537 6.66e-09

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: 58.87  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFRGLDTETG--VAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKY 358
Cdd:cd05075     2 LALGKTLGEGEFGSVMEGQLNQDDsvLKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESEGYPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLkRFKRIN-------IKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKIGDL 431
Cdd:cd05075    82 PVVILPFMKHGDLHSFL-LYSRLGdcpvylpTQMLVKFMTDIASGMEYLSSKN--FIHRDLAARNCMLNENM-NVCVADF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  432 GLAT-LKNKSFAKS--VIGTP-EFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSECMNpATIYRKVISGVK--- 502
Cdd:cd05075   158 GLSKkIYNGDYYRQgrISKMPvKWIAIEsLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVEN-SEIYDYLRQGNRlkq 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 392899979  503 -PECFSripaqypEIREIIDRCIRVRREERSTVKQL 537
Cdd:cd05075   237 pPDCLD-------GLYELMSSCWLLNPKDRPSFETL 265
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
328-487 7.96e-09

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 59.31  E-value: 7.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  328 EAEMLKDLQHPNIVRF---------------YDYWESaDLCgkrkYIVLVTELMTSGTLKMYLKRfkriniKVLKSWCRQ 392
Cdd:cd07867    49 EIALLRELKHPNVIALqkvflshsdrkvwllFDYAEH-DLW----HIIKFHRASKANKKPMQLPR------SMVKSLLYQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  393 ILKGLSFLHTRnpPVIHRDLKCDNIFITG---TTGSVKIGDLGLATLKNKSFA-----KSVIGTPEFMAPEMY--EEMYD 462
Cdd:cd07867   118 ILDGIHYLHAN--WVLHRDLKPANILVMGegpERGRVKIADMGFARLFNSPLKpladlDPVVVTFWYRAPELLlgARHYT 195
                         170       180
                  ....*....|....*....|....*
gi 392899979  463 ESVDVYAFGMCLLEMVTGEyPYSEC 487
Cdd:cd07867   196 KAIDIWAIGCIFAELLTSE-PIFHC 219
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
320-537 8.46e-09

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 58.72  E-value: 8.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  320 TERQRFREEAEMLKDLQHPNIVRFydywesADLCGKRKYIVLVTELMTSGTLK-MYLKRFKRINIKVLKSWCRQILKGLS 398
Cdd:cd14045    44 TLSKRIRKEVKQVRELDHPNLCKF------IGGCIEVPNVAIITEYCPKGSLNdVLLNEDIPLNWGFRFSFATDIARGMA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  399 FLHtrNPPVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKSVIGTPE-----FMAPEMYEEMYDE---SVDVYAF 470
Cdd:cd14045   118 YLH--QHKIYHGRLKSSNCVID-DRWVCKIADYGLTTYRKEDGSENASGYQQrlmqvYLPPENHSNTDTEptqATDVYSY 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  471 GMCLLEMVT-------GEYPYSECMNPAtiYRKVISGvKPECFSRIPAQYpeiREIIDRCIRVRREERSTVKQL 537
Cdd:cd14045   195 AIILLEIATrndpvpeDDYSLDEAWCPP--LPELISG-KTENSCPCPADY---VELIRRCRKNNPAQRPTFEQI 262
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
287-521 8.66e-09

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: 59.67  E-value: 8.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELM 366
Cdd:cd07875    32 IGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELM 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLATLKNKSFAKS-V 445
Cdd:cd07875   112 DANLCQVIQMELDHERMSYL---LYQMLCGIKHLHSAG--IIHRDLKPSNIVVK-SDCTLKILDFGLARTAGTSFMMTpY 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  446 IGTPEFMAPEMYEEM-YDESVDVYAFGMCLLEMVTGE--YPYSECMNPatiYRKVISGVKPECFSRIPAQYPEIREIID 521
Cdd:cd07875   186 VVTRYYRAPEVILGMgYKENVDIWSVGCIMGEMIKGGvlFPGTDHIDQ---WNKVIEQLGTPCPEFMKKLQPTVRTYVE 261
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
287-504 1.12e-08

