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Conserved domains on  [gi|922581144|ref|NP_001300142|]
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non-specific serine/threonine protein kinase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
900-1212 3.00e-78

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


:

Pssm-ID: 214481  Cd Length: 302  Bit Score: 260.36  E-value: 3.00e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    900 RVAQCCAIIDRS-KIVIGFSDHGLYCIEISRQlliPVGGEKENKQRCVETVEYDEAEQLLMMIVG----PAKDRHVRIV- 973
Cdd:smart00036    1 NTAKWNHPITCDgKWLLVGTEEGLYVLNISDQ---PGTLEKLIGRRSVTQIWVLEENNVLLMISGkkpqLYSHPLSALVe 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    974 -----PSAALDGRDLKWIKVNDTKGCHLLAVGtNNPggRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLampgtPQSIAI 1048
Cdd:smart00036   78 kkealGSARLVIRKNVLTKIPDVKGCHLCAVV-NGK--RSLFLCVALQSSVVLLQWYNPLKKFKLFKSK-----FLFPLI 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1049 FNGRLYVGFSHSF--RSWSLVGVDSSPvgsgdasGAVLQHIS-LVNMEDTSLQFLNQQTSYEAKLIVNVPGspDEYLLVF 1125
Cdd:smart00036  150 SPVPVFVELVSSSfeRPGICIGSDKGG-------GDVVQFHEsLVSKEDLSLPFLSEETSLKPISVVQVPR--DEVLLCY 220

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1126 NMIGLYVNEMG-RRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRsakPLSGDGILSTclcNDS 1204
Cdd:smart00036  221 DEFGVFVNLYGkRRSRNPILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADR---ETRKIRLLGS---SDR 294


                    ....*...
gi 922581144   1205 PIFVLLQN 1212
Cdd:smart00036  295 KILLSSSP 302
PH_MRCK cd01243
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ...
 734-877 7.40e-68

MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269949  Cd Length: 135  Bit Score: 224.10  E-value: 7.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  734 PLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDrqnKMQDVKNEIRLVLDMRDPDFTVCGVSE 813
Cdd:cd01243     1 PLGIDPTRGIGTAYEGYVRVPKPGGVKKGWQRQFAVVCDFKLFLFDISED---KASQPSQVASQVLDMRDEEFSVSSVLA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  814 ADVIHAQKGDIPKIFRVTTTQILNssseysSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRS 877
Cdd:cd01243    78 SDVIHANKKDIPCIFRVSASQLAP------PSLKFSLLMLADSENEKQKWVDALNELHKLLKKN 135
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 1-135 1.67e-67

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05597:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 331  Bit Score: 231.08  E-value: 1.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05597   201 MLYGETPFYAESLVETYGKIMNHKEHFSFPDDEDD--VSEEAKDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDWDNIR 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSYT 135
Cdd:cd05597   279 DSTPPYIPEVTSPTDTSNFDVD--DDDLRHTDSLPPPSNAAFSGLHLPFVGFTYT 331
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 676-728 1.06e-27

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410359  Cd Length: 53  Bit Score: 106.59  E-value: 1.06e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCPVP 53
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 8.74e-19

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 92.81  E-value: 8.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   172 MVELENEKAELVQKLKEAQTIIAQHvaenprSEEDRNYESTIAQLKDEIQILNKRLEDEalaqqqqkpkdeivaesEKKL 251
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEEL------TAELQELEEKLEELRLEVSELEEEIEEL-----------------QKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   252 KELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADF 331
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   332 EEKLKEIETE------KIALIKKQEEVtiearksvetddhLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDE----E 401
Cdd:TIGR02168  371 ESRLEELEEQletlrsKVAQLELQIAS-------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkE 437

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   402 RASHTAQSEQEMKQLEAHYERAQ---KMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEK 476
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 1262-1300 2.43e-07

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


:

Pssm-ID: 197628  Cd Length: 36  Bit Score: 47.97  E-value: 2.43e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 922581144   1262 ISTPSDFMHIVHMGPAPVMelqQNFIDLQSNHSHTSSDK 1300
Cdd:smart00285    1 ISTPTNFKHIAHVGFDGQT---GGFTGLPTEWKSLLKTS 36
 
Name Accession Description Interval E-value
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
900-1212 3.00e-78

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


Pssm-ID: 214481  Cd Length: 302  Bit Score: 260.36  E-value: 3.00e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    900 RVAQCCAIIDRS-KIVIGFSDHGLYCIEISRQlliPVGGEKENKQRCVETVEYDEAEQLLMMIVG----PAKDRHVRIV- 973
Cdd:smart00036    1 NTAKWNHPITCDgKWLLVGTEEGLYVLNISDQ---PGTLEKLIGRRSVTQIWVLEENNVLLMISGkkpqLYSHPLSALVe 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    974 -----PSAALDGRDLKWIKVNDTKGCHLLAVGtNNPggRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLampgtPQSIAI 1048
Cdd:smart00036   78 kkealGSARLVIRKNVLTKIPDVKGCHLCAVV-NGK--RSLFLCVALQSSVVLLQWYNPLKKFKLFKSK-----FLFPLI 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1049 FNGRLYVGFSHSF--RSWSLVGVDSSPvgsgdasGAVLQHIS-LVNMEDTSLQFLNQQTSYEAKLIVNVPGspDEYLLVF 1125
Cdd:smart00036  150 SPVPVFVELVSSSfeRPGICIGSDKGG-------GDVVQFHEsLVSKEDLSLPFLSEETSLKPISVVQVPR--DEVLLCY 220

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1126 NMIGLYVNEMG-RRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRsakPLSGDGILSTclcNDS 1204
Cdd:smart00036  221 DEFGVFVNLYGkRRSRNPILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADR---ETRKIRLLGS---SDR 294


                    ....*...
gi 922581144   1205 PIFVLLQN 1212
Cdd:smart00036  295 KILLSSSP 302
PH_MRCK cd01243
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ...
 734-877 7.40e-68

MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269949  Cd Length: 135  Bit Score: 224.10  E-value: 7.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  734 PLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDrqnKMQDVKNEIRLVLDMRDPDFTVCGVSE 813
Cdd:cd01243     1 PLGIDPTRGIGTAYEGYVRVPKPGGVKKGWQRQFAVVCDFKLFLFDISED---KASQPSQVASQVLDMRDEEFSVSSVLA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  814 ADVIHAQKGDIPKIFRVTTTQILNssseysSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRS 877
Cdd:cd01243    78 SDVIHANKKDIPCIFRVSASQLAP------PSLKFSLLMLADSENEKQKWVDALNELHKLLKKN 135
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 1-135 1.67e-67

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: 231.08  E-value: 1.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05597   201 MLYGETPFYAESLVETYGKIMNHKEHFSFPDDEDD--VSEEAKDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDWDNIR 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSYT 135
Cdd:cd05597   279 DSTPPYIPEVTSPTDTSNFDVD--DDDLRHTDSLPPPSNAAFSGLHLPFVGFTYT 331
CNH pfam00780
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ...
 909-1190 5.85e-38

CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.


Pssm-ID: 459938  Cd Length: 261  Bit Score: 143.54  E-value: 5.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   909 DRSKIVIGfSDHGLYCIEISRQL-LIPVGGEKENKQrcvetVEYDEAEQLLMMIVGpaKDRHVRIVPSAALDGRDL---- 983
Cdd:pfam00780    1 GGQNLLLG-TEEGLYVLNRSGPRePVRIIDKKRVTQ-----LAVLEEFNLLLLLSG--KDKRLYVYPLSALDSREEndrk 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   984 --KWIKVNDTKGCHLLAVGTNNpGGRagFFAVAFKKSVTIFQIDRSE-KRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHS 1060
Cdd:pfam00780   73 daAKNKLPETKGCHFFKVGRHS-NGR--FLVVAVKRTIKLLEWYEPLlDKFRKFKEFYLPSPPVSIELLKSKLCVGCAKG 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  1061 FrswSLVGVDSSPVGSGDasgavlqhislvnmedTSLQFLNQQTSYEAKLIVNVpgSPDEYLLVFNMIGLYVNEMGRRSR 1140
Cdd:pfam00780  150 F---EIVSLDSKATESLL----------------TSLLFANRQENLKPLAVVRL--DRSEFLLCYNEFGVYVNLQGRRSR 208

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 922581144  1141 LPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPL 1190
Cdd:pfam00780  209 PWEIEWEGAPEAVAYLYPYLLAFHDNFIEIRDVETGELVQEIAGRKIRFL 258
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 676-728 1.06e-27

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 106.59  E-value: 1.06e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCPVP 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 8.74e-19

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 92.81  E-value: 8.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   172 MVELENEKAELVQKLKEAQTIIAQHvaenprSEEDRNYESTIAQLKDEIQILNKRLEDEalaqqqqkpkdeivaesEKKL 251
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEEL------TAELQELEEKLEELRLEVSELEEEIEEL-----------------QKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   252 KELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADF 331
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   332 EEKLKEIETE------KIALIKKQEEVtiearksvetddhLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDE----E 401
Cdd:TIGR02168  371 ESRLEELEEQletlrsKVAQLELQIAS-------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkE 437

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   402 RASHTAQSEQEMKQLEAHYERAQ---KMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEK 476
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 143-465 1.45e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 88.84  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  143 ARSLTDEIRAIaqrcqgDAELMEKSVDgfmvELENEKAELVQKLKEAQTIIAQHVAENprseedRNYESTIAQLKDEIQI 222
Cdd:COG1196   215 YRELKEELKEL------EAELLLLKLR----ELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  223 LNKRLEDealAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELAD 302
Cdd:COG1196   279 LELELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  303 VGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVA-AKNTIASLQ 381
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEE 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  382 ATNEERETEIKKLKQRMDEERAShtAQSEQEMKQLEAHYERAQKMLQDNVEQMNvENRGLRDEIEKLSQQMAALPRGGLN 461
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYEGFLEGVKA 512


                  ....
gi 922581144  462 EQQL 465
Cdd:COG1196   513 ALLL 516
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 177-583 4.21e-16

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 84.07  E-value: 4.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   177 NEKAELVQKLKEAQTIIAQHVAEnprseedrnYESTIAQLKDEIQILNKRLEDEA------------LAQQQQKpKDEIV 244
Cdd:pfam01576    8 QAKEEELQKVKERQQKAESELKE---------LEKKHQQLCEEKNALQEQLQAETelcaeaeemrarLAARKQE-LEEIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   245 AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLD------QVL-VEKATV--------------VQQRDDMQAE---- 299
Cdd:pfam01576   78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaarQKLqLEKVTTeakikkleedilllEDQNSKLSKErkll 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   300 ---LADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLK--------------------------------EIETEKIA 344
Cdd:pfam01576  158 eerISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeekgrqelekakrklegestdlqeqiaelqaQIAELRAQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   345 LIKKQEEVTI-------------EARKSV-ETDDH------------------------LSEEVVAAK-------NTIAS 379
Cdd:pfam01576  238 LAKKEEELQAalarleeetaqknNALKKIrELEAQiselqedleseraarnkaekqrrdLGEELEALKteledtlDTTAA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   380 LQATNEERETEIKKLKQRMDEERASHTAQSeQEMKQleaHYERAQKMLQDNVEQ-----MNVEN--RGLRDEIEKLSQQM 452
Cdd:pfam01576  318 QQELRSKREQEVTELKKALEEETRSHEAQL-QEMRQ---KHTQALEELTEQLEQakrnkANLEKakQALESENAELQAEL 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   453 AALPRGGLN--------EQQLHEIFNWVSEEKATREEMENLTRKITGEVESLknnsplttsNYIQNTPSGWGSRRMNNVA 524
Cdd:pfam01576  394 RTLQQAKQDsehkrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESV---------SSLLNEAEGKNIKLSKDVS 464

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   525 RKDG--LDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:pfam01576  465 SLESqlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 676-726 4.45e-14

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 67.85  E-value: 4.45e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 922581144   676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECG 51
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
73-136 1.18e-12

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 63.92  E-value: 1.18e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144     73 GIDWNTI--RDSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAfTGNHLPFVGFSYTH 136
Cdd:smart00133    2 GIDWDKLenKEIEPPFVPKIKSPTDTSNFDPE--FTEETPVLTPVDSPLSG-GIQQEPFRGFSYVF 64
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 676-725 5.30e-12

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 61.71  E-value: 5.30e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 922581144    676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
137-444 8.63e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.07  E-value: 8.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  137 GSLLSDARSLTDEIRA-IAQRCQGD-------AELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHvaenprsEEDRn 208
Cdd:PRK02224  179 ERVLSDQRGSLDQLKAqIEEKEEKDlherlngLESELAELDEEIERYEEQREQARETRDEADEVLEEH-------EERR- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  209 yeSTIAQLKDEIQILNkrledealaqqqqkpkdEIVAESEKKLKELKERnkqlVMEKSEIQREL-DNINDHLDQVLVEKA 287
Cdd:PRK02224  251 --EELETLEAEIEDLR-----------------ETIAETEREREELAEE----VRDLRERLEELeEERDDLLAEAGLDDA 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  288 ---TVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDD 364
Cdd:PRK02224  308 daeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  365 HLSEEvvaakntIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEmKQLEAHYERAqkmlQDNVEqmnvENRGLRDE 444
Cdd:PRK02224  388 ELEEE-------IEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATLRTA----RERVE----EAEALLEA 451
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 1-100 1.85e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 67.15  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidWVvSEEAKDLIRQLICSSDV-RFG--RNGLSDFQLHPFFEGIDWN 77
Cdd:PTZ00263  208 FIAGYPPFFDDTPFRIYEKILAGR--LKFPN----WF-DGRARDLVKGLLQTDHTkRLGtlKGGVADVKNHPYFHGANWD 280

                          90       100
                  ....*....|....*....|....*
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFD 100
Cdd:PTZ00263  281 KLyaRYYPAPIPVRVKSPGDTSNFE 305
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1015-1199 1.40e-07

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 56.44  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144 1015 FKKSVTIFQIdrsekrhkkwKDLAMPGTPQSIAIFNGRLYVGfshSFRSWSLVGVDSspvgsgdasgavLQHISLVNMED 1094
Cdd:COG5422   993 LKKALTIELS----------TELYVPSEPLSVHFLKNKLCIG---CKKGFEIVSLEN------------LRTESLLNPAD 1047

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144 1095 TSLQFLNQQTSYEAKLIVNVPGspdEYLLVFNMIGLYVNEMGRRSRlPEVMF--PTQAKYFAYHEPYLCVFSENEVDIFN 1172
Cdd:COG5422  1048 TSPLFFEKKENTKPIAIFRVSG---EFLLCYSEFAFFVNDQGWRKR-TSWIFhwEGEPQEFALSYPYILAFEPNFIEIRH 1123

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 922581144 1173 VTLAEWVQTI---NLR----SAKPLSGDG-ILSTC 1199
Cdd:COG5422  1124 IETGELIRCIlghNIRlltdGRGPLLHGGeILYKC 1158
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 1262-1300 2.43e-07

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 47.97  E-value: 2.43e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 922581144   1262 ISTPSDFMHIVHMGPAPVMelqQNFIDLQSNHSHTSSDK 1300
Cdd:smart00285    1 ISTPTNFKHIAHVGFDGQT---GGFTGLPTEWKSLLKTS 36
Pkinase_C pfam00433
Protein kinase C terminal domain;
90-134 5.13e-07

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 47.20  E-value: 5.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 922581144    90 VSSPEDTSNFDvdvceDDFT--PCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:pfam00433    1 VKSETDTSNFD-----PEFTeePPVLTPPDSSILSSNDQEEFRGFSY 42
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 1260-1298 6.99e-07

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 47.05  E-value: 6.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 922581144 1260 IQISTPSDFMHIVHMGPAPVMELQQNFI-DLQSNHSHTSS 1298
Cdd:cd00132     1 MEISTPTDFKHISHVGWDGVGFDGANLPpDLQSLFQTAGI 40
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 266-447 9.27e-07

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 52.37  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  266 SEIQRELDNINDHLDQVLVEKAtvvqqRDDMQAELADvgdslltEKDSVKRLQDEAEKAKKQVADFEEKLkeiETEKIAL 345
Cdd:cd22656    94 AEILELIDDLADATDDEELEEA-----KKTIKALLDD-------LLKEAKKYQDKAAKVVDKLTDFENQT---EKDQTAL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  346 IKKQEEVtiearksvetDDHLSEEV-VAAKNTIASLQAT-NEERETEIKKLKQRMDEERAshtaqseqEMKQLEAHYERA 423
Cdd:cd22656   159 ETLEKAL----------KDLLTDEGgAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKA--------LIADDEAKLAAA 220

                         170       180
                  ....*....|....*....|....
gi 922581144  424 QKmLQDNVEQMNVENRGLRDEIEK 447
Cdd:cd22656   221 LR-LIADLTAADTDLDNLLALIGP 243
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 747-870 3.00e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 47.16  E-value: 3.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    747 YEGLVKTpRAGGVRKGWQTAYVVVCDFKLYLYDctvdrqNKMQDVKNEIRLVLDMRDpdftvCGVSEADviHAQKGDIPK 826
Cdd:smart00233    3 KEGWLYK-KSGGGKKSWKKRYFVLFNSTLLYYK------SKKDKKSYKPKGSIDLSG-----CTVREAP--DPDSSKKPH 68

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 922581144    827 IFRVTTTQilnssseyssSSKFYtlFMAETEEEKRKWVVALSEL 870
Cdd:smart00233   69 CFEIKTSD----------RKTLL--LQAESEEEREKWVEALRKA 100
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 374-454 5.38e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 5.38e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    374 KNTIASLQATNEERETEIKKLKQRMDEERASHTAQS----EQEMKQLEAHYERAQKMLQDNVEQM-NVENRGLRDEIEKL 448
Cdd:smart00935   24 EKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAArekkEKELQKKVQEFQRKQQKLQQDLQKRqQEELQKILDKINKA 103


                    ....*.
gi 922581144    449 SQQMAA 454
Cdd:smart00935  104 IKEVAK 109
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 169-409 1.92e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 42.90  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  169 DGFMVELENEKAELVQKLKEAQtiIAQHVAENP----------RSEEDRN-YESTIAQLKDEIQILNKRLED---EALAQ 234
Cdd:NF012221 1525 DGLGYILDNVVATSESSQQADA--VSKHAKQDDaaqnaladkeRAEADRQrLEQEKQQQLAAISGSQSQLEStdqNALET 1602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  235 QQQKPKDEIVAESEKKLKELKERNKQLVM---------EKSEIQRE------LDNINDHLD---QVLVEKATVVQQRddM 296
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTTLAQGLDAldsqatyagESGDQWRNpfagglLDRVQEQLDdakKISGKQLADAKQR--H 1680

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  297 QAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEkiALIKKQEEvtiearKSVETDDHLSEEVVAAKNT 376
Cdd:NF012221 1681 VDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDD--ALAKQNEA------QQAESDANAAANDAQSRGE 1752

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 922581144  377 IASLQATNE--ERETEIKKLKQRMDEERASHTAQS 409
Cdd:NF012221 1753 QDASAAENKanQAQADAKGAKQDESDKPNRQGAAG 1787
growth_prot_Scy NF041483
polarized growth protein Scy;
139-468 2.62e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  139 LLSDARSLTDEIRAIAQrcqGDAElmeksvdgfMVELEN-EKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLK 217
Cdd:NF041483  485 LLTKAKADADELRSTAT---AESE---------RVRTEAiERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAE 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  218 DEIQILNKRLEdEALAQQQQKPKDEIV---AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRD 294
Cdd:NF041483  553 RAARELREETE-RAIAARQAEAAEELTrlhTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQA 631