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: 58.47  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWEsadlcgKRKYIVLVTELM 366
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFR------RRGKLYLVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  367 TSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLA---TLKNKSFAK 443
Cdd:cd07848    83 EKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKND--IVHRDIKPENLLIS-HNDVLKLCDFGFArnlSEGSNANYT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899979  444 SVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGE--YPYSECMNPATIYRKVISGVKPE 504
Cdd:cd07848   160 EYVATRWYRSPElLLGAPYGKAVDMWSVGCILGELSDGQplFPGESEIDQLFTIQKVLGPLPAE 223
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
287-563 1.22e-08

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: 59.28  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVR-FYDYWESADLcgkrkyiVLVTE 364
Cdd:cd05628     9 IGRGAFGEVRLVQKKDTGHVYAMKILRKADmLEKEQVGHIRAERDILVEADSLWVVKmFYSFQDKLNL-------YLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT-LKN----- 438
Cdd:cd05628    82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLG--FIHRDIKPDNLLLD-SKGHVKLSDFGLCTgLKKahrte 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  439 -------------------------------KSFAKSVIGTPEFMAPEMY-EEMYDESVDVYAFGMCLLEMVTGEYPYSE 486
Cdd:cd05628   159 fyrnlnhslpsdftfqnmnskrkaetwkrnrRQLAFSTVGTPDYIAPEVFmQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  487 cMNPATIYRKVISGVKPECFsriPAQYP---EIREIIDR--CIRVRREERSTVKQLLVDDFFTPEDLIGIR-------VE 554
Cdd:cd05628   239 -ETPQETYKKVMNWKETLIF---PPEVPiseKAKDLILRfcCEWEHRIGAPGVEEIKTNPFFEGVDWEHIRerpaaipIE 314

                  ....*....
gi 392899979  555 IKNRDADLN 563
Cdd:cd05628   315 IKSIDDTSN 323
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
386-538 1.29e-08

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 59.15  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  386 LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFItgTTGSV-KIGDLGLA-TLKNKS--FAKSVIGTP-EFMAPE-MYEE 459
Cdd:cd05104   216 LLSFSYQVAKGMEFLASKN--CIHRDLAARNILL--THGRItKICDFGLArDIRNDSnyVVKGNARLPvKWMAPEsIFEC 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  460 MYDESVDVYAFGMCLLEMVT-GEYPYSECMNPATIYRKVISGVK---PECFSripaqyPEIREIIDRCIRVRREERSTVK 535
Cdd:cd05104   292 VYTFESDVWSYGILLWEIFSlGSSPYPGMPVDSKFYKMIKEGYRmdsPEFAP------SEMYDIMRSCWDADPLKRPTFK 365

                  ...
gi 392899979  536 QLL 538
Cdd:cd05104   366 QIV 368
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
281-526 1.40e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 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 FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 58.49  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  281 LKFDEELGRGSFKTVFR----GLDTE---TGVAVAWCELQESKLNKtERQRFREEAEMLKDL-QHPNIVRFYDywesadL 352
Cdd:cd05100    14 LTLGKPLGEGCFGQVVMaeaiGIDKDkpnKPVTVAVKMLKDDATDK-DLSDLVSEMEMMKMIgKHKNIINLLG------A 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  353 CGKRKYIVLVTELMTSGTLKMYLKRFK----------------RINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDN 416
Cdd:cd05100    87 CTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQK--CIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  417 IFITgTTGSVKIGDLGLA-TLKNKSFAKSVIG---TPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYS----- 485
Cdd:cd05100   165 VLVT-EDNVMKIADFGLArDVHNIDYYKKTTNgrlPVKWMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPgipve 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  486 ----------ECMNPATIYRKVISgVKPECFSRIPAQYPEIREIIDRCIRV 526
Cdd:cd05100   244 elfkllkeghRMDKPANCTHELYM-IMRECWHAVPSQRPTFKQLVEDLDRV 293
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
282-521 1.90e-08