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  295 DMQAEladvgdslltekdsvkRLQDEA-EKAKKQVADFEEKLKEIETEKIAlikKQEEVTIEARksvETDDHLSEEVVAA 373
Cdd:NF041483  632 EQEAE----------------RLRTEAaADASAARAEGENVAVRLRSEAAA---EAERLKSEAQ---ESADRVRAEAAAA 689

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  374 KNTIAS-----LQATNEE-----RETE--IKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGL 441
Cdd:NF041483  690 AERVGTeaaeaLAAAQEEaarrrREAEetLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATEL 769

                         330       340
                  ....*....|....*....|....*..
gi 922581144  442 RDEIEKLSQQMAAlPRGGLNEQQLHEI 468
Cdd:NF041483  770 VSAAEQTAQQVRD-SVAGLQEQAEEEI 795
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
207-455 5.36e-03

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 39.92  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  207 RNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLvmekseiqreldnindhldQVLVEK 286
Cdd:NF033927   10 RKSAAKIANKLDDLSQINLREATLDLLAQLQEQIAELEAQIAALESKLNELAEDR-------------------KVIIEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  287 ATVVQQRDdmqaeLADVGDSLLTEKDSVKRLQDEaeKAKKQVADFeeklkeieteKIALIKKQEEVTIEARKS---VETD 363
Cdd:NF033927   71 IDLIEKYN-----IADLFKDLLPTAEEIDSLGLP--PPEKDLVKA----------AIERLKKLLGKISEGLTYidlVEAR 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  364 DHLSEEVVAAKNTIASLQatneereTEIKKLKQRMDEERASHTAQSE-----QEMKQLEAHYERaqkmLQDNVEQMNVEN 438
Cdd:NF033927  134 DKLRDRINALLAESRTLD-------KDIKALAGKLEELTAIAAIDEEratwvAEARKVEQAWES----FLDQLTELTSDS 202

                         250
                  ....*....|....*..
gi 922581144  439 RGLRDEIEKLSQQMAAL 455
Cdd:NF033927  203 ANLAQLITQLNGFIKFL 219
 
Name Accession Description Interval E-value
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
900-1212 3.00e-78

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


Pssm-ID: 214481  Cd Length: 302  Bit Score: 260.36  E-value: 3.00e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    900 RVAQCCAIIDRS-KIVIGFSDHGLYCIEISRQlliPVGGEKENKQRCVETVEYDEAEQLLMMIVG----PAKDRHVRIV- 973
Cdd:smart00036    1 NTAKWNHPITCDgKWLLVGTEEGLYVLNISDQ---PGTLEKLIGRRSVTQIWVLEENNVLLMISGkkpqLYSHPLSALVe 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    974 -----PSAALDGRDLKWIKVNDTKGCHLLAVGtNNPggRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLampgtPQSIAI 1048
Cdd:smart00036   78 kkealGSARLVIRKNVLTKIPDVKGCHLCAVV-NGK--RSLFLCVALQSSVVLLQWYNPLKKFKLFKSK-----FLFPLI 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1049 FNGRLYVGFSHSF--RSWSLVGVDSSPvgsgdasGAVLQHIS-LVNMEDTSLQFLNQQTSYEAKLIVNVPGspDEYLLVF 1125
Cdd:smart00036  150 SPVPVFVELVSSSfeRPGICIGSDKGG-------GDVVQFHEsLVSKEDLSLPFLSEETSLKPISVVQVPR--DEVLLCY 220

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   1126 NMIGLYVNEMG-RRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRsakPLSGDGILSTclcNDS 1204
Cdd:smart00036  221 DEFGVFVNLYGkRRSRNPILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADR---ETRKIRLLGS---SDR 294


                    ....*...
gi 922581144   1205 PIFVLLQN 1212
Cdd:smart00036  295 KILLSSSP 302
PH_MRCK cd01243
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ...
 734-877 7.40e-68

MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269949  Cd Length: 135  Bit Score: 224.10  E-value: 7.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  734 PLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDrqnKMQDVKNEIRLVLDMRDPDFTVCGVSE 813
Cdd:cd01243     1 PLGIDPTRGIGTAYEGYVRVPKPGGVKKGWQRQFAVVCDFKLFLFDISED---KASQPSQVASQVLDMRDEEFSVSSVLA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  814 ADVIHAQKGDIPKIFRVTTTQILNssseysSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRS 877
Cdd:cd01243    78 SDVIHANKKDIPCIFRVSASQLAP------PSLKFSLLMLADSENEKQKWVDALNELHKLLKKN 135
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 1-135 1.67e-67

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: 231.08  E-value: 1.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05597   201 MLYGETPFYAESLVETYGKIMNHKEHFSFPDDEDD--VSEEAKDLIRRLICSRERRLGQNGIDDFKKHPFFEGIDWDNIR 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSYT 135
Cdd:cd05597   279 DSTPPYIPEVTSPTDTSNFDVD--DDDLRHTDSLPPPSNAAFSGLHLPFVGFTYT 331
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 1-142 3.59e-54

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: 195.23  E-value: 3.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05623   272 MLYGETPFYAESLVETYGKIMNHKERFQFPTQVTD--VSENAKDLIRRLICSREHRLGQNGIEDFKNHPFFVGIDWDNIR 349

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSYTHGSLLSD 142
Cdd:cd05623   350 NCEAPYIPEVSSPTDTSNFDVD--DDCLKNCETMPPPTHTAFSGHHLPFVGFTYTSSCVLSD 409
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 1-142 2.02e-53

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: 192.92  E-value: 2.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05624   272 MLYGETPFYAESLVETYGKIMNHEERFQFPSHVTD--VSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIR 349

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSYTHGSLLSD 142
Cdd:cd05624   350 NLEAPYIPDVSSPSDTSNFDVD--DDVLRNPEILPPSSHTGFSGLHLPFVGFTYTTESCFSD 409
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 1-135 3.38e-47

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: 173.33  E-value: 3.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWN--T 78
Cdd:cd05596   223 MLVGDTPFYADSLVGTYGKIMNHKNSLQFPDDV---EISKDAKSLICAFLTDREVRLGRNGIEEIKAHPFFKNDQWTwdN 299

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   79 IRDSNPPYVPEVSSPEDTSNFDvDVcEDDFTPCETQPPRvlAAFTGNHLPFVGFSYT 135
Cdd:cd05596   300 IRETVPPVVPELSSDIDTSNFD-DI-EEDETPEETFPVP--KAFVGNHLPFVGFTYS 352
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 1-134 1.73e-45

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: 168.23  E-value: 1.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRngLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05573   223 MLYGFPPFYSDSLVETYSKIMNWKESLVFPDDP---DVSPEAIDLIRRLLCDPEDRLGS--AEEIKAHPFFKGIDWENLR 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:cd05573   298 ESPPPFVPELSSPTDTSNFDDF--EDDLLLSEYLSNGSPLLGKGKQLAFVGFTF 349
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 1-135 1.68e-39

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: 150.15  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDfqlHPFFEGIDWNTIR 80
Cdd:cd05601   202 MLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDP---KVSESAVDLIKGLLTDAKERLGYEGLCC---HPFFSGIDWNNLR 275

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   81 DSNPPYVPEVSSPEDTSNFdvdvceDDFTPCETQPPRVL----AAFTGNHLPFVGFSYT 135
Cdd:cd05601   276 QTVPPFVPTLTSDDDTSNF------DEFEPKKTRPSYENfnksKGFSGKDLPFVGFTFT 328
CNH pfam00780
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ...
 909-1190 5.85e-38

CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.


Pssm-ID: 459938  Cd Length: 261  Bit Score: 143.54  E-value: 5.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   909 DRSKIVIGfSDHGLYCIEISRQL-LIPVGGEKENKQrcvetVEYDEAEQLLMMIVGpaKDRHVRIVPSAALDGRDL---- 983
Cdd:pfam00780    1 GGQNLLLG-TEEGLYVLNRSGPRePVRIIDKKRVTQ-----LAVLEEFNLLLLLSG--KDKRLYVYPLSALDSREEndrk 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   984 --KWIKVNDTKGCHLLAVGTNNpGGRagFFAVAFKKSVTIFQIDRSE-KRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHS 1060
Cdd:pfam00780   73 daAKNKLPETKGCHFFKVGRHS-NGR--FLVVAVKRTIKLLEWYEPLlDKFRKFKEFYLPSPPVSIELLKSKLCVGCAKG 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  1061 FrswSLVGVDSSPVGSGDasgavlqhislvnmedTSLQFLNQQTSYEAKLIVNVpgSPDEYLLVFNMIGLYVNEMGRRSR 1140
Cdd:pfam00780  150 F---EIVSLDSKATESLL----------------TSLLFANRQENLKPLAVVRL--DRSEFLLCYNEFGVYVNLQGRRSR 208

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 922581144  1141 LPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPL 1190
Cdd:pfam00780  209 PWEIEWEGAPEAVAYLYPYLLAFHDNFIEIRDVETGELVQEIAGRKIRFL 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 1-134 1.15e-37

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: 144.68  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIdwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05599   193 MLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVP---ISPEAKDLIERLLCDAEHRLGANGVEEIKSHPFFKGVDWDHIR 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:cd05599   270 ERPAPILPEVKSILDTSNFDEFEEVDLQIPSSPEAGKDSKELKSKDWVFIGYTY 323
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 1-134 1.87e-33

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 133.97  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWN--T 78
Cdd:cd05621   249 MLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDV---EISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFRNDQWNwdN 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   79 IRDSNPPYVPEVSSPEDTSNFDvDVcEDDFTPCETQPprVLAAFTGNHLPFVGFSY 134
Cdd:cd05621   326 IRETAAPVVPELSSDIDTSNFD-DI-EDDKGDVETFP--IPKAFVGNQLPFVGFTY 377
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 1-134 7.04e-31

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: 126.66  E-value: 7.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIdwvVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGID--WNT 78
Cdd:cd05622   270 MLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDND---ISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQwaWET 346

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   79 IRDSNPPYVPEVSSPEDTSNFDvDVcEDDFTPCETQPprVLAAFTGNHLPFVGFSY 134
Cdd:cd05622   347 LRDTVAPVVPDLSSDIDTSNFD-DL-EEDKGEEETFP--IPKAFVGNQLPFVGFTY 398
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
 2-134 6.97e-29

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: 120.34  E-value: 6.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    2 LYGTTPFYSERLVDTYGKIMSHQDMLDFPDDeidWVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIRD 81
Cdd:cd05629   242 LIGWPPFCSENSHETYRKIINWRETLYFPDD---IHLSVEAEDLIRRLITNAENRLGRGGAHEIKSHPFFRGVDWDTIRQ 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144   82 SNPPYVPEVSSPEDTSNFDVDVCED-DFTPCETQPPRV-LAAFTGNHLPFVGFSY 134
Cdd:cd05629   319 IRAPFIPQLKSITDTSYFPTDELEQvPEAPALKQAAPAqQEESVELDLAFIGYTY 373
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 676-728 1.06e-27

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 106.59  E-value: 1.06e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCPVP 53
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 1-136 1.07e-25

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: 109.71  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05598   198 MLVGQPPFLAQTPAETQLKVINWRTTLKIPHEA---NLSPEAKDLILRLCCDAEDRLGRNGADEIKAHPFFAGIDWEKLR 274

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   81 DSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCEtQPPRVLAAFTGNH--LPFVGFSYTH 136
Cdd:cd05598   275 KQKAPYIPTIRHPTDTSNFDPVDPEKLRSSDE-EPTTPNDPDNGKHpeHAFYEFTFRR 331
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 1-95 2.38e-20

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: 93.46  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidWVVSEEAKDLIRQLICS-SDVRFG-RNGLSDFQLHPFFEGIDWNT 78
Cdd:cd05574   225 MLYGTTPFKGSNRDETFSNILKKE--LTFPES---PPVSSEAKDLIRKLLVKdPSKRLGsKRGASEIKRHPFFRGVNWAL 299

                          90
                  ....*....|....*..
gi 922581144   79 IRDSNPPYVPEVSSPED 95
Cdd:cd05574   300 IRNMTPPIIPRPDDPID 316
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 1-136 5.24e-19

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: 90.86  E-value: 5.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFP---DDEIDWVVSEEAKDLIRQLICSSDVRFGRngLSDFQLHPFFEGIDWN 77
Cdd:cd05600   241 CLVGFPPFSGSTPNETWANLYHWKKTLQRPvytDPDLEFNLSDEAWDLITKLITDPQDRLQS--PEQIKNHPFFKNIDWD 318

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   78 TIRD-SNPPYVPEVSSPEDTSNFDVDVCEDDF--------TPCETQPPRVLAAFTGNHLPFVGFSYTH 136
Cdd:cd05600   319 RLREgSKPPFIPELESEIDTSYFDDFNDEADMakykdvheKQKSLEGSGKNGGDNGNRSLFVGFTFRH 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-476 8.74e-19

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 92.81  E-value: 8.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   172 MVELENEKAELVQKLKEAQTIIAQHvaenprSEEDRNYESTIAQLKDEIQILNKRLEDEalaqqqqkpkdeivaesEKKL 251
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEEL------TAELQELEEKLEELRLEVSELEEEIEEL-----------------QKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   252 KELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADF 331
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   332 EEKLKEIETE------KIALIKKQEEVtiearksvetddhLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDE----E 401
Cdd:TIGR02168  371 ESRLEELEEQletlrsKVAQLELQIAS-------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkE 437

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   402 RASHTAQSEQEMKQLEAHYERAQ---KMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEK 476
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
 1-100 4.27e-18

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: 88.14  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNT-I 79
Cdd:cd05626   241 MLVGQPPFLAPTPTETQLKVINWENTLHIPPQV---KLSPEAVDLITKLCCSAEERLGRNGADDIKAHPFFSEVDFSSdI 317

                          90       100
                  ....*....|....*....|.
gi 922581144   80 RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05626   318 RTQPAPYVPKISHPMDTSNFD 338
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 1-100 4.33e-18

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: 86.09  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMShqDMLDFPDDeidwvVSEEAKDLIRQLiCSSDV--RFG--RNGLSDFQLHPFFEGIDW 76
Cdd:cd05580   191 MLAGYPPFFDENPMKIYEKILE--GKIRFPSF-----FDPDAKDLIKRL-LVVDLtkRLGnlKNGVEDIKNHPWFAGIDW 262

                          90       100
                  ....*....|....*....|....*.
gi 922581144   77 NTI--RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05580   263 DALlqRKIPAPYVPKVRGPGDTSNFD 288
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 674-733 1.26e-17

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase 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 alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 78.14  E-value: 1.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEERR 733
Cdd:cd20864     1 KAHQFVVKSFTTPTKCNQCTSLMVGLIRQGCTCEVCGFSCHVTCADKAPSVCPIPPEQTK 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 143-465 1.45e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 88.84  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  143 ARSLTDEIRAIaqrcqgDAELMEKSVDgfmvELENEKAELVQKLKEAQTIIAQHVAENprseedRNYESTIAQLKDEIQI 222
Cdd:COG1196   215 YRELKEELKEL------EAELLLLKLR----ELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  223 LNKRLEDealAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELAD 302
Cdd:COG1196   279 LELELEE---AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  303 VGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVA-AKNTIASLQ 381
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEE 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  382 ATNEERETEIKKLKQRMDEERAShtAQSEQEMKQLEAHYERAQKMLQDNVEQMNvENRGLRDEIEKLSQQMAALPRGGLN 461
Cdd:COG1196   436 EEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYEGFLEGVKA 512


                  ....
gi 922581144  462 EQQL 465
Cdd:COG1196   513 ALLL 516
C1_MRCKgamma cd20866
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 676-728 9.43e-17

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase gamma (MRCK gamma) and similar proteins; MRCK gamma (MRCKG), also called Cdc42-binding protein kinase gamma, DMPK-like gamma, myotonic dystrophy protein kinase-like gamma, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed in heart and skeletal muscles. It may act as a downstream effector of Cdc42 in cytoskeletal reorganization and contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410416  Cd Length: 52  Bit Score: 75.18  E-value: 9.43e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSqSCPVP 728
Cdd:cd20866     1 HTFKPKTFTSPTKCLRCTSLMVGLVRQGLACEACNYVCHVSCAEGAP-ICPTP 52
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 177-583 4.21e-16

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 84.07  E-value: 4.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   177 NEKAELVQKLKEAQTIIAQHVAEnprseedrnYESTIAQLKDEIQILNKRLEDEA------------LAQQQQKpKDEIV 244
Cdd:pfam01576    8 QAKEEELQKVKERQQKAESELKE---------LEKKHQQLCEEKNALQEQLQAETelcaeaeemrarLAARKQE-LEEIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   245 AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLD------QVL-VEKATV--------------VQQRDDMQAE---- 299
Cdd:pfam01576   78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaarQKLqLEKVTTeakikkleedilllEDQNSKLSKErkll 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   300 ---LADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLK--------------------------------EIETEKIA 344
Cdd:pfam01576  158 eerISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeekgrqelekakrklegestdlqeqiaelqaQIAELRAQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   345 LIKKQEEVTI-------------EARKSV-ETDDH------------------------LSEEVVAAK-------NTIAS 379
Cdd:pfam01576  238 LAKKEEELQAalarleeetaqknNALKKIrELEAQiselqedleseraarnkaekqrrdLGEELEALKteledtlDTTAA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   380 LQATNEERETEIKKLKQRMDEERASHTAQSeQEMKQleaHYERAQKMLQDNVEQ-----MNVEN--RGLRDEIEKLSQQM 452
Cdd:pfam01576  318 QQELRSKREQEVTELKKALEEETRSHEAQL-QEMRQ---KHTQALEELTEQLEQakrnkANLEKakQALESENAELQAEL 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   453 AALPRGGLN--------EQQLHEIFNWVSEEKATREEMENLTRKITGEVESLknnsplttsNYIQNTPSGWGSRRMNNVA 524
Cdd:pfam01576  394 RTLQQAKQDsehkrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESV---------SSLLNEAEGKNIKLSKDVS 464

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   525 RKDG--LDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:pfam01576  465 SLESqlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
 1-115 7.10e-16

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: 80.87  E-value: 7.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05627   230 MLIGYPPFCSETPQETYRKVMNWKETLVFPPEV---PISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEHIR 306

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 922581144   81 DsNPPYVP-EVSSPEDTSNFDvDVCEDDF---TPCETQP 115
Cdd:cd05627   307 E-RPAAIPiEIKSIDDTSNFD-DFPESDIlqpAPNTTEP 343
C1_MRCKbeta cd20865
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 676-728 1.53e-15

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase beta (MRCK beta) and similar proteins; MRCK beta, also called Cdc42-binding protein kinase beta (Cdc42BP-beta), DMPK-like beta, or myotonic dystrophy protein kinase-like beta, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. MRCK beta is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410415  Cd Length: 53  Bit Score: 71.94  E-value: 1.53e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20865     1 HQLSIKSFSSPTQCSHCTSLMVGLVRQGYACEVCSFACHVSCKDSAPQVCPIP 53
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
 1-134 4.34e-15

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: 78.54  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIR 80
Cdd:cd05628   229 MLIGYPPFCSETPQETYKKVMNWKETLIFPPEV---PISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEHIR 305

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144   81 DsNPPYVP-EVSSPEDTSNFDVDVCEDDFTPCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:cd05628   306 E-RPAAIPiEIKSIDDTSNFDEFPDSDILKPSVAVSNHPETDYKNKDWVFINYTY 359
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 1-100 9.78e-15