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: 57.27  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  282 KFDEELGRGSFKTVFRGLDTETGVAVAW-CELQEsklnkTERQRFREEAEMLKDLQ-HPNIVRFYDywesadlCGKRK-- 357
Cdd:cd14017     3 KVVKKIGGGGFGEIYKVRDVVDGEEVAMkVESKS-----QPKQVLKMEVAVLKKLQgKPHFCRLIG-------CGRTEry 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 -YIVlvtelMTS-----GTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHtrNPPVIHRDLKCDNiFITGTTGS----VK 427
Cdd:cd14017    71 nYIV-----MTLlgpnlAELRRSQPR-GKFSVSTTLRLGIQILKAIEDIH--EVGFLHRDVKPSN-FAIGRGPSdertVY 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  428 IGDLGLA---TLKNKSFAKSVIGTPEFMAPEMY--------EEM--YDesvDVYAFGMCLLEMVTGEYPYSECMNPATI- 493
Cdd:cd14017   142 ILDFGLArqyTNKDGEVERPPRNAAGFRGTVRYasvnahrnKEQgrRD---DLWSWFYMLIEFVTGQLPWRKLKDKEEVg 218
                         250       260
                  ....*....|....*....|....*....
gi 392899979  494 -YRKVISgvKPECFSRIPAQYPEIREIID 521
Cdd:cd14017   219 kMKEKID--HEELLKGLPKEFFQILKHIR 245
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
285-472 2.10e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 57.34  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  285 EELGRGSFKTVFRGLDTETGVAVAwceLQESKL----NKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkYIV 360
Cdd:cd14138    11 EKIGSGEFGSVFKCVKRLDGCIYA---IKRSKKplagSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDD------HML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  361 LVTELMTSGTLKMYL----KRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTT------------- 423
Cdd:cd14138    82 IQNEYCNGGSLADAIsenyRIMSYFTEPELKDLLLQVARGLKYIHSMS--LVHMDIKPSNIFISRTSipnaaseegdede 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899979  424 ---GSV--KIGDLGLATLKNKSFAKSviGTPEFMAPEMYEEMYDE--SVDVYAFGM 472
Cdd:cd14138   160 wasNKVifKIGDLGHVTRVSSPQVEE--GDSRFLANEVLQENYTHlpKADIFALAL 213
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
269-489 2.42e-08

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: 58.16  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  269 EKPIDKSKNGRFLKFDEE----LGRGSFKTV--FRGLDTETGVAVawcelqeSKLNKTERQR------FREEAEMLKDLQ 336
Cdd:cd05596    12 EKPVNEITKLRMNAEDFDvikvIGRGAFGEVqlVRHKSTKKVYAM-------KLLSKFEMIKrsdsafFWEERDIMAHAN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  337 HPNIVRFYDYWESAdlcgkrKYIVLVTELMTSGTLKMYLKRFKrINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDN 416
Cdd:cd05596    85 SEWIVQLHYAFQDD------KYLYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMG--FVHRDVKPDN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  417 IFITGTtGSVKIGDLGLATLKNKS---FAKSVIGTPEFMAPEMYEE-----MYDESVDVYAFGMCLLEMVTGEYP----- 483
Cdd:cd05596   156 MLLDAS-GHLKLADFGTCMKMDKDglvRSDTAVGTPDYISPEVLKSqggdgVYGRECDWWSVGVFLYEMLVGDTPfyads 234
                         250
                  ....*....|
gi 392899979  484 ----YSECMN 489
Cdd:cd05596   235 lvgtYGKIMN 244
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
287-483 3.32e-08

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 57.83  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWcelqesKLNKTERQRFREEAEMLKDLQH---------PNIVRFYDYWESadlcgkRK 357
Cdd:cd14224    73 IGKGSFGQVVKAYDHKTHQHVAL------KMVRNEKRFHRQAAEEIRILEHlkkqdkdntMNVIHMLESFTF------RN 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 YIVLVTELMtSGTLKMYLKR--FKRINIKVLKSWCRQILKGLSFLHtRNPpVIHRDLKCDNIFIT--GTTGsVKIGDLGL 433
Cdd:cd14224   141 HICMTFELL-SMNLYELIKKnkFQGFSLQLVRKFAHSILQCLDALH-RNK-IIHCDLKPENILLKqqGRSG-IKVIDFGS 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392899979  434 ATLKNKSFAkSVIGTPEFMAPE-MYEEMYDESVDVYAFGMCLLEMVTGeYP 483
Cdd:cd14224   217 SCYEHQRIY-TYIQSRFYRAPEvILGARYGMPIDMWSFGCILAELLTG-YP 265
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
290-544 3.40e-08

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 57.08  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  290 GSFKTVFRG-LDTETGVavawcelQESKLNKTERQ--------RFREEAEMLKDLQHPNIvrfydyweSADLC----GKR 356
Cdd:cd05043    17 GTFGRIFHGiLRDEKGK-------EEEVLVKTVKDhaseiqvtMLLQESSLLYGLSHQNL--------LPILHvcieDGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  357 KYIVLVTeLMTSGTLKMYLKRFKRINIKV--------LKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITGTTgSVKI 428
Cdd:cd05043    82 KPMVLYP-YMNWGNLKLFLQQCRLSEANNpqalstqqLVHMALQIACGMSYLHRRG--VIHKDIAARNCVIDDEL-QVKI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDlglATLKNKSFAKS--VIGTPE-----FMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKVIS 499
Cdd:cd05043   158 TD---NALSRDLFPMDyhCLGDNEnrpikWMSLEsLVNKEYSSASDVWSFGVLLWELMTlGQTPYVE-IDPFEMAAYLKD 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 392899979  500 GVkpecfsRI--PAQYP-EIREIIDRCIRVRREERSTVKQLL--VDDFFT 544
Cdd:cd05043   234 GY------RLaqPINCPdELFAVMACCWALDPEERPSFQQLVqcLTDFHA 277
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
287-522 3.79e-08

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 56.71  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRG--LDT---ETGVAVawcelqeSKLNKT----ERQRFREEAEMLKDLQHPNIVrfydywesaDLCGkrk 357
Cdd:cd05058     3 IGKGHFGCVYHGtlIDSdgqKIHCAV-------KSLNRItdieEVEQFLKEGIIMKDFSHPNVL---------SLLG--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  358 yIVLVTE--------LMTSGTLKMYLKRFKR-INIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKI 428
Cdd:cd05058    64 -ICLPSEgsplvvlpYMKHGDLRNFIRSETHnPTVKDLIGFGLQVAKGMEYLASKK--FVHRDLAARNCMLD-ESFTVKV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  429 GDLGLA---------TLKNKSFAKSVIgtpEFMAPE-MYEEMYDESVDVYAFGMCLLEMVT-GEYPYSEcMNPATIYRKV 497
Cdd:cd05058   140 ADFGLArdiydkeyySVHNHTGAKLPV---KWMALEsLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPD-VDSFDITVYL 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 392899979  498 ISG---VKPE------------CFSRIPAQYPEIREIIDR 522
Cdd:cd05058   216 LQGrrlLQPEycpdplyevmlsCWHPKPEMRPTFSELVSR 255
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
277-484 4.04e-08

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: 56.39  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  277 NGRFlKFDEELGRGSFKTVFRGLD--TETGVAVAwCELQESKLNKTERQRfreEAEMLKDLQHPNIVRFYDYWEsadlcg 354
Cdd:cd14112     2 TGRF-SFGSEIFRGRFSVIVKAVDstTETDAHCA-VKIFEVSDEASEAVR---EFESLRTLQHENVQRLIAAFK------ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  355 KRKYIVLVTELMTSGTLKMYLKRfKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNI-FITGTTGSVKIGDLGL 433
Cdd:cd14112    71 PSNFAYLVMEKLQEDVFTRFSSN-DYYSEEQVATTVRQILDALHYLHFKG--IAHLDVQPDNImFQSVRSWQVKLVDFGR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  434 ATLKNKSFAKSVIGTPEFMAPEMY--EEMYDESVDVYAFGMCLLEMVTGEYPY 484
Cdd:cd14112   148 AQKVSKLGKVPVDGDTDWASPEFHnpETPITVQSDIWGLGVLTFCLLSGFHPF 200
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
287-480 4.32e-08