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: 76.84  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMshQDMLDFPDDeidwvVSEEAKDLIRQLICSSDV-RFGRNGLSDFQLHPFFEGIDWNTI 79
Cdd:cd05585   187 MLTGLPPFYDENTNEMYRKIL--QEPLRFPDG-----FDRDAKDLLIGLLNRDPTkRLGYNGAQEIKNHPFFDQIDWKRL 259

                          90       100
                  ....*....|....*....|...
gi 922581144   80 --RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05585   260 lmKKIQPPFKPAVENAIDTSNFD 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 178-564 1.24e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.21  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  178 EKAELvqKLKEAQtiiaqhvaENprseedrnyestIAQLKDEIQILNKRLEdeALAQQQQKpkdeivAESEKKLK-ELKE 256
Cdd:COG1196   175 EEAER--KLEATE--------EN------------LERLEDILGELERQLE--PLERQAEK------AERYRELKeELKE 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  257 RNKQL-VMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKL 335
Cdd:COG1196   225 LEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  336 KEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQ 415
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  416 LEAHYERAQKMLQDNVEQMNVENR--GLRDEIEKLSQQMAALPRGGLNEQQLHEifnwvSEEKATREEMENLTRKITGEV 493
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAeeALLERLERLEEELEELEEALAELEEEEE-----EEEEALEEAAEEEAELEEEEE 459

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144  494 ESLKNNSPLTTSnyiqntpsgwgsrrmnNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLD 564
Cdd:COG1196   460 ALLELLAELLEE----------------AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 676-725 1.39e-14

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 69.08  E-value: 1.39e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 1-135 1.71e-14

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: 76.10  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMsHQDMLdFPDdeidWVvSEEAKDLIRQLICSSDVR---FGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05570   189 MLAGQSPFEGDDEDELFEAIL-NDEVL-YPR----WL-SREAVSILKGLLTKDPARrlgCGPKGEADIKAHPFFRNIDWD 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDvdvceDDFT--PCETQPPRVLAAFTGNHLPFVGFSYT 135
Cdd:cd05570   262 KLekKEVEPPFKPKVKSPRDTSNFD-----PEFTseSPRLTPVDSDLLTNIDQEEFRGFSYI 318
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 676-726 3.29e-14

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 68.11  E-value: 3.29e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIWGLSKKGLSCKDCGFNCHIKCELKVPPECP 52
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 676-726 4.45e-14

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 67.85  E-value: 4.45e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 922581144   676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECG 51
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
 1-100 5.96e-14

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 75.47  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEidwVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNT-I 79
Cdd:cd05625   241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQA---KLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSdL 317

                          90       100
                  ....*....|....*....|.
gi 922581144   80 RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05625   318 RQQSAPYIPKITHPTDTSNFD 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 143-496 6.36e-14

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 77.03  E-value: 6.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   143 ARSLTDEIRAIAQRCQGDAELMEKSVDgfmVELENEKAELVQKLKEAQTIIAQHVA-ENPRSEEdrnyESTIAQLKDEIQ 221
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQA---LLKEKREYEGYELLKEKEALERQKEAiERQLASL----EEELEKLTEEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   222 ILNKRL------------------EDEALAQQ--------QQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNI 275
Cdd:TIGR02169  262 ELEKRLeeieqlleelnkkikdlgEEEQLRVKekigeleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   276 NDHLDQVLVEKATVVQQRDDMQAELAdvgdslltekDSVKRLQDEAEKAKKQVadfeEKLKEIETEKIALIKKQEEVTIE 355
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELE----------DLRAELEEVDKEFAETR----DELKDYREKLEKLKREINELKRE 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   356 ARKSVETDDHLSEEVVAAKNTIASLqatneerETEIKKLKQRMDEERAShTAQSEQEMKQLEAHYERAQKMLQDNVEqmn 435
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAIAGI-------EAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKE--- 476

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   436 vENRGLRDEIEKLSQQMAALprgglnEQQLHEIFNWVSEEKATREEMENLTRKITGEVESL 496
Cdd:TIGR02169  477 -EYDRVEKELSKLQRELAEA------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 1-134 6.56e-14

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: 74.28  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMsHQDmLDFPDDeidwvVSEEAKDLIRQLICSS-DVRFG-RNGLSDFQLHPFFEGIDWNT 78
Cdd:cd05575   189 MLYGLPPFYSRDTAEMYDNIL-HKP-LRLRTN-----VSPSARDLLEGLLQKDrTKRLGsGNDFLEIKNHSFFRPINWDD 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   79 I--RDSNPPYVPEVSSPEDTSNFDvdvceDDFTPcETQPPRVLAAFTGNHL---------PFVGFSY 134
Cdd:cd05575   262 LeaKKIPPPFNPNVSGPLDLRNID-----PEFTR-EPVPASVGKSADSVAVsasvqeadnAFDGFSY 322
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 1-135 8.96e-14

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: 73.96  E-value: 8.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMShqDMLDFPDdeidWVvSEEAKDLIRQLICSS-DVRFGRNGLS--DFQLHPFFEGIDWN 77
Cdd:cd05592   189 MLIGQSPFHGEDEDELFWSICN--DTPHYPR----WL-TKEAASCLSLLLERNpEKRLGVPECPagDIRDHPFFKTIDWD 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDvdvceDDFT--PCETQPP--RVLAafTGNHLPFVGFSYT 135
Cdd:cd05592   262 KLerREIDPPFKPKVKSANDVSNFD-----PDFTmeKPVLTPVdkKLLA--SMDQEQFKGFSFT 318
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-597 1.74e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 75.49  E-value: 1.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   130 VGFSYTHGSLLSDARSLTDEIRAIAQRCQGdaelMEKSVDGFMVEL---ENEKAELVQKLKEAqtiiaqhvaenprSEED 206
Cdd:TIGR02169  656 TGGSRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELrriENRLDELSQELSDA-------------SRKI 718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   207 RNYESTIAQLKDEIQILNKRLEDeaLAQQQQKPKDEIvAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQvlvek 286
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEE--LEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH----- 790

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   287 atvvqqrddmqaeladvgdslltekDSVKRLQDEAEKAKKQVADFEEKLKEIE--TEKIALIKKQEEVTIEarksvetdd 364
Cdd:TIGR02169  791 -------------------------SRIPEIQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLEKEIQ--------- 836

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   365 HLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERAShTAQSEQEMKQLEAHYERAQKML---QDNVEQMNVENRGL 441
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-LRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKK 915

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   442 RDEIEKLSQQMAALprgglnEQQLHEIfnwvseEKATREEMEnltrkITGEVESLKnnsplttsnyiqntpsgwgsrrmn 521
Cdd:TIGR02169  916 RKRLSELKAKLEAL------EEELSEI------EDPKGEDEE-----IPEEELSLE------------------------ 954

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   522 nvarkdglDLQRQLQaEIDAKLKLKAELKN-SQEQYLTSAARLDDTEKRMASLMRE-VAMLKQQKNIENSSDSAFSST 597
Cdd:TIGR02169  955 --------DVQAELQ-RVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEErKAILERIEEYEKKKREVFMEA 1023
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 165-585 2.17e-13

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 75.06  E-value: 2.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   165 EKSVDGFMVELENEKAELVQKLKEAQTIIAQ-HVAENPR---SEEDRNYESTIAQLKDEIQILNKRLEDealaqqqqkpk 240
Cdd:TIGR04523  137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQkEELENELnllEKEKLNIQKNIDKIKNKLLKLELLLSN----------- 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   241 deivaesekkLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDE 320
Cdd:TIGR04523  206 ----------LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   321 AEKAKKQVADFEEKLKEIETEKIAL---------------IKKQEEVTIEAR----KSVETDDHLSEEVVAAKNTIASLQ 381
Cdd:TIGR04523  276 LEQNNKKIKELEKQLNQLKSEISDLnnqkeqdwnkelkseLKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSE 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   382 ATNEERETEIKKlKQRMDEERASHTAQSEQEMKQLEA----------HYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQ 451
Cdd:TIGR04523  356 SENSEKQRELEE-KQNEIEKLKKENQSYKQEIKNLESqindleskiqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   452 maalprgglNEQQLHEIFNWVSEEKATREEMENLTRKItgevESLKNNSPLTTSNYiqntpsgwgsrrmnNVARKDGLDL 531
Cdd:TIGR04523  435 ---------IIKNNSEIKDLTNQDSVKELIIKNLDNTR----ESLETQLKVLSRSI--------------NKIKQNLEQK 487

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 922581144   532 QRQLQAEIDAKLKLKAELKNSQEQyltsaarLDDTEKRMASLMREVAMLKQQKN 585
Cdd:TIGR04523  488 QKELKSKEKELKKLNEEKKELEEK-------VKDLTKKISSLKEKIEKLESEKK 534
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 1-134 3.18e-13

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: 72.30  E-value: 3.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMsHQDMLDFPDDEID-WVVSEEAKDLIRQLicssdvRFG-RNGLSDFQLHPFFEGIDWNT 78
Cdd:cd05604   190 MLYGLPPFYCRDTAEMYENIL-HKPLVLRPGISLTaWSILEELLEKDRQL------RLGaKEDFLEIKNHPFFESINWTD 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   79 IRDSN--PPYVPEVSSPEDTSNFDVDVCED--DFTPCETQPPRVL-AAFTGNHLPFVGFSY 134
Cdd:cd05604   263 LVQKKipPPFNPNVNGPDDISNFDAEFTEEmvPYSVCVSSDYSIVnASVLEADDAFVGFSY 323
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 1-135 3.35e-13

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: 72.44  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidwVVSEEAKDLIRQLIC-SSDVRFGrNGLSD---FQLHPFFEGIDW 76
Cdd:cd05584   193 MLTGAPPFTAENRKKTIDKILKGK--LNLPP-----YLTNEARDLLKKLLKrNVSSRLG-SGPGDaeeIKAHPFFRHINW 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   77 NTI--RDSNPPYVPEVSSPEDTSNFDVDVCEDdfTPCETQPPRVLAAFTGNhlPFVGFSYT 135
Cdd:cd05584   265 DDLlaKKVEPPFKPLLQSEEDVSQFDSKFTKQ--TPVDSPDDSTLSESANQ--VFQGFTYV 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 233-586 3.61e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 74.72  E-value: 3.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   233 AQQQQKPKDEI--VAE----SEKKLKELKERNKQLvmekSEIQRELDNINDHLDQVLVEKATVvQQRDDMQAELADV-GD 305
Cdd:TIGR02169  152 PVERRKIIDEIagVAEfdrkKEKALEELEEVEENI----ERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYeGY 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   306 SLLTEKD----SVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVEtddhlsEEVVAAKNTIASLQ 381
Cdd:TIGR02169  227 ELLKEKEalerQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------EEQLRVKEKIGELE 300

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   382 ATNEERETEIKKLKQRMDeerashtaQSEQEMKQLEAHYERAQKMLQD---NVEQMNVENRGLRDEIEKLSQQMAALprg 458
Cdd:TIGR02169  301 AEIASLERSIAEKERELE--------DAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDL--- 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   459 glnEQQLHEI----FNWVSEEKATREEMENLTRKItgevESLKNNSPLTTSNYIQNTPSGwgsRRMNNvARKDGLDLQRQ 534
Cdd:TIGR02169  370 ---RAELEEVdkefAETRDELKDYREKLEKLKREI----NELKRELDRLQEELQRLSEEL---ADLNA-AIAGIEAKINE 438

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   535 LQAEIDAKLK-----------LKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNI 586
Cdd:TIGR02169  439 LEEEKEDKALeikkqewkleqLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 675-726 5.16e-13

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 64.57  E-value: 5.16e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKCP 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 131-496 8.46e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   131 GFSYTHGSLLSDARSLtDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPR----SEED 206
Cdd:TIGR02168  664 GSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarlEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   207 RNYESTIAQLKDEIQILN-----------------KRLEDEALAQQQQkpkdeivaesekkLKELKERNKQLVMEKSEIQ 269
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEaeieeleerleeaeeelAEAEAEIEELEAQ-------------IEQLKEELKALREALDELR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   270 RELDNINDHLdqvlvekATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtEKIALIKKQ 349
Cdd:TIGR02168  810 AELTLLNEEA-------ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNE 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   350 EEVTIEARKSVETDdhlseevvaakntIASLQATNEERETEIKKLKQRMDEERASHtAQSEQEMKQLE-----------A 418
Cdd:TIGR02168  882 RASLEEALALLRSE-------------LEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEvridnlqerlsE 947

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   419 HYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALprGGLNE------QQLHEIFNWVSEEKA----TREEMENLTRK 488
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL--GPVNLaaieeyEELKERYDFLTAQKEdlteAKETLEEAIEE 1025


                   ....*...
gi 922581144   489 ITGEVESL 496
Cdd:TIGR02168 1026 IDREARER 1033
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 1-134 9.59e-13

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: 70.89  E-value: 9.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidwVVSEEAKDLIRQLI---CSSDVRFGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05582   190 MLTGSLPFQGKDRKETMTMILKAK--LGMPQ-----FLSPEAQSLLRALFkrnPANRLGAGPDGVEEIKRHPFFATIDWN 262

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDVDVCEDdfTPCETqpPRVLAAFTGNHLpFVGFSY 134
Cdd:cd05582   263 KLyrKEIKPPFKPAVSRPDDTFYFDPEFTSR--TPKDS--PGVPPSANAHQL-FRGFSF 316
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 158-593 1.18e-12

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 72.84  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   158 QGDAELMEKsVDGFMVELENEKaELVQKLKEAQTIIAQHVAENPRSEED-----RNYESTIAQLKDEIQILNKRLEDEAL 232
Cdd:pfam15921  454 QGKNESLEK-VSSLTAQLESTK-EMLRKVVEELTAKKMTLESSERTVSDltaslQEKERAIEATNAEITKLRSRVDLKLQ 531

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   233 AQQQQKPKDE----IVAESEKKLKELKERNKQLVMEKSEIQRELDNINDH---LDQVLVEKATVVQQRDDMQAELADVgd 305
Cdd:pfam15921  532 ELQHLKNEGDhlrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtAGAMQVEKAQLEKEINDRRLELQEF-- 609

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   306 slltekdsvKRLQDeaeKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASL----- 380
Cdd:pfam15921  610 ---------KILKD---KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLsedye 677

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   381 ------QATNEERETEIKKLKQRMDEERaSHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVEnrglRDEIEKLSQQMAA 454
Cdd:pfam15921  678 vlkrnfRNKSEEMETTTNKLKMQLKSAQ-SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK----RGQIDALQSKIQF 752

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   455 LPRGGLNEQQ----LHEIFNWVSEEKATREEMENltrKITGEVESLKNNSPLTTSNyIQNTPSGWGSRRMNNVARKDglD 530
Cdd:pfam15921  753 LEEAMTNANKekhfLKEEKNKLSQELSTVATEKN---KMAGELEVLRSQERRLKEK-VANMEVALDKASLQFAECQD--I 826

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   531 LQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDdtekrmASLMREVAMLKQQKNIENSSDSA 593
Cdd:pfam15921  827 IQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMK------PRLLQPASFTRTHSNVPSSQSTA 883
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
73-136 1.18e-12

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 63.92  E-value: 1.18e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144     73 GIDWNTI--RDSNPPYVPEVSSPEDTSNFDVDvcEDDFTPCETQPPRVLAAfTGNHLPFVGFSYTH 136
Cdd:smart00133    2 GIDWDKLenKEIEPPFVPKIKSPTDTSNFDPE--FTEETPVLTPVDSPLSG-GIQQEPFRGFSYVF 64
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 1-101 2.66e-12

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: 69.00  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdEIDWVvseeAKDLIRQLICSSDV-RFG--RNGLSDFQLHPFFEGIDWN 77
Cdd:cd05612   191 MLVGYPPFFDDNPFGIYEKILAGK--LEFPR-HLDLY----AKDLIKKLLVVDRTrRLGnmKNGADDVKNHRWFKSVDWD 263

                          90       100
                  ....*....|....*....|....*.
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDV 101
Cdd:cd05612   264 DVpqRKLKPPIVPKVSHDGDTSNFDD 289
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
 676-726 2.98e-12

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 62.69  E-value: 2.98e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20796     2 HTFVVHTYTKPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKKCAEKVPKDCT 52
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 676-725 5.30e-12

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 61.71  E-value: 5.30e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 922581144    676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 1-71 5.33e-12

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: 67.54  E-value: 5.33e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLICSS-DVRFGRNGLSDFQLHPFF 71
Cdd:cd05123   186 MLTGKPPFYAENRKEIYEKILKSP--LKFPEY-----VSPEAKSLISGLLQKDpTKRLGSGGAEEIKAHPFF 250
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
 676-725 6.10e-12

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 61.66  E-value: 6.10e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20827     2 HRFEKHNFTTPTYCDYCSSLLWGLVKTGMRCADCGYSCHEKCLEHVPKNC 51
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
137-444 8.63e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 70.07  E-value: 8.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  137 GSLLSDARSLTDEIRA-IAQRCQGD-------AELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHvaenprsEEDRn 208
Cdd:PRK02224  179 ERVLSDQRGSLDQLKAqIEEKEEKDlherlngLESELAELDEEIERYEEQREQARETRDEADEVLEEH-------EERR- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  209 yeSTIAQLKDEIQILNkrledealaqqqqkpkdEIVAESEKKLKELKERnkqlVMEKSEIQREL-DNINDHLDQVLVEKA 287
Cdd:PRK02224  251 --EELETLEAEIEDLR-----------------ETIAETEREREELAEE----VRDLRERLEELeEERDDLLAEAGLDDA 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  288 ---TVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDD 364
Cdd:PRK02224  308 daeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  365 HLSEEvvaakntIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEmKQLEAHYERAqkmlQDNVEqmnvENRGLRDE 444
Cdd:PRK02224  388 ELEEE-------IEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATLRTA----RERVE----EAEALLEA 451
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 1-100 1.09e-11

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: 67.04  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLIcSSDV--RFG--RNGLSDFQLHPFFEGIDW 76
Cdd:cd14209   191 MAAGYPPFFADQPIQIYEKIVSGK--VRFPSH-----FSSDLKDLLRNLL-QVDLtkRFGnlKNGVNDIKNHKWFATTDW 262

                          90       100
                  ....*....|....*....|....*.
gi 922581144   77 NTI--RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd14209   263 IAIyqRKVEAPFIPKLKGPGDTSNFD 288
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 1-135 1.39e-11

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: 67.42  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLICSSDVR---FGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05587   190 MLAGQPPFDGEDEDELFQSIMEHN--VSYPKS-----LSKEAVSICKGLLTKHPAKrlgCGPTGERDIKEHPFFRRIDWE 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDVDVCED--DFTPCEtqpPRVLAAFTGNHlpFVGFSYT 135
Cdd:cd05587   263 KLerREIQPPFKPKIKSPRDAENFDKEFTKEppVLTPTD---KLVIMNIDQSE--FEGFSFV 319
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
171-429 1.42e-11

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 68.89  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  171 FMVELENEKAELVQKLkeAQTIIAQHVAENPRSEEDRNyESTIAQLKDEIQILNKRLEdealaqqqqkpkdeivaESEKK 250
Cdd:COG3206   138 IEISYTSPDPELAAAV--ANALAEAYLEQNLELRREEA-RKALEFLEEQLPELRKELE-----------------EAEAA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  251 LKELKERNK--QLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSL--LTEKDSVKRLQDEAEKAKK 326
Cdd:COG3206   198 LEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  327 QVADFEEKLKEiETEKIALIKKQEEvTIEARKSVETDDHLSEevvaAKNTIASLQATNEERETEIKKLKQRMDEerashT 406
Cdd:COG3206   278 ELAELSARYTP-NHPDVIALRAQIA-ALRAQLQQEAQRILAS----LEAELEALQAREASLQAQLAQLEARLAE-----L 346

                         250       260
                  ....*....|....*....|...
gi 922581144  407 AQSEQEMKQLEAHYERAQKMLQD 429
Cdd:COG3206   347 PELEAELRRLEREVEVARELYES 369
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 1-100 1.85e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 67.15  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidWVvSEEAKDLIRQLICSSDV-RFG--RNGLSDFQLHPFFEGIDWN 77
Cdd:PTZ00263  208 FIAGYPPFFDDTPFRIYEKILAGR--LKFPN----WF-DGRARDLVKGLLQTDHTkRLGtlKGGVADVKNHPYFHGANWD 280

                          90       100
                  ....*....|....*....|....*
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFD 100
Cdd:PTZ00263  281 KLyaRYYPAPIPVRVKSPGDTSNFE 305
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 1-116 2.15e-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: 66.61  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYS---ERLvdtYGKIMshQDMLDFPDDeidwvVSEEAKDLIRQLICSS-DVRFG--RNGLSDFQLHPFFEGI 74
Cdd:cd05571   188 MMCGRLPFYNrdhEVL---FELIL--MEEVRFPST-----LSPEAKSLLAGLLKKDpKKRLGggPRDAKEIMEHPFFASI 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 922581144   75 DWNTI--RDSNPPYVPEVSSPEDTSNFDvdvceDDFT--PCETQPP 116
Cdd:cd05571   258 NWDDLyqKKIPPPFKPQVTSETDTRYFD-----EEFTaeSVELTPP 298
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 207-588 2.22e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.61  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   207 RNYESTIAQLKDEIQILNKRLED---------EALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINd 277
Cdd:pfam15921  227 RELDTEISYLKGRIFPVEDQLEAlksesqnkiELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ- 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   278 hlDQVLVEKATVVQQRDDMQAeladvgdslltekdSVKRLQDEAEKAKKQvadFEEKLKEIETEkiaLIKKQEEVTiEAR 357
Cdd:pfam15921  306 --EQARNQNSMYMRQLSDLES--------------TVSQLRSELREAKRM---YEDKIEELEKQ---LVLANSELT-EAR 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   358 KSvetDDHLSEEVVAAKNTIASLQATNEERETEI---KKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKmLQDNVEQM 434
Cdd:pfam15921  363 TE---RDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR-LEALLKAM 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   435 NVENRGlrdeieKLSQQMAALPrgGLNEqQLHEIFNWVSEEKATREEMENLTRKITGEVESLKnNSPLTTSNYiqnTPSG 514
Cdd:pfam15921  439 KSECQG------QMERQMAAIQ--GKNE-SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE-SSERTVSDL---TASL 505

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144   515 WGSRRMNNVARKDgldlQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQknIEN 588
Cdd:pfam15921  506 QEKERAIEATNAE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ--IEN 573
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-612 3.99e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   265 KSEIQRELDNINDHLDQVlvekatvvqqrDDMQAELadvgdsllteKDSVKRLQDEAEKAKK---------------QVA 329
Cdd:TIGR02168  174 RKETERKLERTRENLDRL-----------EDILNEL----------ERQLKSLERQAEKAERykelkaelrelelalLVL 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   330 DFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSE---EVVAAKNTIASLQATNEERETEIKKLKQRMDEERAShT 406
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISRLEQQKQILRER-L 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   407 AQSEQEMKQLEAHYERAQKMLQDNVEQMNVenrgLRDEIEKLSQQMAALprgglnEQQLheifnwvSEEKATREEMENLT 486
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAE----LEEKLEELKEELESL------EAEL-------EELEAELEELESRL 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   487 RKITGEVESLKNNSPLTTSNYIQNTpsgwgSRRMNNVARKDGLDLQRQ-LQAEIDAKLK--LKAELKNSQEQYLTSAARL 563
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLN-----NEIERLEARLERLEDRRErLQQEIEELLKklEEAELKELQAELEELEEEL 449

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 922581144   564 DDTEKRMASLMREVAMLKQQ----KNIENSSDSAFSSTMGRGDLMISMNNDYE 612
Cdd:TIGR02168  450 EELQEELERLEEALEELREEleeaEQALDAAERELAQLQARLDSLERLQENLE 502
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 145-661 4.03e-11

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 67.82  E-value: 4.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   145 SLTDEIRAIAQRCQGDAELMEKSVDGFM-VELENEKA--ELVQKLKEAQTIIAQHVAEN----------PRS-EEDRNYE 210
Cdd:pfam05483   96 SIEAELKQKENKLQENRKIIEAQRKAIQeLQFENEKVslKLEEEIQENKDLIKENNATRhlcnllketcARSaEKTKKYE 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   211 STIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVA-ESEKKLKELKERNKQLvmeKSEIQRELDNINDHLDQVLVekatv 289
Cdd:pfam05483  176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHL---EEEYKKEINDKEKQVSLLLI----- 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   290 vqQRDDMQAELADVGDSLLTEKDSVKRLQdeaEKAKKQvadfEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEE 369
Cdd:pfam05483  248 --QITEKENKMKDLTFLLEESRDKANQLE---EKTKLQ----DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   370 VVAAKNTIASLqatNEERETEIKKLkqrmDEERASHT---AQSEQEMKQLEAHYERAQKMLQDNVEQMNVenrgLRDEIE 446
Cdd:pfam05483  319 LQIATKTICQL---TEEKEAQMEEL----NKAKAAHSfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKI----ITMELQ 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   447 KLSQQMAALPRGGLN-EQQLHEI----------------FNWVSEE-KATREEMENLTRKITGEVESLKNNSPLTT---- 504
Cdd:pfam05483  388 KKSSELEEMTKFKNNkEVELEELkkilaedeklldekkqFEKIAEElKGKEQELIFLLQAREKEIHDLEIQLTAIKtsee 467

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   505 --SNYIQNTPSGWGSRRMNNV---ARKDGLDLQRQLQAEIDAKLKLkaELKNSQEQyltsaarLDDTEKRMASLMREVAM 579
Cdd:pfam05483  468 hyLKEVEDLKTELEKEKLKNIeltAHCDKLLLENKELTQEASDMTL--ELKKHQED-------IINCKKQEERMLKQIEN 538

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   580 LKQQK-NIENSSDSAFSSTMGRGDLMISMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVP---KRVDDLRYKQK 655
Cdd:pfam05483  539 LEEKEmNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEnknKNIEELHQENK 618


                   ....*.
gi 922581144   656 PMKTAS 661
Cdd:pfam05483  619 ALKKKG 624
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
 676-725 9.95e-11

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 58.22  E-value: 9.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20828     6 HNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQC 55
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 676-725 1.19e-10

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 57.67  E-value: 1.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 225-496 1.64e-10

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 65.76  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   225 KRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLvMEKSEIQRELDNINdhLDQVLVEKATVVQQR-DDMQAELADV 303
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA-LEYYQLKEKLELEE--EYLLYLDYLKLNEERiDLLQELLRDE 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   304 GDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQAT 383
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   384 NEERETEIKKLKQRMDEERAShTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQ 463
Cdd:pfam02463  330 LKKEKEEIEELEKELKELEIK-REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408

                          250       260       270
                   ....*....|....*....|....*....|...
gi 922581144   464 QLHEIFNwvSEEKATREEMENLTRKITGEVESL 496
Cdd:pfam02463  409 LLLELAR--QLEDLLKEEKKEELEILEEEEESI 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 174-497 1.91e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 65.43  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   174 ELENEK-AELVQKLKEAQTIIAQHVaENPRSEEDRNyESTIAQLKDEIQIL-----NKRLEDEALAQQQQKPKDEIvaES 247
Cdd:TIGR04523  299 DLNNQKeQDWNKELKSELKNQEKKL-EEIQNQISQN-NKIISQLNEQISQLkkeltNSESENSEKQRELEEKQNEI--EK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   248 EKKLKE-LKERNKQLVMEKSEIQRELDNI---NDHLDQVL----VEKATVVQQRDDMQAELADVGDSL--LTEKDSVKRL 317
Cdd:TIGR04523  375 LKKENQsYKQEIKNLESQINDLESKIQNQeklNQQKDEQIkklqQEKELLEKEIERLKETIIKNNSEIkdLTNQDSVKEL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   318 QDEAEKAKKQvaDFEEKLK----EIETEKIALIKKQEEV----------TIEARKSVETDDHLSEEVVAAKNTIASLQAT 383
Cdd:TIGR04523  455 IIKNLDNTRE--SLETQLKvlsrSINKIKQNLEQKQKELkskekelkklNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   384 NEERETEIKKLKQRMD-----------EERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQM 452
Cdd:TIGR04523  533 KKEKESKISDLEDELNkddfelkkenlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 922581144   453 AALprgglnEQQLHEIfnwvseeKATREEMENLTRKITGEVESLK 497
Cdd:TIGR04523  613 SSL------EKELEKA-------KKENEKLSSIIKNIKSKKNKLK 644
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 262-454 2.59e-10

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 62.25  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  262 VMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtE 341
Cdd:COG1579     2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  342 KIALIKKQEEVtiearksvetdDHLSEEvvaakntIASLQATNEERETEIKKLKQRMDEERASHtAQSEQEMKQLEAHYE 421
Cdd:COG1579    81 QLGNVRNNKEY-----------EALQKE-------IESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELE 141

                         170       180       190
                  ....*....|....*....|....*....|...
gi 922581144  422 RAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAA 454
Cdd:COG1579   142 EKKAELDEELAELEAELEELEAEREELAAKIPP 174
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 1-134 2.62e-10

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: 63.45  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMsHQDmLDFPDDEidwvvSEEAKDLIRQLIcSSDVRFGRNGLSDFQL---HPFFEGIDWN 77
Cdd:cd05603   189 MLYGLPPFYSRDVSQMYDNIL-HKP-LHLPGGK-----TVAACDLLQGLL-HKDQRRRLGAKADFLEiknHVFFSPINWD 260

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:cd05603   261 DLyhKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGRTPDLTASSSSSSSAFLGFSY 319
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 231-457 2.74e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.01  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  231 ALAQQQQKpkdeivAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTE 310
Cdd:COG4942    15 AAAQADAA------AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  311 KDSVKRLQDEAEKAKKQVADFEEKL-KEIETEKIALIKKQEEVTIEARKS------VETDDHLSEEVVAAKNTIASLQAT 383
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAE 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  384 NEERETEIKKLKQRMDEERAShTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPR 457
Cdd:COG4942   169 LEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PTZ00121 PTZ00121
MAEBL; Provisional
 148-638 2.93e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  148 DEIRAIAQRCQGDAELMEKSvdgfmvELENEKAELVQKLKEAQTII--AQHVAENPRSEEDRNYEStiAQLKDEIqilnK 225
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKA------EEAKKKADEAKKAAEAKKKAdeAKKAEEAKKADEAKKAEE--AKKADEA----K 1540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  226 RLEDEALAQQQQKPKDEIVAESEKKLKELK--ERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADV 303
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  304 GDSLLTEKDSVKRL------QDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKnti 377
Cdd:PTZ00121 1621 KAEELKKAEEEKKKveqlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--- 1697

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  378 aslqatnEERETEIKKLKQRMDEERashtAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPR 457
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEAEEK----KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  458 GGLNEQQLHEIFNWVSEEkaTREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQA 537
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE 1844

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  538 EIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSS-DSAFSSTMGRGdlmismnNDYEMSNS 616
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDiEREIPNNNMAG-------KNNDIIDD 1917

                         490       500
                  ....*....|....*....|..
gi 922581144  617 SLMRQEMISRQSTPSYENAILL 638
Cdd:PTZ00121 1918 KLDKDEYIKRDAEETREEIIKI 1939
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 264-532 3.03e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 63.63  E-value: 3.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  264 EKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKI 343
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  344 ALIKKQEEVTIEARKSVETDDHL----SEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQ--EMKQLE 417
Cdd:COG4942   101 AQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraELEALL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  418 AHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRgglNEQQLHEIFnwvseEKATREEMENLTRKITGEVESLK 497
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ---EAEELEALI-----ARLEAEAAAAAERTPAAGFAALK 252

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 922581144  498 NNSPLTTSNYIQntpSGWGSRRMNNVARKdGLDLQ 532
Cdd:COG4942   253 GKLPWPVSGRVV---RRFGERDGGGGRNK-GIDIA 283
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 645-725 3.33e-10

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 58.10  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  645 KRVDDLRYKQKPMKTASGIFSPVSISAMERGHNFERmkiktPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQS 724
Cdd:cd20842     9 KRSNSQSYIGRPIQLDKILLSKVKVPHTFVIHSYTR-----PTVCQYCKKLLKGLFRQGLQCKDCKFNCHKRCAPKVPNN 83


                  .
gi 922581144  725 C 725
Cdd:cd20842    84 C 84
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 166-498 3.92e-10

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 64.43  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   166 KSVDGFMVELENE----------KAELVQKLKEAQTIIaqHVAENPRSEEDRNYESTIAQLKDeiqiLNKRLEDEALAQq 235
Cdd:pfam01576  749 KQVRELEAELEDErkqraqavaaKKKLELDLKELEAQI--DAANKGREEAVKQLKKLQAQMKD----LQRELEEARASR- 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   236 qqkpkDEIVA---ESEKKLKELKERNKQLVMEKSEIQREldnindhldqvlveKATVVQQRDDMQAELAdvgdSLLTEKD 312
Cdd:pfam01576  822 -----DEILAqskESEKKLKNLEAELLQLQEDLAASERA--------------RRQAQQERDELADEIA----SGASGKS 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   313 SvkrLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQeevtieaRKSVETDDHLSEEVVAAKNTIASLQATNEERETEIK 392
Cdd:pfam01576  879 A---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-------RKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   393 KLKQRMDEERA-------SHTAQSEQEMKQLEAHYE--------------RAQKMLQDNVEQMNVENRG---LRDEIEKL 448
Cdd:pfam01576  949 ELKAKLQEMEGtvkskfkSSIAALEAKIAQLEEQLEqesrerqaanklvrRTEKKLKEVLLQVEDERRHadqYKDQAEKG 1028

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   449 SQQMAALPRgglneqQLHEifnwvSEEKATR----------------EEMENLTRkitgEVESLKN 498
Cdd:pfam01576 1029 NSRMKQLKR------QLEE-----AEEEASRanaarrklqrelddatESNESMNR----EVSTLKS 1079
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 674-726 4.25e-10

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410435  Cd Length: 54  Bit Score: 56.51  E-value: 4.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20885     2 EGHDFQPCSLTNPTWCDLCGDFIWGLYKQCLRCTHCKYTCHLRCRDLVTLDCS 54
C1_Munc13 cd20807
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ...
 676-725 5.04e-10

protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene family encodes a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-1 is a component of presynaptic active zones in which it acts as an essential synaptic vesicle priming protein. Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410357  Cd Length: 53  Bit Score: 56.33  E-value: 5.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20807     1 HNFEVWTATTPTYCYECEGLLWGIARQGVRCTECGVKCHEKCKDLLNADC 50
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 155-552 5.28e-10

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 63.97  E-value: 5.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   155 QRCQGDAELMEKSVDGFMVELEnekaELVQKLKEAQTIIaqhvaenprsEEDRNYESTIAQLKDEIQILNKRLEDEALAQ 234
Cdd:pfam05483  387 QKKSSELEEMTKFKNNKEVELE----ELKKILAEDEKLL----------DEKKQFEKIAEELKGKEQELIFLLQAREKEI 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   235 QQQKPKDEIVAESEKK-LKELKERNKQLVMEKseiqreLDNI--NDHLDQVLVEKATVVQQRDDMQAELADvgdslltEK 311
Cdd:pfam05483  453 HDLEIQLTAIKTSEEHyLKEVEDLKTELEKEK------LKNIelTAHCDKLLLENKELTQEASDMTLELKK-------HQ 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   312 DSVKRLQDEAEKAKKQVADFEEK----LKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAK-------NTIASL 380
Cdd:pfam05483  520 EDIINCKKQEERMLKQIENLEEKemnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEkqmkileNKCNNL 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   381 QATNEERETEIKKLKQRMDEERASHTAQSEQ----EMK------QLEAHYERAQKML---QDNVEQMNVENRGLRDEIEK 447
Cdd:pfam05483  600 KKQIENKNKNIEELHQENKALKKKGSAENKQlnayEIKvnklelELASAKQKFEEIIdnyQKEIEDKKISEEKLLEEVEK 679

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   448 --LSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNtpsgwgSRRMNNVaR 525
Cdd:pfam05483  680 akAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL------EIELSNI-K 752

                          410       420
                   ....*....|....*....|....*..
gi 922581144   526 KDGLDLQRQLQAEIDAKLKLKAELKNS 552
Cdd:pfam05483  753 AELLSLKKQLEIEKEEKEKLKMEAKEN 779
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 676-725 5.52e-10

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 55.91  E-value: 5.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 674-726 6.34e-10

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 56.18  E-value: 6.34e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20834     6 KGHEFIAKFFRQPTFCSVCKEFLWGFNKQGYQCRQCNAAVHKKCHDKILGKCP 58
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
223-567 6.64e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 62.61  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  223 LNKRLEDEALAQQQQKPKDEI-VAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELA 301
Cdd:COG4372     4 LGEKVGKARLSLFGLRPKTGIlIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  302 DVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQ 381
Cdd:COG4372    84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  382 atneERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLN 461
Cdd:COG4372   164 ----EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  462 EQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQL-QAEID 540
Cdd:COG4372   240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALeDALLA 319

                         330       340
                  ....*....|....*....|....*..
gi 922581144  541 AKLKLKAELKNSQEQYLTSAARLDDTE 567
Cdd:COG4372   320 ALLELAKKLELALAILLAELADLLQLL 346
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
 675-726 6.70e-10

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410370  Cd Length: 52  Bit Score: 55.91  E-value: 6.70e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20820     1 GHRFVPLELEQPTWCDLCGSVILGLFRKCLRCANCKMTCHPRCRSLVCLTCR 52
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
172-434 8.93e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.52  E-value: 8.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  172 MVELENEKAELVQKLKEAQTIIAQHvaenprseedrnyESTIAQLKDEIQILNKRLED-EALAQQQQKPKDEIVAESEKK 250
Cdd:PRK02224  504 LVEAEDRIERLEERREDLEELIAER-------------RETIEEKRERAEELRERAAElEAEAEEKREAAAEAEEEAEEA 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  251 LKELKERNKQLVMEKSEIQReLDNINDHLDQvLVEKATVVQQRDDMQAELADVGDslltekDSVKRLQDEAEKAKKQVAD 330
Cdd:PRK02224  571 REEVAELNSKLAELKERIES-LERIRTLLAA-IADAEDEIERLREKREALAELND------ERRERLAEKRERKRELEAE 642

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  331 F-EEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETeikkLKQRMDEERASHtaqs 409
Cdd:PRK02224  643 FdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA----LENRVEALEALY---- 714

                         250       260
                  ....*....|....*....|....*.
gi 922581144  410 eQEMKQLEAHYERAQ-KMLQDNVEQM 434
Cdd:PRK02224  715 -DEAEELESMYGDLRaELRQRNVETL 739
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
174-489 9.81e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 9.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQH-VAENPRS-----------------EEDRNYESTIAQLKDEIQILNKRLEDEAlaqq 235
Cdd:PRK03918  477 KLRKELRELEKVLKKESELIKLKeLAEQLKEleeklkkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLE---- 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  236 qqkpkdeivaESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVK 315
Cdd:PRK03918  553 ----------ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  316 RLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEaRKSVETDDhLSEEVVAAKNTIASLQATNEERETEIKKLK 395
Cdd:PRK03918  623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLK 700