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 56.43  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAWCElQESKLN-KTERQRFREEAEMLKDLQHPNIVRFYDYW-ESADLCgkrkyivLVTE 364
Cdd:cd14160     1 IGEGEIFEVYRVRIGNRSYAVKLFK-QEKKMQwKKHWKRFLSELEVLLLFQHPNILELAAYFtETEKFC-------LVYP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  365 LMTSGTLkmyLKRFKRINIKVLKSWCRQ--ILKGLS----FLHTRNP-PVIHRDLKCDNIFITGTTgSVKIGDLGLATLK 437
Cdd:cd14160    73 YMQNGTL---FDRLQCHGVTKPLSWHERinILIGIAkaihYLHNSQPcTVICGNISSANILLDDQM-QPKLTDFALAHFR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392899979  438 NKSFAKS---VIGTPE----FMAPEMYEEMYDESV--DVYAFGMCLLEMVTG 480
Cdd:cd14160   149 PHLEDQSctiNMTTALhkhlWYMPEEYIRQGKLSVktDVYSFGIVIMEVLTG 200
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
280-548 6.50e-08

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: 56.94  E-value: 6.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  280 FLKFdEELGRGSFKTVFRGLDTETGVAVAWCELQESK-LNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADlcgkrkY 358
Cdd:cd05626     3 FVKI-KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDvLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKD------N 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  359 IVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLGLAT--- 435
Cdd:cd05626    76 LYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMG--FIHRDIKPDNILID-LDGHIKLTDFGLCTgfr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  436 ------------------------------------LK----------NKSFAKSVIGTPEFMAPE-MYEEMYDESVDVY 468
Cdd:cd05626   153 wthnskyyqkgshirqdsmepsdlwddvsncrcgdrLKtleqratkqhQRCLAHSLVGTPNYIAPEvLLRKGYTQLCDWW 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  469 AFGMCLLEMVTGEYPYSeCMNPATIYRKVISGvkpECFSRIPAQY---PEIREIIDR--CIRVRREERSTVKQLLVDDFF 543
Cdd:cd05626   233 SVGVILFEMLVGQPPFL-APTPTETQLKVINW---ENTLHIPPQVklsPEAVDLITKlcCSAEERLGRNGADDIKAHPFF 308

                  ....*
gi 392899979  544 TPEDL 548
Cdd:cd05626   309 SEVDF 313
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
222-498 7.17e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 57.01  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  222 DGPRTLTgdDMDKMVSEEERARKEQEKREEEEKAARRIDveDDFDAQEKPIDKSKNGRFLK-FDEELGRGSFKTVFRGLD 300
Cdd:PHA03210  107 DGPSGAE--DSDASHLDFDEAPPDAAGPVPLAQAKLKHD--DEFLAHFRVIDDLPAGAFGKiFICALRASTEEAEARRGV 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  301 TETGVAVAWCELQESK-LNKTERQRFREEAEML--KDLQHPNIVRFYDYWESADLCG--KRKYIVLVTELMTSGTLKM-- 373
Cdd:PHA03210  183 NSTNQGKPKCERLIAKrVKAGSRAAIQLENEILalGRLNHENILKIEEILRSEANTYmiTQKYDFDLYSFMYDEAFDWkd 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  374 --YLKRFKRInikvlkswCRQILKGLSFLHTRNppVIHRDLKCDNIFITGtTGSVKIGDLGLATLKNK---SFAKSVIGT 448
Cdd:PHA03210  263 rpLLKQTRAI--------MKQLLCAVEYIHDKK--LIHRDIKLENIFLNC-DGKIVLGDFGTAMPFEKereAFDYGWVGT 331
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392899979  449 PEFMAPEMYE-EMYDESVDVYAFGMCLLEMVTGEY-PYSE-CMNPATIYRKVI 498
Cdd:PHA03210  332 VATNSPEILAgDGYCEITDIWSCGLILLDMLSHDFcPIGDgGGKPGKQLLKII 384
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
287-432 8.28e-08

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: 52.83  E-value: 8.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899979  287 LGRGSFKTVFRGLDTETGVAVAwceLQESKL-NKTERQRFREEAEMLKDLQ--HPNIVRFYDYWESADlcgkrkYIVLVT 363
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVA---VKIGDDvNNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDG------PNILLM 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392899979  364 ELMTSGTLKMYLKRFKRINIKVlKSWCRQILKGLSFLHTRNppVIHRDLKCDNIFITgTTGSVKIGDLG 432
Cdd:cd13968    72 ELVKGGTLIAYTQEEELDEKDV-ESIMYQLAECMRLLHSFH--LIHRDLNNDNILLS-EDGNVKLIDFG 136
 
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.
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