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  396 QRMDEERashtaQSEQEMKQLEahyeraqKMLQDnveqmnvenrgLRDEIEKLSQQMAALPRGGLNEQQ--LHEIFNWVS 473
Cdd:PRK03918  701 EELEERE-----KAKKELEKLE-------KALER-----------VEELREKVKKYKALLKERALSKVGeiASEIFEELT 757

                         330       340
                  ....*....|....*....|
gi 922581144  474 EEK----ATREEMENLTRKI 489
Cdd:PRK03918  758 EGKysgvRVKAEENKVKLFV 777
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 669-725 1.20e-09

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 56.14  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  669 ISAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20843     5 LSKVKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
 676-725 1.46e-09

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410358  Cd Length: 52  Bit Score: 54.65  E-value: 1.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20808     2 HNFQETTYFKPTFCDHCTGLLWGLIKQGYKCKDCGINCHKHCKDLVVVEC 51
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 5-135 1.60e-09

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: 61.16  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    5 TTPFYSeRLVDTYGKIMSHQDML----DFP-DDE---IDWVVSEE----------AKDLIRQLIC-SSDVRFG--RNGLS 63
Cdd:cd05589   174 TDTSYT-RAVDWWGLGVLIYEMLvgesPFPgDDEeevFDSIVNDEvryprflsteAISIMRRLLRkNPERRLGasERDAE 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   64 DFQLHPFFEGIDWNTI--RDSNPPYVPEVSSPEDTSNFDvdvceDDFT---PCETQP--PRVLAAftGNHLPFVGFSYT 135
Cdd:cd05589   253 DVKKQPFFRNIDWEALlaRKIKPPFVPTIKSPEDVSNFD-----EEFTsekPVLTPPkePRPLTE--EEQALFKDFDYV 324
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
249-589 1.69e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  249 KKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLT---EKDSVKRLQDEAEKAK 325
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  326 KQVADFEEKLKEIET------EKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMD 399
Cdd:PRK03918  252 GSKRKLEEKIRELEErieelkKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  400 --EERASHTAQSEQEMKQLEAHYERaqkmLQDNVEQMNvENRGLRDEIEKLSQQMAALPRGGLnEQQLHEIfnwvseEKA 477
Cdd:PRK03918  332 elEEKEERLEELKKKLKELEKRLEE----LEERHELYE-EAKAKKEELERLKKRLTGLTPEKL-EKELEEL------EKA 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  478 tREEMENLTRKITGEVESLKNNsplttsnyiqntpsgwGSRRMNNVAR-----------------KDGLDLQRQLQAEID 540
Cdd:PRK03918  400 -KEEIEEEISKITARIGELKKE----------------IKELKKAIEElkkakgkcpvcgrelteEHRKELLEEYTAELK 462

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 922581144  541 AKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENS 589
Cdd:PRK03918  463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 177-507 1.77e-09

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 62.76  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   177 NEKAELVQKLKEAQTIIAQHvAENPRSEEDrNYESTIAQLKDEIQI------LNKRLEDEAL---AQQQQKPKDEIVAES 247
Cdd:TIGR01612 1358 NKIKKIIDEVKEYTKEIEEN-NKNIKDELD-KSEKLIKKIKDDINLeeckskIESTLDDKDIdecIKKIKELKNHILSEE 1435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   248 ---EKKLKELKERNKQLVMEKSEIQRElDNINDHLDQVLVEKATvvqqrDDMQAELadvgDSLLTEKDSVKRLQDEAEKA 324
Cdd:TIGR01612 1436 sniDTYFKNADENNENVLLLFKNIEMA-DNKSQHILKIKKDNAT-----NDHDFNI----NELKEHIDKSKGCKDEADKN 1505

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   325 KKQVADFEEKLKEIETEKIALIKKQEEVTIEAR--KSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEER 402
Cdd:TIGR01612 1506 AKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDA 1585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   403 ASHTaQSEQEMKQLEAHYERAQ-KMLQ--DNVEQMN---VENRGLRDEIEKLS--QQMAALPRGGLNEQQLHEIFNWVSE 474
Cdd:TIGR01612 1586 AKND-KSNKAAIDIQLSLENFEnKFLKisDIKKKINdclKETESIEKKISSFSidSQDTELKENGDNLNSLQEFLESLKD 1664

                          330       340       350
                   ....*....|....*....|....*....|...
gi 922581144   475 EKATREEMENLTRKITGEVESLKNNSPLTTSNY 507
Cdd:TIGR01612 1665 QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNY 1697
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 680-725 2.55e-09

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 54.30  E-value: 2.55e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 922581144  680 RMK-IKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20799     9 RLKhFNKPAYCNVCENMLVGLRKQGLCCTFCKYTVHERCVSRAPASC 55
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 1-135 2.66e-09

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: 60.31  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMshQDMLDFPDdeidWVvSEEAKDLIRQLICSS-DVRFG---RNGLSDFQLHPFFEGIDW 76
Cdd:cd05590   189 MLCGHAPFEAENEDDLFEAIL--NDEVVYPT----WL-SQDAVDILKAFMTKNpTMRLGsltLGGEEAILRHPFFKELDW 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   77 NTI--RDSNPPYVPEVSSPEDTSNFDVDVCEDDftPCETQPPRVLAAFTgNHLPFVGFSYT 135
Cdd:cd05590   262 EKLnrRQIEPPFRPRIKSREDVSNFDPDFIKED--PVLTPIEESLLPMI-NQDEFRNFSYT 319
C1_RASGRP4 cd20863
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ...
 676-725 2.77e-09

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410413  Cd Length: 57  Bit Score: 54.40  E-value: 2.77e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20863     4 HNFHETTFKKPTFCDSCSGFLWGVTKQGYRCQDCGINCHKHCKDQVDVEC 53
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
 676-725 2.88e-09

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 54.04  E-value: 2.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20798     2 HTLAEHNYKKPTVCKVCDKLLVGLVRQGLKCRDCGVNVHKKCASLLPSNC 51
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 674-726 3.12e-09

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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. 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. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 53.95  E-value: 3.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20833     1 KDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSCP 53
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
 675-726 3.56e-09

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 53.91  E-value: 3.56e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20832     1 GHQFVLQHYYQVTFCNHCSGLLWGIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 1-76 3.80e-09

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: 59.15  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLY----GTTPFYSERLVDTYGKIMSHQdmLDFPDDEidwVVSEEAKDLIRQLICS-SDVRFGRNGLSDFQLHPFFEGID 75
Cdd:cd05579   197 ILYeflvGIPPFHAETPEEIFQNILNGK--IEWPEDP---EVSDEAKDLISKLLTPdPEKRLGAKGIEEIKNHPFFKGID 271


                  .
gi 922581144   76 W 76
Cdd:cd05579   272 W 272
PTZ00121 PTZ00121
MAEBL; Provisional
 142-451 4.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  142 DARSLTDEIRAIAQRcqgDAELMEKSVDGFMVElENEKAELVQKLKEAQTI-IAQHVAENPRSEEDRNYESTIAQLKDEI 220
Cdd:PTZ00121 1174 DAKKAEAARKAEEVR---KAEELRKAEDARKAE-AARKAEEERKAEEARKAeDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  221 QILNKRLEDEALAQQQQKPKDEIVAESEKKLKELK---ERNKQLVMEKSEIQRELDNINDHLDQVlvEKATVVQQRDDMQ 297
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaeEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEA 1327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  298 AELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKI--------ALIKKQEEV--TIEARKSVETDDHLS 367
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeakkkadAAKKKAEEKkkADEAKKKAEEDKKKA 1407

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  368 EEV---VAAKNTIASLQATNEEREtEIKKLKQRMDEERASHTAQSE-QEMKQLEAHYERAQKMLQDNVEQMNVENRGLRD 443
Cdd:PTZ00121 1408 DELkkaAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486


                  ....*...
gi 922581144  444 EIEKLSQQ 451
Cdd:PTZ00121 1487 EAKKKAEE 1494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 318-600 4.40e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.16  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  318 QDEAEKAKKQVADFEEKLKEIEtEKIALIKKQEEVTIEARKSVEtddhlsEEVVAAKNTIASLQATNEERETEIKKLKQR 397
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALE------RRIAALARRIRALEQELAALEAELAELEKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  398 MDEERASHTAQSEQEMKQLEAHYERAQ----KML--QDNVEQMNVENRGLRDEIEKLSQQMAALprgglneqqlheifnw 471
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALYRLGRqpplALLlsPEDFLDAVRRLQYLKYLAPARREQAEEL---------------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  472 vseeKATREEMENLTRKITGEVESLKNnsplttsnyiqntpsgwgsrrmnnvARKDGLDLQRQLQAEIDAKLKLKAELKN 551
Cdd:COG4942   156 ----RADLAELAALRAELEAERAELEA-------------------------LLAELEEERAALEALKAERQKLLARLEK 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 922581144  552 SQEQYLTSAARLDDTEKRMASLMREVAMlKQQKNIENSSDSAFSSTMGR 600
Cdd:COG4942   207 ELAELAAELAELQQEAEELEALIARLEA-EAAAAAERTPAAGFAALKGK 254
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
174-497 4.52e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQHVAENPR-SEEDRNYEST---IAQLKDEIQILNKRLED-EALAQQQQKPkdeiVAESE 248
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKlEKEVKELEELkeeIEELEKELESLEGSKRKlEEKIRELEER----IEELK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  249 KKLKELKERNKQL------VMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELadvgdslltekdsvkrlqDEAE 322
Cdd:PRK03918  273 KEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI------------------KELE 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  323 KAKKQVADFEEKLKEIEtEKIALIKKQEEVTIEARKSVETDDHLS-----EEVVAAKNTIASLQATNEERETEIKKLKQR 397
Cdd:PRK03918  335 EKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  398 ---MDEERASHTAQ------------------SEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALP 456
Cdd:PRK03918  414 igeLKKEIKELKKAieelkkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  457 RGGLNEQQLHEIFNWVSE---------EKATR--EEMENLTRKITGEVESLK 497
Cdd:PRK03918  494 ELIKLKELAEQLKELEEKlkkynleelEKKAEeyEKLKEKLIKLKGEIKSLK 545
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 245-451 4.66e-09

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.84  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  245 AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADvgdslltekdsvkrLQDEAEKA 324
Cdd:COG3883    12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------LQAEIAEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  325 KKQVADFEEKLKEIetekIALIKKQEEVT------------------IEARKSV-ETDDHLSEEVVAAKNTIASLQATNE 385
Cdd:COG3883    78 EAEIEERREELGER----ARALYRSGGSVsyldvllgsesfsdfldrLSALSKIaDADADLLEELKADKAELEAKKAELE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144  386 ERETEIKKLKQRMDEERASHTAQSEqEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQ 451
Cdd:COG3883   154 AKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 676-727 4.74e-09

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 53.43  E-value: 4.74e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPV 727
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNCGV 54
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
233-499 4.84e-09

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  233 AQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQV--LVEKATVVQQRDDMQAELADvgdsLLTE 310
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELER----LDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  311 KDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETE 390
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  391 IKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMA-ALPRgglNEQQLHEIF 469
Cdd:COG4913   764 ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEdGLPE---YEERFKELL 840

                         250       260       270
                  ....*....|....*....|....*....|
gi 922581144  470 NwvseeKATREEMENLTRKITGEVESLKNN 499
Cdd:COG4913   841 N-----ENSIEFVADLLSKLRRAIREIKER 865
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 1-100 5.99e-09

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: 59.19  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKImsHQDMLDFPDdeidWVvSEEAKDLIRQLICSSDVRfgRNGLS-DFQLHPFFEGIDWNTI 79
Cdd:cd05620   189 MLIGQSPFHGDDEDELFESI--RVDTPHYPR----WI-TKESKDILEKLFERDPTR--RLGVVgNIRGHPFFKTINWTAL 259

                          90       100
                  ....*....|....*....|...
gi 922581144   80 --RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05620   260 ekRELDPPFKPKVKSPSDYSNFD 282
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
 676-725 6.22e-09

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 (RASGRP2) and similar proteins; RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. It may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is also involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410411  Cd Length: 56  Bit Score: 53.35  E-value: 6.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20861     4 HNFAERTFLRPVACRHCKNLILGIYKQGLKCRACGVNCHKQCKDHLSIEC 53
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 179-465 6.35e-09

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 59.91  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   179 KAELVQK-----LKEAQTIIAQHVAENPRSEEDRNYESTIaqlKDEIQILNKRLEDEalaqqqqkpkdeiVAESEKKLKE 253
Cdd:pfam07888   28 RAELLQNrleecLQERAELLQAQEAANRQREKEKERYKRD---REQWERQRRELESR-------------VAELKEELRQ 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   254 LKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQvadfee 333
Cdd:pfam07888   92 SREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ------ 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   334 kLKEIETEKIALIKKQEEVTIEARksvetddHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERaSHTAQSEQEM 413
Cdd:pfam07888  166 -RKEEEAERKQLQAKLQQTEEELR-------SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-RKEAENEALL 236

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   414 KQLEAHYERAqkmlqdNVEQMNVEnrGLRDEIEKLSQQ----MAALPRGGLNEQQL 465
Cdd:pfam07888  237 EELRSLQERL------NASERKVE--GLGEELSSMAAQrdrtQAELHQARLQAAQL 284
PTZ00121 PTZ00121
MAEBL; Provisional
 141-497 8.27e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 8.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  141 SDARSLTDEIRAIAQRCQGDAELMEKSvdgfmvELENEKAELVQKLKEAQTII--AQHVAENPRSEEDRNYESTIAQLKD 218
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKA------EEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEEAKKAD 1447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  219 EiqiLNKRLEDEALAQQQQKPKDEI--------VAESEKKLKELKERNKQlVMEKSEIQRELDNINDHLDQVlvEKATVV 290
Cdd:PTZ00121 1448 E---AKKKAEEAKKAEEAKKKAEEAkkadeakkKAEEAKKADEAKKKAEE-AKKKADEAKKAAEAKKKADEA--KKAEEA 1521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  291 QQRDDM-QAELADVGDSLltEKDSVKRLQDEAEKAKK-----QVADFEEKLKEIETEKIAL-----IKKQEEVTIEARKS 359
Cdd:PTZ00121 1522 KKADEAkKAEEAKKADEA--KKAEEKKKADELKKAEElkkaeEKKKAEEAKKAEEDKNMALrkaeeAKKAEEARIEEVMK 1599

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  360 VETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKmLQDNVEQMNVENR 439
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKAEEDKKKAE 1678

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144  440 GLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLK 497
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-438 8.82e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 59.01  E-value: 8.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  203 SEEDRNYESTIAQLKDEIQILNKRLEdeALAQQQQKPKDEIvAESEKKLKELKERNKqlvmeksEIQRELDNINDHLDQV 282
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELA--ALKKEEKALLKQL-AALERRIAALARRIR-------ALEQELAALEAELAEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  283 LVEKATVVQQRDDMQAELADVGDSL--LTEKDSVKRL--QDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARK 358
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALyrLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  359 SVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERAShTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVEN 438
Cdd:COG4942   169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 675-727 1.04e-08

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 52.69  E-value: 1.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPV 727
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWGLLNQGYQCEVCNFVSHERCLKTVVTPCSS 53
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 138-582 1.17e-08

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 59.80  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   138 SLLSDARSLTDEIRAIAQRcQGDAELMEKSVDGFMVEL-------ENEKAELVQKL------------------------ 186
Cdd:pfam01576  381 ALESENAELQAELRTLQQA-KQDSEHKRKKLEGQLQELqarlsesERQRAELAEKLsklqselesvssllneaegknikl 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   187 -KEAQTIIAQ-HVAENPRSEEDR---NYESTIAQLKDEIQILNKRLEDEALAQQ----QQKPKDEIVAESEKKLKELKER 257
Cdd:pfam01576  460 sKDVSSLESQlQDTQELLQEETRqklNLSTRLRQLEDERNSLQEQLEEEEEAKRnverQLSTLQAQLSDMKKKLEEDAGT 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   258 NKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELadvgDSLLTEKDSVKRLQDEAEKAKKQvadFEEKLKE 337
Cdd:pfam01576  540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL----DDLLVDLDHQRQLVSNLEKKQKK---FDQMLAE 612

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   338 ietEKIALIKKQEEvtieaRKSVETDDHLSE-EVVAAKNTIASLQATNEERETEIKKLKQRMDEERASH--TAQSEQEMk 414
Cdd:pfam01576  613 ---EKAISARYAEE-----RDRAEAEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNVHEL- 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   415 qleahyERAQKMLQDNVEQMNVENRGLRDEIE-------KLSQQMAAL---------PRGGLNEQ-------QLHEIFNW 471
Cdd:pfam01576  684 ------ERSKRALEQQVEEMKTQLEELEDELQatedaklRLEVNMQALkaqferdlqARDEQGEEkrrqlvkQVRELEAE 757

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   472 VSEEKATREEMENLTRKITGEVESLKnnsplttsnyiqntpsgwGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKN 551
Cdd:pfam01576  758 LEDERKQRAQAVAAKKKLELDLKELE------------------AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819

                          490       500       510
                   ....*....|....*....|....*....|.
gi 922581144   552 SQEQYLTSAArldDTEKRMASLMREVAMLKQ 582
Cdd:pfam01576  820 SRDEILAQSK---ESEKKLKNLEAELLQLQE 847
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 1-135 1.29e-08

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: 58.27  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMsHQDMLdFPDdeidWVvSEEAKDLIRQLICSSDV-RFG----RNGLSDFQLHPFFEGID 75
Cdd:cd05591   189 MMAGQPPFEADNEDDLFESIL-HDDVL-YPV----WL-SKEAVSILKAFMTKNPAkRLGcvasQGGEDAIRQHPFFREID 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144   76 WNTI--RDSNPPYVPEVSSPEDTSNFDVDVCEDD--FTPCEtqpPRVLAAFtgNHLPFVGFSYT 135
Cdd:cd05591   262 WEALeqRKVKPPFKPKIKTKRDANNFDQDFTKEEpvLTPVD---PAVIKQI--NQEEFRGFSFV 320
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 271-477 1.37e-08

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 57.85  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   271 ELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDslltekdsvkRLQDEAEKAKKQVADFEEKLkeiETEKialiKKQE 350
Cdd:pfam09787   48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEA----------QQQEEAESSREQLQELEEQL---ATER----SARR 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   351 EVTIEARKSVETDDHLSEEVVAAKNTiasLQATNEERETEIKKLKQRMDEERASHTAQSEQE--MKQL-EAHYERaqkml 427
Cdd:pfam09787  111 EAEAELERLQEELRYLEEELRRSKAT---LQSRIKDREAEIEKLRNQLTSKSQSSSSQSELEnrLHQLtETLIQK----- 182

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 922581144   428 QDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHeIFNWVSEEKA 477
Cdd:pfam09787  183 QTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSIN-MEGISDGEGT 231
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 1-134 1.38e-08

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: 58.10  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLDfPDdeidwvVSEEAKDLIRQLICSSDV-RFG-RNGLSDFQLHPFFEGIDWNT 78
Cdd:cd05602   201 MLYGLPPFYSRNTAEMYDNILNKPLQLK-PN------ITNSARHLLEGLLQKDRTkRLGaKDDFTEIKNHIFFSPINWDD 273

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144   79 I--RDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCETQPPR---VLAAFTGNHLPFVGFSY 134
Cdd:cd05602   274 LinKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQSPDsilVTASIKEAAEAFLGFSY 334
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 675-725 1.49e-08

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 52.00  E-value: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILiglDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20826     2 SHSFKEKSFRKPRTCDVCKQII---WNEGSSCRVCKYACHRKCEPKVTAAC 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 174-429 1.57e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.26  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   174 ELENEKAEL---VQKLKEAQTIIAQHVAENPRS--EEDRNYESTIAQLKDEIQILNKrledealAQQQQKPKDEIVAESE 248
Cdd:TIGR04523  444 DLTNQDSVKeliIKNLDNTRESLETQLKVLSRSinKIKQNLEQKQKELKSKEKELKK-------LNEEKKELEEKVKDLT 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   249 KKLKELKERNKQLVMEKSEIQRELDNINDHL---DQVLVEKA--TVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEK 323
Cdd:TIGR04523  517 KKISSLKEKIEKLESEKKEKESKISDLEDELnkdDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   324 AK----KQVADFEEKLKEIEtEKIALIKKQ-EEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRM 398
Cdd:TIGR04523  597 EKkdliKEIEEKEKKISSLE-KELEKAKKEnEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 922581144   399 DE----------ERASHTAQ------SEQEMKQLEAHYERAQKMLQD 429
Cdd:TIGR04523  676 DDiielmkdwlkELSLHYKKyitrmiRIKDLPKLEEKYKEIEKELKK 722
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-580 1.64e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  139 LLSDARSLTDEIRAIAQRCQGDAELMEksvdgfmvELENEKAELVQKLKEAQTIIAQHVAENPRSEEDR----------- 207
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeeeleela 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  208 ----NYESTIAQLKDEIQILNKRLEDEAL----AQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHL 279
Cdd:COG1196   386 eellEALRAAAELAAQLEELEEAEEALLErlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  280 DQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKS 359
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  360 VETDDHLSEEVVAAKNTIASLQATNEERETEI-----------KKLKQRMDEERASHTAQSEQ----EMKQLEAHYERAQ 424
Cdd:COG1196   546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpldkiraraalAAALARGAIGAAVDLVASDLreadARYYVLGDTLLGR 625

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  425 KMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNwvSEEKATREEMENLTRKITGEVESLKNNSPLTT 504
Cdd:COG1196   626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--AALLEAEAELEELAERLAEEELELEEALLAEE 703

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  505 SNyiqntpsgwgsRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQ-----------YLTSAARLDDTEKRMASL 573
Cdd:COG1196   704 EE-----------ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEeeelleeealeELPEPPDLEELERELERL 772


                  ....*..
gi 922581144  574 MREVAML 580
Cdd:COG1196   773 EREIEAL 779
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
 676-725 2.08e-08

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 52.32  E-value: 2.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20844     6 HTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCRFNCHKRCASKVPRDC 55
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 176-596 2.13e-08

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 58.90  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   176 ENEKAELVQKLKEAqtiiaqhvaenprsEEDRnyeSTIAQLKDEIQILNKR-LEDEALAQQQQKPKDEIVAESEKKLKEL 254
Cdd:TIGR00606  244 ENELDPLKNRLKEI--------------EHNL---SKIMKLDNEIKALKSRkKQMEKDNSELELKMEKVFQGTDEQLNDL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   255 KERNKQLVMEKSE----IQRELDNINDHLDQVLVEKAT--VVQQRDDMQAELADVG----DSLLTE-------------- 310
Cdd:TIGR00606  307 YHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTEllVEQGRLQLQADRHQEHirarDSLIQSlatrleldgfergp 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   311 ----------KDSVKRLQDEAEKAKKQVADFEEK--LKEIETEKIALIKKQEEVTIEARKSVetddhLSEEVVAAKNTIA 378
Cdd:TIGR00606  387 fserqiknfhTLVIERQEDEAKTAAQLCADLQSKerLKQEQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIK 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   379 SLQATNEERETEIKKlkqrmdeerashtaqsEQEMKQLEAHYERAQKmlQDNVEQMNVENRGLRDEIEKLSQQMAALPRG 458
Cdd:TIGR00606  462 ELQQLEGSSDRILEL----------------DQELRKAERELSKAEK--NSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   459 glNEQQLHEifnwvseeKATREEMENLTRKITGEVESLKNNS-----PLTT-SNYIQNTP--SGWGSRRMN--NVARKDG 528
Cdd:TIGR00606  524 --MEQLNHH--------TTTRTQMEMLTKDKMDKDEQIRKIKsrhsdELTSlLGYFPNKKqlEDWLHSKSKeiNQTRDRL 593

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144   529 LDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARL------DDTEKRMASLMREVAMLKQQKNIENSSDSAFSS 596
Cdd:TIGR00606  594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
C1_Munc13-1 cd20858
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ...
 676-725 2.30e-08

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410408  Cd Length: 60  Bit Score: 51.63  E-value: 2.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20858     8 HNFEVWTATTPTYCYECEGLLWGIARQGMRCTECGVKCHEKCQDLLNADC 57
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 140-646 2.41e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 58.83  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   140 LSDARSLTDEIRAIAQRCQGDAELMEKSvdgfmveleneKAELVQKLKEAQTIIAQHVAENPRSEEdrnyestIAQLKDE 219
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKLQSL-----------CKELDILQREQATIDTRTSAFRDLQGQ-------LAHAKKQ 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   220 IQILNKRLEDEALA----QQQQKPKDEIVAESEKKLKELKER--NKQLVMEKSEiqrELDNINDHLDQVLVEKATVVQQR 293
Cdd:TIGR00618  433 QELQQRYAELCAAAitctAQCEKLEKIHLQESAQSLKEREQQlqTKEQIHLQET---RKKAVVLARLLELQEEPCPLCGS 509

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   294 D-DMQAELADVGDS------LLTEKDSVKRLQDEAEKA-------KKQVADFEEKLKEIETEKIALIKKQEEVTIEARKS 359
Cdd:TIGR00618  510 CiHPNPARQDIDNPgpltrrMQRGEQTYAQLETSEEDVyhqltseRKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   360 VETDDHLSEEVvaAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQ-KMLQDNVEQMNVEN 438
Cdd:TIGR00618  590 QNITVRLQDLT--EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQlTLTQERVREHALSI 667

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   439 RglRDEIEKLSQQMAALPRGGLNEQQLHEIfnwvseekatREEMENLTRKITGEVESLKNNSPLTtsNYIQNTPSGWGSR 518
Cdd:TIGR00618  668 R--VLPKELLASRQLALQKMQSEKEQLTYW----------KEMLAQCQTLLRELETHIEEYDREF--NEIENASSSLGSD 733

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   519 -RMNNVARKDgldLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDtekrmaslmrEVAMLKQqkNIENssdsafsst 597
Cdd:TIGR00618  734 lAAREDALNQ---SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA----------ELSHLAA--EIQF--------- 789

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 922581144   598 mgrgdlmisMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVPKR 646
Cdd:TIGR00618  790 ---------FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 279-425 2.75e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.51  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  279 LDQVLVEKATVVQQRDDMQAELADVGDSlltEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIAL--IKKQEEvtiEA 356
Cdd:PRK09510   50 IDAVMVDPGAVVEQYNRQQQQQKSAKRA---EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAqeQKKQAE---EA 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144  357 RKSVETDDHLSEEVVAAKNTIASLQATNEER---------ETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQK 425
Cdd:PRK09510  124 AKQAALKQKQAEEAAAKAAAAAKAKAEAEAKraaaaakkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 1-116 2.91e-08

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 57.24  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMLD--FPDdeidwVVSEEAKDLIRQLICSSDVR---FGRNGLSDFQLHPFFEGID 75
Cdd:cd05614   200 LLTGASPFTLEGEKNTQSEVSRRILKCDppFPS-----FIGPVARDLLQKLLCKDPKKrlgAGPQGAQEIKEHPFFKGLD 274

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 922581144   76 WNTI--RDSNPPYVPEVSSPEDTSNF--DVDVCEDDFTPCETQPP 116
Cdd:cd05614   275 WEALalRKVNPPFRPSIRSELDVGNFaeEFTNLEPVYSPAGTPPS 319
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
 674-725 3.80e-08

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 50.76  E-value: 3.80e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20795     2 RPHSLFVHSYKSPTFCDFCGEMLFGLVRQGLKCEGCGLNFHKRCAYKIPNNC 53
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 676-725 3.86e-08

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 50.79  E-value: 3.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERmKIKTPTKCGHCTSILIGldrqGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20812     3 HRFSK-KLFMRQTCDYCHKQMFF----GLKCKDCKYKCHKKCAKKAPPSC 47
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 1-77 4.83e-08

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: 55.95  E-value: 4.83e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDEIDWVvSEEAKDLIRQLICSS-DVRFGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05611   189 FLFGYPPFHAETPDAVFDNILSRR--INWPEEVKEFC-SPEAVDLINRLLCMDpAKRLGANGYQEIKSHPFFKSINWD 263
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 2-76 5.21e-08

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: 55.87  E-value: 5.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144    2 LYGTTPFYSERLVDTYGKIMShqDMLDFPDDEiDWVvSEEAKDLIRQLICSSDV-RFGRNGLSDFQLHPFFEGIDW 76
Cdd:cd05609   209 LVGCVPFFGDTPEELFGQVIS--DEIEWPEGD-DAL-PDDAQDLITRLLQQNPLeRLGTGGAEEVKQHPFFQDLDW 280
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
141-437 5.49e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.36  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  141 SDARSLTDEIRAIAQRCQGDAELMEKSVDgfmvELENEKAELVQKLKEAQTIIaqhvaENPRSE-EDRnyESTIAQLKDE 219
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDAD----DLEERAEELREEAAELESEL-----EEAREAvEDR--REEIEELEEE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  220 IQILNKRLED--------EALAQQQQKPKDEI---VAESEKKLKELKER---NKQLV-----------MEKSEIQRELDN 274
Cdd:PRK02224  393 IEELRERFGDapvdlgnaEDFLEELREERDELrerEAELEATLRTARERveeAEALLeagkcpecgqpVEGSPHVETIEE 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  275 INDHLDQVLVEKATVVQQRDDMQAELaDVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEiETEKIALIKKQ-EEVT 353
Cdd:PRK02224  473 DRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRERaAELE 550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  354 IEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLK----------------QRMDEERASHTAQSEQEMKQLE 417
Cdd:PRK02224  551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllaaiadaedeiERLREKREALAELNDERRERLA 630

                         330       340
                  ....*....|....*....|
gi 922581144  418 AHYERAQKmLQDNVEQMNVE 437
Cdd:PRK02224  631 EKRERKRE-LEAEFDEARIE 649
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 1-100 5.52e-08

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: 56.47  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQDMldFPDdeidWVvSEEAKD-LIRQLICSSDVRFGRNGlsDFQLHPFFEGIDWNTI 79
Cdd:cd05619   199 MLIGQSPFHGQDEEELFQSIRMDNPF--YPR----WL-EKEAKDiLVKLFVREPERRLGVRG--DIRQHPFFREINWEAL 269

                          90       100
                  ....*....|....*....|...
gi 922581144   80 --RDSNPPYVPEVSSPEDTSNFD 100
Cdd:cd05619   270 eeREIEPPFKPKVKSPFDCSNFD 292
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 136-418 6.10e-08

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 56.96  E-value: 6.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   136 HGSLLSDARSLTDEIRAI-----------------AQRCQGDAELMEKSVDGFMVELENEKAELvqklKEAQTiiAQHVA 198
Cdd:pfam05701  133 HAAAVAELKSVKEELESLrkeyaslvserdiaikrAEEAVSASKEIEKTVEELTIELIATKESL----ESAHA--AHLEA 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   199 ENPR------SEEDR-NYESTIAQLKDEIQILNKRL--------EDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVM 263
Cdd:pfam05701  207 EEHRigaalaREQDKlNWEKELKQAEEELQRLNQQLlsakdlksKLETASALLLDLKAELAAYMESKLKEEADGEGNEKK 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   264 EKSEIQRELDNINDHLDQVlveKATVVQQRDD----------MQAELADvgdslltEKDSVKRLQDEAEKAKKQVADFEE 333
Cdd:pfam05701  287 TSTSIQAALASAKKELEEV---KANIEKAKDEvnclrvaaasLRSELEK-------EKAELASLRQREGMASIAVSSLEA 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   334 KLKEIETEkIALIKKQEEvtiEAR-KSVETDDHLSEEVVAAKNTIASLQATNEeretEIKKLKQRMDEERAS-HTAQS-- 409
Cdd:pfam05701  357 ELNRTKSE-IALVQAKEK---EAReKMVELPKQLQQAAQEAEEAKSLAQAARE----ELRKAKEEAEQAKAAaSTVESrl 428


                   ....*....
gi 922581144   410 EQEMKQLEA 418
Cdd:pfam05701  429 EAVLKEIEA 437
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
177-583 6.79e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  177 NEKAELVQKLKEAQTIIAQHVAENPRSEEDR----NYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIvAESEKKLK 252
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEeeleELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-AELPERLE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  253 ELKERN---KQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQR-DDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQV 328
Cdd:COG4717   150 ELEERLeelRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  329 ADFEEKLkeiETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASL------------------QATNEERETE 390
Cdd:COG4717   230 EQLENEL---EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallflllareKASLGKEAEE 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  391 IKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQD--NVEQMNVENRGLRDE--IEKLSQQMAAL--PRGGLNEQQ 464
Cdd:COG4717   307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEElqLEELEQEIAALlaEAGVEDEEE 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  465 LHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNtpsgwgsrRMNNVARKdgldlQRQLQAEIDAKLK 544
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE--------ELEELEEE-----LEELEEELEELRE 453

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 922581144  545 LKAELKNSQEQyLTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:COG4717   454 ELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEE 491
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
 675-725 6.98e-08

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 50.38  E-value: 6.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRqGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20818     3 GHKFATVQFNIPTYCEVCNSFIWLMEK-GLVCQVCKFTCHKKCYSKITAPC 52
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 249-422 8.00e-08

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.55  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  249 KKLKELKERNKQLvmekSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVgdsllteKDSVKRLQDEAEKAKKQV 328
Cdd:COG1579     7 RALLDLQELDSEL----DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  329 ADFEEKLKEIETEK--------IALIKKQ----EEVTIEARKSVETddhLSEEVVAAKNTIASLQAT----NEERETEIK 392
Cdd:COG1579    76 KKYEEQLGNVRNNKeyealqkeIESLKRRisdlEDEILELMERIEE---LEEELAELEAELAELEAEleekKAELDEELA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 922581144  393 KLKQRMDEERASHTAQSEQEMKQLEAHYER 422
Cdd:COG1579   153 ELEAELEELEAEREELAAKIPPELLALYER 182
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 676-725 8.33e-08

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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. 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. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 50.03  E-value: 8.33e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 144-492 8.53e-08

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.98  E-value: 8.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   144 RSLTDEIraiaQRCQGDAELMEKSVDGFMVELENEKA---------ELVQKLKEAQTIIAQHVAENPRSEEDRNYestia 214
Cdd:TIGR00606  754 QKVNRDI----QRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQAAKLQGSDLDRTV----- 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   215 qlkdeiQILNKRLEDealaqqQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIqreldninDHLDQVLVEKATVVQQRD 294
Cdd:TIGR00606  825 ------QQVNQEKQE------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT--------NELKSEKLQIGTNLQRRQ 884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   295 DMQAELadvgDSLLTEkdsVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEA-----------------R 357
Cdd:TIGR00606  885 QFEEQL----VELSTE---VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAqdkvndikekvknihgyM 957

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   358 KSVET--DDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEmkqleahyeraqKMLQDNVEQMN 435
Cdd:TIGR00606  958 KDIENkiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE------------RWLQDNLTLRK 1025

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   436 VENrglrdEIEKLSQQMAALpRGGLNEQQlheifnwVSEEKATREEMENLTRKITGE 492
Cdd:TIGR00606 1026 REN-----ELKEVEEELKQH-LKEMGQMQ-------VLQMKQEHQKLEENIDLIKRN 1069
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 674-725 8.95e-08

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 49.59  E-value: 8.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGldrQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20822     1 RGHKFVQKQFYQIMRCAVCGEFLVN---AGYQCEDCKYTCHKKCYEKVVTKC 49
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
244-504 9.18e-08

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.30  E-value: 9.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 VAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQvLVEKA-TVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAE 322
Cdd:COG1340    17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-LREEAqELREKRDELNEKVKELKEERDELNEKLNELREELD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  323 KAKKQVADFEEKLKEIET--EKIA-LIKKQE--EVTIEA-RKSVETDDHLSEEVVAAKnTIASLQATNEERETEIKKLKQ 396
Cdd:COG1340    96 ELRKELAELNKAGGSIDKlrKEIErLEWRQQteVLSPEEeKELVEKIKELEKELEKAK-KALEKNEKLKELRAELKELRK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  397 RMDEERA--SHTAQSEQEMK-QLEAHYERAQKmLQDNVEQMNVENRGLRDEIEKLSQQMAALPRgGLNE--QQLHEIFNW 471
Cdd:COG1340   175 EAEEIHKkiKELAEEAQELHeEMIELYKEADE-LRKEADELHKEIVEAQEKADELHEEIIELQK-ELRElrKELKKLRKK 252

                         250       260       270
                  ....*....|....*....|....*....|...
gi 922581144  472 VSEEKATREEMEnLTRKITGEVESLKNNSPLTT 504
Cdd:COG1340   253 QRALKREKEKEE-LEEKAEEIFEKLKKGEKLTT 284
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 2-100 1.02e-07

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: 55.66  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    2 LYGTTPFYSERLVDTYGKIMSHqdmlDFPDDEIDWVVSEEAKDLIRQLICSSDVRfgRNGLSDFQLHPFFEGIDWNTIRD 81
Cdd:cd05610   251 LTGIPPFNDETPQQVFQNILNR----DIPWPEGEEELSVNAQNAIEILLTMDPTK--RAGLKELKQHPLFHGVDWENLQN 324

                          90
                  ....*....|....*....
gi 922581144   82 SNPPYVPEVSSPEDTSNFD 100
Cdd:cd05610   325 QTMPFIPQPDDETDTSYFE 343
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
204-470 1.10e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.68  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  204 EEDRNYESTIAQLKDEIQILNKRLEDealAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVL 283
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQ---ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  284 VEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKiaLIKKQEEVTIEARKSVETD 363
Cdd:COG4372   122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEANRNAEKE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  364 DHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAH----YERAQKMLQDNVEQMNVENR 439
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVilkeIEELELAILVEKDTEEEELE 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 922581144  440 GLRDEIEKLSQQMAALPRGGLNEQQLHEIFN 470
Cdd:COG4372   280 IAALELEALEEAALELKLLALLLNLAALSLI 310
C1_Stac2 cd20881
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 674-726 1.12e-07

protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich domain-containing protein 2 (Stac2) and similar proteins; Stac2, also called 24b2/Stac2, or Src homology 3 and cysteine-rich domain-containing protein 2, plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. It slows down the inactivation rate of the calcium channel CACNA1C. Stac2 contains a cysteine-rich C1 domain and one SH3 domain at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410431  Cd Length: 59  Bit Score: 49.83  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVS-QSCP 726
Cdd:cd20881     4 RTHSFQEHVFKKPSPCELCHQMIVGNSKQGLRCKMCKVSVHLWCSEEVShQQCT 57
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
 748-836 1.12e-07

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


Pssm-ID: 269948  Cd Length: 110  Bit Score: 51.20  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  748 EGLVKTPRAGGVRK-GWQTAYVVVCDFKLYLYDCTVDRQNkmqdvkNEIRLVLDMrDPDFTVCGVSEADVIHAQKGDIPK 826
Cdd:cd01242     4 EGWLSLPNKQNIRRhGWKKQYVVVSSKKILFYNSEQDKAN------SNPILVLDI-DKLFHVRSVTQGDVIRADAKEIPR 76

                          90
                  ....*....|
gi 922581144  827 IFrvtttQIL 836
Cdd:cd01242    77 IF-----QIL 81
Filament pfam00038
Intermediate filament protein;
217-455 1.13e-07

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 55.31  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   217 KDEIQILNKRLE---DEALAQQQQKpkdeivAESEKKLKELKERNKQLVMEKSEI-QRELDNINDHLDQVLVEKATVVQQ 292
Cdd:pfam00038    3 KEQLQELNDRLAsyiDKVRFLEQQN------KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   293 RDDMQAELADVGDSLltEKDSVKRLQDEAEKA--KKQV-------ADFEEKLKEIeTEKIALIKK--QEEVTiEARKSVe 361
Cdd:pfam00038   77 LDNLRLAAEDFRQKY--EDELNLRTSAENDLVglRKDLdeatlarVDLEAKIESL-KEELAFLKKnhEEEVR-ELQAQV- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   362 TDDHLSEEVVAAKNtiaslqatneereteiKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGL 441
Cdd:pfam00038  152 SDTQVNVEMDAARK----------------LDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA 215

                          250
                   ....*....|....
gi 922581144   442 RDEIEKLSQQMAAL 455
Cdd:pfam00038  216 KEEITELRRTIQSL 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-425 1.34e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  221 QILNKRLEDEALA---QQQQKPKDEI--VAESEKKLKELKERNKQLvmekSEIQRELDNINDHLDQVLVEKATVVQQRDD 295
Cdd:COG4717    45 AMLLERLEKEADElfkPQGRKPELNLkeLKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  296 M--QAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEV-TIEARKSVETDDHLSEevva 372
Cdd:COG4717   121 LekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQD---- 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  373 AKNTIASLQATNEERETEIKKLKQRMDeerashtaQSEQEMKQLEAHYERAQK 425
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELE--------ELEEELEQLENELEAAAL 241
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1015-1199 1.40e-07

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 56.44  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144 1015 FKKSVTIFQIdrsekrhkkwKDLAMPGTPQSIAIFNGRLYVGfshSFRSWSLVGVDSspvgsgdasgavLQHISLVNMED 1094
Cdd:COG5422   993 LKKALTIELS----------TELYVPSEPLSVHFLKNKLCIG---CKKGFEIVSLEN------------LRTESLLNPAD 1047

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144 1095 TSLQFLNQQTSYEAKLIVNVPGspdEYLLVFNMIGLYVNEMGRRSRlPEVMF--PTQAKYFAYHEPYLCVFSENEVDIFN 1172
Cdd:COG5422  1048 TSPLFFEKKENTKPIAIFRVSG---EFLLCYSEFAFFVNDQGWRKR-TSWIFhwEGEPQEFALSYPYILAFEPNFIEIRH 1123

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 922581144 1173 VTLAEWVQTI---NLR----SAKPLSGDG-ILSTC 1199
Cdd:COG5422  1124 IETGELIRCIlghNIRlltdGRGPLLHGGeILYKC 1158
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 204-504 1.48e-07

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 56.21  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   204 EEDRNYESTIAQLKDEIQILNKRLEdealaqQQQKPKDEIVAESEKKLKELKERNKQL--VMEKS-------EIQRELDN 274
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKID------HHIKALEEIKKKSENYIDEIKAQINDLedVADKAisnddpeEIEKKIEN 1177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   275 INDHLDQvlveKATVVQQRDDMQAELADVgdslltEKDsvkrlQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTI 354
Cdd:TIGR01612 1178 IVTKIDK----KKNIYDEIKKLLNEIAEI------EKD-----KTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMI 1242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   355 EA-RKSVETDDHLSEEVVAAKNTIASLQATNEERETeikkLKQRMDEERASHTAqSEQEMKQLEAHYERAQKMLQDNVEQ 433
Cdd:TIGR01612 1243 KAmEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMET----FNISHDDDKDHHII-SKKHDENISDIREKSLKIIEDFSEE 1317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   434 MNVENrgLRDEIEKL---SQQMAALPRGGLNE-------QQLHEIFNWVSEEKATREEMENLTRKITGE-------VESL 496
Cdd:TIGR01612 1318 SDIND--IKKELQKNlldAQKHNSDINLYLNEianiyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDEldkseklIKKI 1395


                   ....*...
gi 922581144   497 KNNSPLTT 504
Cdd:TIGR01612 1396 KDDINLEE 1403
C1_Munc13-2-like cd20859
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar ...
 658-725 1.53e-07

protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar proteins; Munc13-2, also called protein unc-13 homolog B (Unc13B), plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410409  Cd Length: 82  Bit Score: 50.06  E-value: 1.53e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144  658 KTASGIFSPVSISAmerGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20859     5 KTLQALIYPISCTT---PHNFEVWTATTPTYCYECEGLLWGIARQGMRCSECGVKCHEKCQDLLNADC 69
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
174-435 1.61e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIA---------QHVAENPRSEED-RNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEI 243
Cdd:COG4913   621 ELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDLAALEEQLEELEAE 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 VAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQvlVEKATVVQQRDDMQAELADVGDSLLtEKDSVKRLQDEAEK 323
Cdd:COG4913   701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERFAAALGDAV-ERELRENLEERIDA 777

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  324 AKKQVADFEEKLkeieTEKIALIKKQ-EEVTIEARKSVET----DDHLSEevvaakntiasLQATN-EERETEIKKLKQR 397
Cdd:COG4913   778 LRARLNRAEEEL----ERAMRAFNREwPAETADLDADLESlpeyLALLDR-----------LEEDGlPEYEERFKELLNE 842

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 922581144  398 mdeerashtaQSEQEMKQLEAHYERAQKMLQDNVEQMN 435
Cdd:COG4913   843 ----------NSIEFVADLLSKLRRAIREIKERIDPLN 870
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 169-424 1.66e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  169 DGFMVELENEKAELVQKLKEAQtiiaqhvaenprsEEDRNYESTIAQLKDEIQILNKRLEDealAQQQQKPKDEIVAESE 248
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQ-------------AELDALQAELEELNEEYNELQAELEA---LQAEIDKLQAEIAEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  249 KKLKELKERNKQLVmekSEIQRELDNINDhLDQVLVEK--ATVVQQRDDMQAeLADVGDSLLTEkdsVKRLQDEAEKAKK 326
Cdd:COG3883    79 AEIEERREELGERA---RALYRSGGSVSY-LDVLLGSEsfSDFLDRLSALSK-IADADADLLEE---LKADKAELEAKKA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  327 QVadfEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHT 406
Cdd:COG3883   151 EL---EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227

                         250
                  ....*....|....*...
gi 922581144  407 AQSEQEMKQLEAHYERAQ 424
Cdd:COG3883   228 AAAAAAAAAAAAAAAAAS 245
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
 137-400 1.75e-07

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 55.63  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   137 GSLLSDARSLTDEIRAIAQRCQGDAelmeksvdgfMVELENE----KAELVQKLKEAQTIIAQHvaeNPRSEEDRNYEST 212
Cdd:pfam09726  372 GKSGARHKDPAENCIPNNQLSKPDA----------LVRLEQDikklKAELQASRQTEQELRSQI---SSLTSLERSLKSE 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   213 IAQLKDEIQILNKRLEDeaLAQQQQKPKdEIVAESEKKLKELKER----NKQLVMEKSEIQRELDNINDHLDQVL---VE 285
Cdd:pfam09726  439 LGQLRQENDLLQTKLHN--AVSAKQKDK-QTVQQLEKRLKAEQEArasaEKQLAEEKKRKKEEEATAARAVALAAasrGE 515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   286 KATVVQQR-DDMQAELADVGDSLLTEKDSVKRLQDEAekakKQVADFEEKLKEIETEKIALIKKQEE-VTIEARKSVETD 363
Cdd:pfam09726  516 CTESLKQRkRELESEIKKLTHDIKLKEEQIRELEIKV----QELRKYKESEKDTEVLMSALSAMQDKnQHLENSLSAETR 591

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 922581144   364 DHLS--EEVVAAKNTIASLQATNEERETEIKKLKQRMDE 400
Cdd:pfam09726  592 IKLDlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 1-128 1.83e-07

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 54.50  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwVVSEEAKDLIRQLICSS-DVRFGR-NGLSDFQLHPFFEGIDWNT 78
Cdd:cd05586   190 MCCGWSPFYAEDTQQMYRNIAFGK--VRFPKD----VLSDEGRSFVKGLLNRNpKHRLGAhDDAVELKEHPFFADIDWDL 263

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144   79 IRDS--NPPYVPEVSSPEDTSNFDvdvceDDFTPCETQPPRVLAAFTGNHLP 128
Cdd:cd05586   264 LSKKkiTPPFKPIVDSDTDVSNFD-----PEFTNASLLNANIVPWAQRPGLP 310
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 225-504 2.36e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.51  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   225 KRLEDEALAQQQQKPKDEIvaESEKKLKElKERNKQLVMEKS------------EIQRELDNIndHLDQVLVEKATVVQQ 292
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREV--ERRRKLEE-AEKARQAEMDRQaaiyaeqermamERERELERI--RQEERKRELERIRQE 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   293 RDDMQAELADVGDSLLTEKDSV-KRLQDEAEKAKKQVADFEEKLKEIETEKIALIK---KQEEVTIEARKSVETD----- 363
Cdd:pfam17380  369 EIAMEISRMRELERLQMERQQKnERVRQELEAARKVKILEEERQRKIQQQKVEMEQiraEQEEARQREVRRLEEErarem 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   364 DHLSEEVVAAKNTIASLQATNEERETeiKKL--------KQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMN 435
Cdd:pfam17380  449 ERVRLEEQERQQQVERLRQQEEERKR--KKLelekekrdRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   436 V-----ENRGLRDEIEKLSQQMAalprgglNEQQLHEIFNWVSEEKATREEME---NLTRKITgEVESLKNNSPLTT 504
Cdd:pfam17380  527 KaiyeeERRREAEEERRKQQEME-------ERRRIQEQMRKATEERSRLEAMErerEMMRQIV-ESEKARAEYEATT 595
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 240-582 2.41e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.57  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   240 KDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDH---LDQVLVEKATVVQQRDDMQAELA-----------DVGD 305
Cdd:pfam01576    3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEEMRARLAarkqeleeilhELES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   306 SLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEietEKIALIKKQ-EEVTIEAR-KSVETD--------DHLSEEVVAAKN 375
Cdd:pfam01576   83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---EEAARQKLQlEKVTTEAKiKKLEEDillledqnSKLSKERKLLEE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   376 TIASLQATNEERETEIKKLkQRMDEERASHTAQSEQEMKQleahYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAAL 455
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSL-SKLKNKHEAMISDLEERLKK----EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   456 pRGGL--NEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLttsnyiqntpsgwgSRRMNNVARKDGLDLQR 533
Cdd:pfam01576  235 -RAQLakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES--------------ERAARNKAEKQRRDLGE 299

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 922581144   534 QLQAeidaklkLKAELKNSQEqylTSAARLDDTEKRmaslMREVAMLKQ 582
Cdd:pfam01576  300 ELEA-------LKTELEDTLD---TTAAQQELRSKR----EQEVTELKK 334
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 1262-1300 2.43e-07

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 47.97  E-value: 2.43e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 922581144   1262 ISTPSDFMHIVHMGPAPVMelqQNFIDLQSNHSHTSSDK 1300
Cdd:smart00285    1 ISTPTNFKHIAHVGFDGQT---GGFTGLPTEWKSLLKTS 36
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-584 3.06e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   174 ELENEKAELVQKLKEAQTII-AQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLED-EALAQQQQKPKDEIVAESEKKL 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELeELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRRERLQQEIEELL 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   252 KELKERNKQLV-MEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLT---EKDSVKRLQDEAE---KA 324
Cdd:TIGR02168  428 KKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqaRLDSLERLQENLEgfsEG 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   325 KKQVADFEEKLKEIetekIALIKKQEEVTIEARKSVET------DDHLSEEVVAAKNTIASL------------------ 380
Cdd:TIGR02168  508 VKALLKNQSGLSGI----LGVLSELISVDEGYEAAIEAalggrlQAVVVENLNAAKKAIAFLkqnelgrvtflpldsikg 583

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   381 ---QATNEERETEI-----------------------------------------KKLKQRM------------------ 398
Cdd:TIGR02168  584 teiQGNDREILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnalelaKKLRPGYrivtldgdlvrpggvitg 663

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   399 -DEERASHTAQSEQEMKQLEAhyerAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLN-EQQLHEIFNWVSEEK 476
Cdd:TIGR02168  664 gSAKTNSSILERRREIEELEE----KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElSRQISALRKDLARLE 739

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   477 ATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQY 556
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          490       500
                   ....*....|....*....|....*...
gi 922581144   557 LTSAARLDDTEKRMASLMREVAMLKQQK 584
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQI 847
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 176-591 3.55e-07

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 54.58  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  176 ENEKAELVQKLKEAQTIIAqhvaenpRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQ---------QQQKPKDEIVAE 246
Cdd:COG5185   133 LKDELIKVEKLDEIADIEA-------SYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLtlgllkgisELKKAEPSGTVN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  247 SEKKLKELKERNKQLVMEKS-------EIQRELDNIND---HLDQVLVEKATVVQQRDDMqaELADVGDSllteKDSVKR 316
Cdd:COG5185   206 SIKESETGNLGSESTLLEKAkeiinieEALKGFQDPESeleDLAQTSDKLEKLVEQNTDL--RLEKLGEN----AESSKR 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  317 LQDEAEKAKKQVADFEEKLKEIE--TEKIALIKKQEEVTIEARKSVETDDHLSE---EVVAAKNTIASLQATNEERETEI 391
Cdd:COG5185   280 LNENANNLIKQFENTKEKIAEYTksIDIKKATESLEEQLAAAEAEQELEESKREtetGIQNLTAEIEQGQESLTENLEAI 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  392 KKLKQRMDEERAShtAQSEQEMKQLEAHYERA-QKMLQDNVEQMNVENRGLrdeiEKLSQQMaalprgGLNEQQLHEIFN 470
Cdd:COG5185   360 KEEIENIVGEVEL--SKSSEELDSFKDTIESTkESLDEIPQNQRGYAQEIL----ATLEDTL------KAADRQIEELQR 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  471 WVSEEKATREEMENLTRKITGE-VESLKNNSPLTTSNYIQNTpsgwgsRRMNNVARKDGLDLQRQLQAEIDAKLKLKAEL 549
Cdd:COG5185   428 QIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAY------DEINRSVRSKKEDLNEELTQIESRVSTLKATL 501

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 922581144  550 KNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSD 591
Cdd:COG5185   502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 674-726 3.77e-07

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 48.02  E-value: 3.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  674 RGHNFERMKikTPTKCGHCTSILIgldRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20816     1 QTHRFRRLR--TPSKCRECDSYVY---FNGAECEECGLACHKKCLETLAIQCG 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 174-418 3.81e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQhvaenpRSEEDRNYESTIAQLKDEIQILNKRLEdeALAQQQQKPKDEIvAESEKKLKE 253
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIR--ALEQELAALEAEL-AELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  254 LkernkqlvmekseiQRELDNINDHLDQVLVEKATVVQQRDDM----QAELADVGDSLLTEKDSVKRLQDEAEKAKKQVA 329
Cdd:COG4942    95 L--------------RAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  330 DFEEKLKEIETEKIALIKKQEEVTIEARKsvetddhLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQS 409
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233


                  ....*....
gi 922581144  410 EQEMKQLEA 418
Cdd:COG4942   234 AEAAAAAER 242
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 210-425 3.84e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  210 ESTIAQLKDEIQILNKRLEDealAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLD--QVLVEKA 287
Cdd:COG3883    15 DPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  288 TVVQQRDDMQAELADVgdsLLTEK------DSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEvtiearksve 361
Cdd:COG3883    92 ARALYRSGGSVSYLDV---LLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---------- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  362 tddhLSEEVVAAKNTIASLQATNEERETEIKKLKqrmdEERASHTAQSEQEMKQLEAHYERAQK 425
Cdd:COG3883   159 ----LEALKAELEAAKAELEAQQAEQEALLAQLS----AEEAAAEAQLAELEAELAAAEAAAAA 214
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 676-725 4.55e-07

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They 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 (C1), 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. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 47.68  E-value: 4.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIgldrQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20811     3 HNFVRKTFFTLAFCDVCRKLLF----QGFRCQTCGFKFHQRCSDQVPALC 48
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 175-599 4.87e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.59  E-value: 4.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   175 LENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYE------STIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESE 248
Cdd:TIGR00618  258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   249 KKLKELKERNKQLVMEKSEIQRELD---NINDHLDQVLVEKATVVQQRDDMQAeLADVGDSLLTEKDSVKRLQDEAEKAK 325
Cdd:TIGR00618  338 SSIEEQRRLLQTLHSQEIHIRDAHEvatSIREISCQQHTLTQHIHTLQQQKTT-LTQKLQSLCKELDILQREQATIDTRT 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   326 KQVADFEEKL----KEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNE--ERETEIKKLKqrmd 399
Cdd:TIGR00618  417 SAFRDLQGQLahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKKAVV---- 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   400 EERASHTAQSEQEMKQLEAHYErAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALprgglnEQQLHEIFNWVSEEKATR 479
Cdd:TIGR00618  493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV------YHQLTSERKQRASLKEQM 565

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   480 EEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDaKLKLKAELKNSQE----- 554
Cdd:TIGR00618  566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD-LQDVRLHLQQCSQelalk 644

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 922581144   555 -----QYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSDSAFSSTMG 599
Cdd:TIGR00618  645 ltalhALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTY 694
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 140-368 4.90e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   140 LSDARSLTDEIRAIAQRCQGDAELMEKSVDGF---MVELENEKAELVQKLKEAQTIIAQHVAENPRSE-EDRNYESTIAQ 215
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDLESRLGD 886

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   216 LKDEIQILNKRLEdealaqQQQKPKDEIVAESEKK---LKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKaTVVQQ 292
Cdd:TIGR02169  887 LKKERDELEAQLR------ELERKIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAE 959

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   293 RDDMQAELADVGDSLLtekdsvkRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKS-VETDDHLSE 368
Cdd:TIGR02169  960 LQRVEEEIRALEPVNM-------LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVfMEAFEAINE 1029
Pkinase_C pfam00433
Protein kinase C terminal domain;
90-134 5.13e-07

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 47.20  E-value: 5.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 922581144    90 VSSPEDTSNFDvdvceDDFT--PCETQPPRVLAAFTGNHLPFVGFSY 134
Cdd:pfam00433    1 VKSETDTSNFD-----PEFTeePPVLTPPDSSILSSNDQEEFRGFSY 42
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 676-728 5.32e-07

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 47.58  E-value: 5.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILiglDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVI---DSQGISCRVCKYACHKKCEAKVVTPCFPP 52
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 175-348 5.79e-07

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 51.45  E-value: 5.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   175 LENEKAELVQKLKEAQTIIAQHVAENPRSEEdrnyesTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKEL 254
Cdd:pfam13851   31 LKEEIAELKKKEERNEKLMSEIQQENKRLTE------PLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLEKELKDL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   255 KERNKQLVMEKSEIQRELDNINDHLDQVLVEkatvVQQRDDMQaeladvgdSLLTEKdSVKRLQDEAEKAKKQ------- 327
Cdd:pfam13851  105 KWEHEVLEQRFEKVERERDELYDKFEAAIQD----VQQKTGLK--------NLLLEK-KLQALGETLEKKEAQlnevlaa 171

                          170       180
                   ....*....|....*....|....*...
gi 922581144   328 -------VADFEEKLKEIETEKIALIKK 348
Cdd:pfam13851  172 anldpdaLQAVTEKLEDVLESKNQLIKD 199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
182-589 5.89e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  182 LVQKLKEAQTIIaqhvaENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQL 261
Cdd:COG4717    47 LLERLEKEADEL-----FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  262 vmekseiqreldnindhldQVLVEKATVVQQRDDMQAELADVG---DSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEI 338
Cdd:COG4717   122 -------------------EKLLQLLPLYQELEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEEL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  339 ETEKIALIKKQEEVTIEARksvetdDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEA 418
Cdd:COG4717   183 LEQLSLATEEELQDLAEEL------EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  419 ---------------------------------HYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQL 465
Cdd:COG4717   257 allallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  466 HEIFNWVSEEKATRE---EMENLTRKITGEVESLKNNSPLTTSNyiQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAK 542
Cdd:COG4717   337 EELLELLDRIEELQEllrEAEELEEELQLEELEQEIAALLAEAG--VEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  543 LKL------KAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQ-KNIENS 589
Cdd:COG4717   415 LGEleelleALDEEELEEELEELEEELEELEEELEELREELAELEAElEQLEED 468
C1_RASGRP3 cd20862
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 3 ...
 676-725 6.20e-07

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 3 (RASGRP3) and similar proteins; RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410412  Cd Length: 59  Bit Score: 47.72  E-value: 6.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20862     8 HNFQEMTYLKPTFCEHCAGFLWGIIKQGYKCKDCGVNCHKQCKDLLVLAC 57
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
 676-726 6.40e-07

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 47.32  E-value: 6.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSqSCP 726
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLRCKNCKMNVHHKCQEGVP-DCS 50
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 1260-1298 6.99e-07

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 47.05  E-value: 6.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 922581144 1260 IQISTPSDFMHIVHMGPAPVMELQQNFI-DLQSNHSHTSS 1298
Cdd:cd00132     1 MEISTPTDFKHISHVGWDGVGFDGANLPpDLQSLFQTAGI 40
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 205-522 7.16e-07

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 53.70  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  205 EDRNYESTIAQLKDEI---QILNKRLEDEALAQQQQKPKDEIVAESEKKLKE--LKERnkqLVMEKSEIQREldNINDHL 279
Cdd:PLN03229  430 PVRELEGEVEKLKEQIlkaKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmgLQER---LENLREEFSKA--NSQDQL 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  280 -DQVLVEKatVVQQRDDMQAELADVGD--------SLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIET-----EKIAL 345
Cdd:PLN03229  505 mHPVLMEK--IEKLKDEFNKRLSRAPNylslkyklDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDrpeikEKMEA 582

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  346 IKKQEEVTiEARKSVETDDHLSEEVVAAKNtiaslqatneERETEIKKLKQRMDEERASHTAqseqemKQLEAHYERAQK 425
Cdd:PLN03229  583 LKAEVASS-GASSGDELDDDLKEKVEKMKK----------EIELELAGVLKSMGLEVIGVTK------KNKDTAEQTPPP 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  426 MLQDNVEQMN----------VENRGLRDEIEKLSQQMAalpRGGLN------------EQQLHEIFNWVSEEKATREEME 483
Cdd:PLN03229  646 NLQEKIESLNeeinkkiervIRSSDLKSKIELLKLEVA---KASKTpdvtekekiealEQQIKQKIAEALNSSELKEKFE 722

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 922581144  484 NLTRKITGEVE-------SLKNNSPLttsnyiQNTPSGWGSRRMNN 522
Cdd:PLN03229  723 ELEAELAAAREtaaesngSLKNDDDK------EEDSKEDGSRVEVN 762
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 1-136 8.08e-07

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: 52.69  E-value: 8.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLICSSDVR---FGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05616   194 MLAGQAPFEGEDEDELFQSIMEHN--VAYPKS-----MSKEAVAICKGLMTKHPGKrlgCGPEGERDIKEHAFFRYIDWE 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   78 TI--RDSNPPYVPEVSSpEDTSNFDvdvceDDFT--PCETQPPRVLAAFTGNHLPFVGFSYTH 136
Cdd:cd05616   267 KLerKEIQPPYKPKACG-RNAENFD-----RFFTrhPPVLTPPDQEVIRNIDQSEFEGFSFVN 323
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
172-591 8.11e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  172 MVELENEKAELVQKLKEAQTIIAQHVAENpRSEEDRNYESTIAQLKDEIQilnkRLEDEALAQQQQKpkdeivAESEKKL 251
Cdd:COG4913   257 IRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELA----RLEAELERLEARL------DALREEL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  252 KELKE-RNKQLVMEKSEIQRELDNINDHLDQvlvekatVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEA----EKAKK 326
Cdd:COG4913   326 DELEAqIRGNGGDRLEQLEREIERLERELEE-------RERRRARLEALLAALGLPLPASAEEFAALRAEAaallEALEE 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  327 QVADFEEKLKEIETEKIALIKKQEEVT-----IEARKSVetddhLSEEVVAAKNTIAslQATNeERETEIK---KLKQ-R 397
Cdd:COG4913   399 ELEALEEALAEAEAALRDLRRELRELEaeiasLERRKSN-----IPARLLALRDALA--EALG-LDEAELPfvgELIEvR 470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  398 MDE-------ERASHT-AQSeqemkqL---EAHYERAQKmlqdNVEQMNVENR--GLRDEIEKLSQQMAALPRGGLNEQ- 463
Cdd:COG4913   471 PEEerwrgaiERVLGGfALT------LlvpPEHYAAALR----WVNRLHLRGRlvYERVRTGLPDPERPRLDPDSLAGKl 540

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  464 --QLHEIFNWVSEEKATR---------EEMENLTRKIT--------GEVESLKNNSPLTTSNYIqntpsGWgsrrmNNVA 524
Cdd:COG4913   541 dfKPHPFRAWLEAELGRRfdyvcvdspEELRRHPRAITragqvkgnGTRHEKDDRRRIRSRYVL-----GF-----DNRA 610

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581144  525 RKDGLDLQR-QLQAEIDAKLKLKAELKNSQEQY------LTSAARLDDTEKRMASLMREVAMLKQQK-NIENSSD 591
Cdd:COG4913   611 KLAALEAELaELEEELAEAEERLEALEAELDALqerreaLQRLAEYSWDEIDVASAEREIAELEAELeRLDASSD 685
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 266-447 9.27e-07

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 52.37  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  266 SEIQRELDNINDHLDQVLVEKAtvvqqRDDMQAELADvgdslltEKDSVKRLQDEAEKAKKQVADFEEKLkeiETEKIAL 345
Cdd:cd22656    94 AEILELIDDLADATDDEELEEA-----KKTIKALLDD-------LLKEAKKYQDKAAKVVDKLTDFENQT---EKDQTAL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  346 IKKQEEVtiearksvetDDHLSEEV-VAAKNTIASLQAT-NEERETEIKKLKQRMDEERAshtaqseqEMKQLEAHYERA 423
Cdd:cd22656   159 ETLEKAL----------KDLLTDEGgAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKA--------LIADDEAKLAAA 220

                         170       180
                  ....*....|....*....|....
gi 922581144  424 QKmLQDNVEQMNVENRGLRDEIEK 447
Cdd:cd22656   221 LR-LIADLTAADTDLDNLLALIGP 243
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
 675-726 1.06e-06

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 46.89  E-value: 1.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144  675 GHNFERMKIKTPTK--CGHCTSILIGLdRQGLF-CQSCQYACHVSCAERVSQSCP 726
Cdd:cd20819     5 GHHFVLQKSKSSSKqyCDKCCGIIWGL-LQTWYrCTDCGYRCHSKCLNSITRTCA 58
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 675-725 1.10e-06

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 46.88  E-value: 1.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLfCQSCQYACHVSCAERVSQSC 725
Cdd:cd20883     5 GHIFKSTQYSIPTYCEYCSSLIWMMDRAYV-CKLCRYACHKKCCLKTTTKC 54
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 169-588 1.13e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 53.30  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   169 DGFMVELENEKAELvqklkEAQTIIAQHVAEnprsEEDRNYESTIAQLKDEIQILNKRLED--EALAQQQQKPKDEIVAE 246
Cdd:pfam12128  350 PSWQSELENLEERL-----KALTGKHQDVTA----KYNRRRSKIKEQNNRDIAGIKDKLAKirEARDRQLAVAEDDLQAL 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   247 SEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRddMQAELADVGDSLLTEKD-SVKRLQDEAEKAK 325
Cdd:pfam12128  421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE--NFDERIERAREEQEAANaEVERLQSELRQAR 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   326 KQvadFEEKLKEIETEKIALIKKQ------EEVTIEARKSV-------------------------ETDDH--LSEEVVA 372
Cdd:pfam12128  499 KR---RDQASEALRQASRRLEERQsaldelELQLFPQAGTLlhflrkeapdweqsigkvispellhRTDLDpeVWDGSVG 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   373 AKNTIASLQ------------ATNEERETEIKKLKQRMDEERASHTAQSEQeMKQLEAHYERAQKML----------QDN 430
Cdd:pfam12128  576 GELNLYGVKldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ-LVQANGELEKASREEtfartalknaRLD 654

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   431 VEQMNVENRGLRDEIEKL---SQQMAALPRGGLNEQQ---LHEIFNWVSEEKATREEMENLTRKITGEVESlknnspltt 504
Cdd:pfam12128  655 LRRLFDEKQSEKDKKNKAlaeRKDSANERLNSLEAQLkqlDKKHQAWLEEQKEQKREARTEKQAYWQVVEG--------- 725

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   505 snyiqntpsgwgsrrmnnvARKDGLDlqrQLQAEIDA-KLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:pfam12128  726 -------------------ALDAQLA---LLKAAIAArRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERK 783


                   ....*
gi 922581144   584 knIEN 588
Cdd:pfam12128  784 --IER 786
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 172-418 1.16e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 53.01  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  172 MVELENEKAELVQKLKEAQTIiaqHVAENPRSEED---RNYESTIAQLKDEIQILNK-----RLEDEALAQQQQKPKDEI 243
Cdd:PRK05771   11 IVTLKSYKDEVLEALHELGVV---HIEDLKEELSNerlRKLRSLLTKLSEALDKLRSylpklNPLREEKKKVSVKSLEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 VAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATvvqqrddmqaelaDVGDSLLTEKDSVK----RLQD 319
Cdd:PRK05771   88 IKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNF-------------DLDLSLLLGFKYVSvfvgTVPE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  320 EAEKAKKQVADFeEKLKEIETEK-------IALIKKQEEVTIEARK------SVETDDHLSEEVVAAKNTIASLQATNEE 386
Cdd:PRK05771  155 DKLEELKLESDV-ENVEYISTDKgyvyvvvVVLKELSDEVEEELKKlgferlELEEEGTPSELIREIKEELEEIEKERES 233

                         250       260       270
                  ....*....|....*....|....*....|..
gi 922581144  387 RETEIKKLKQRMDEERASHTAQSEQEMKQLEA 418
Cdd:PRK05771  234 LLEELKELAKKYLEELLALYEYLEIELERAEA 265
46 PHA02562
endonuclease subunit; Provisional
 175-355 1.21e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 52.71  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  175 LENEKAELVQKLKEAQTIIAQHVaenprsEEDRNYESTIAQLKDEIQILNKRLED--EAL-----------AQQQQKPKD 241
Cdd:PHA02562  204 IEEQRKKNGENIARKQNKYDELV------EEAKTIKAEIEELTDELLNLVMDIEDpsAALnklntaaakikSKIEQFQKV 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  242 EIVAES-------EKKLKELKERNKQLVMEKSEIQRELDNINDHLDQV---LVEKATVVQQRDDMQAELADVGDSLLTEK 311
Cdd:PHA02562  278 IKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELeeiMDEFNEQSKKLLELKNKISTNKQSLITLV 357

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 922581144  312 DSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIE 355
Cdd:PHA02562  358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 174-364 1.24e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.46  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNY-ESTIAQLKDEIQILNKRLED--EALAQQ-------QQKPKDEI 243
Cdd:COG4942    45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAAlEAELAELEKEIAELRAELEAqkEELAELlralyrlGRQPPLAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 VAESE---------KKLKELKERNKQLVMEKSEIQRELDNINDHLDQvlvEKATVVQQRDDMQAELAdvgdSLLTEKDSV 314
Cdd:COG4942   125 LLSPEdfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEA---ERAELEALLAELEEERA----ALEALKAER 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  315 KRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDD 364
Cdd:COG4942   198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 174-357 1.26e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQHvaenprseedrnyESTIAQLKDEIQILNKRLEDealAQQQQKPKDEIVAESEKKLKE 253
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAEL-------------EDELAALEARLEAAKTELED---LEKEIKRLELEIEEVEARIKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  254 LKER------NKQ---LVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADvgdslltekdsvkrLQDEAEKA 324
Cdd:COG1579    78 YEEQlgnvrnNKEyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE--------------LEAELEEK 143

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 922581144  325 KKQvadFEEKLKEIETEKIALIKKQEEV--TIEAR 357
Cdd:COG1579   144 KAE---LDEELAELEAELEELEAEREELaaKIPPE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
315-585 1.30e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  315 KRLQDEAEKAKKQVADFEEKLKEIETEKialikKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQAtnEERETEIKKL 394
Cdd:COG4913   221 PDTFEAADALVEHFDDLERAHEALEDAR-----EQIELLEPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  395 KQRMDEERASHtAQSEQEMKQLEAHYERAQKMLQDNVEQMNvENRGlrDEIEKLSQQMAALprgglnEQQLHEIfnwvse 474
Cdd:COG4913   294 EAELEELRAEL-ARLEAELERLEARLDALREELDELEAQIR-GNGG--DRLEQLEREIERL------ERELEER------ 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  475 eKATREEMENLTRKITGEVESlknnsplttsnyiqntpsgwgsrrmnnvARKDGLDLQRQLQAEIDAklkLKAELKNSQE 554
Cdd:COG4913   358 -ERRRARLEALLAALGLPLPA----------------------------SAEEFAALRAEAAALLEA---LEEELEALEE 405

                         250       260       270
                  ....*....|....*....|....*....|.
gi 922581144  555 QYLTSAARLDDTEKRMASLMREVAMLKQQKN 585
Cdd:COG4913   406 ALAEAEAALRDLRRELRELEAEIASLERRKS 436
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
270-507 1.36e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  270 RELDNINDHL-DQVLVEKATvvqqrddmqaeLADVgDSLLTEKDSVKRLQDEAEKAKKQVadfeEKLKEIETEKIALIKK 348
Cdd:COG4913   204 KPIGDLDDFVrEYMLEEPDT-----------FEAA-DALVEHFDDLERAHEALEDAREQI----ELLEPIRELAERYAAA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  349 QEEV-TIEARKS-------VETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHY 420
Cdd:COG4913   268 RERLaELEYLRAalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  421 ERAQK----------MLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGlnEQQLHEIFNWVSEEKATREEMENLTRKIT 490
Cdd:COG4913   348 ERLEReleererrraRLEALLAALGLPLPASAEEFAALRAEAAALLEAL--EEELEALEEALAEAEAALRDLRRELRELE 425

                         250
                  ....*....|....*..
gi 922581144  491 GEVESLKNNSplttSNY 507
Cdd:COG4913   426 AEIASLERRK----SNI 438
PRK12704 PRK12704
phosphodiesterase; Provisional
 230-427 1.55e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  230 EALAQQQQKPKDEIVAESEKKLKELKERnkqlvmEKSEIQRELDNINDHLDQVLVEKATVVQQRDdmqaeladvgdsllt 309
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKE------ALLEAKEEIHKLRNEFEKELRERRNELQKLE--------------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  310 ekdsvKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEvtIEARKsvETDDHLSEEVVAAKNTIASLQAtNEERET 389
Cdd:PRK12704   89 -----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE--LEKKE--EELEELIEEQLQELERISGLTA-EEAKEI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 922581144  390 EIKKLKQRMDEERASHTAQSEQEMKQlEAHyERAQKML 427
Cdd:PRK12704  159 LLEKVEEEARHEAAVLIKEIEEEAKE-EAD-KKAKEIL 194
C1_DGKgamma_rpt1 cd20846
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 670-725 1.63e-06

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DGK-gamma contains two copies of the C1 domain. This model corresponds to the first one. DGK-gamma contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410396  Cd Length: 73  Bit Score: 46.85  E-value: 1.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  670 SAMERGHNFERMK-IKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20846    10 NVKDDGQHAWRLKhFKKPAYCNFCHTMLLGVRKQGLCCSFCKYTVHERCVSKDIASC 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 213-372 1.75e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  213 IAQLKDEIQILNKRLED--EALAQQQQKpkdeiVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHL--DQVLVEKAT 288
Cdd:COG1579    12 LQELDSELDRLEHRLKElpAELAELEDE-----LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  289 VVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSE 368
Cdd:COG1579    87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166


                  ....
gi 922581144  369 EVVA 372
Cdd:COG1579   167 ELAA 170
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 675-726 1.78e-06

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 46.69  E-value: 1.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGL-DRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20835     9 GHKFMATYLRQPTYCSHCKDFIWGViGKQGYQCQVCTCVVHKRCHQLVVTKCP 61
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 152-545 1.84e-06

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 52.45  E-value: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   152 AIAQRcqgDAELMEKSVDGFMVELEnEKAELVQKLKeaQTIIAQHVAENPRSE----------------EDR-NYESTIA 214
Cdd:pfam07111  193 AEAQK---EAELLRKQLSKTQEELE-AQVTLVESLR--KYVGEQVPPEVHSQTwelerqelldtmqhlqEDRaDLQATVE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   215 QLKDEIQILNK--RLEDEALAQQQQkPKDEIVAESEKKLKELKERNKQ-----LVMEKSEIQRELDNINDHLDQV--LVE 285
Cdd:pfam07111  267 LLQVRVQSLTHmlALQEEELTRKIQ-PSDSLEPEFPKKCRSLLNRWREkvfalMVQLKAQDLEHRDSVKQLRGQVaeLQE 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   286 KATV-VQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKA-------KKQVADFEEKLK----EIETEKIALIKKQEEVT 353
Cdd:pfam07111  346 QVTSqSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAqearrrqQQQTASAEEQLKfvvnAMSSTQIWLETTMTRVE 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   354 IEARKSVETDDHLSEEV---------VAAKNTIASLQA-----------TNEERETEIKKLKQ---RMDEE--------- 401
Cdd:pfam07111  426 QAVARIPSLSNRLSYAVrkvhtikglMARKVALAQLRQescpppppappVDADLSLELEQLREernRLDAElqlsahliq 505

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   402 ----RASHTAQSEQEM-----KQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKlsqqmAALPRGGLNEQQlhEIFNWV 472
Cdd:pfam07111  506 qevgRAREQGEAERQQlsevaQQLEQELQRAQESLASVGQQLEVARQGQQESTEE-----AASLRQELTQQQ--EIYGQA 578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   473 SEEKAT------REEMENLTRKI-------TGEVESLKNNSPLTTSNYIQNTPsgwgSRRMNNVARK-DGLDLQRQLQA- 537
Cdd:pfam07111  579 LQEKVAevetrlREQLSDTKRRLnearreqAKAVVSLRQIQHRATQEKERNQE----LRRLQDEARKeEGQRLARRVQEl 654


                   ....*...
gi 922581144   538 EIDAKLKL 545
Cdd:pfam07111  655 ERDKNLML 662
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 676-718 1.85e-06

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 46.09  E-value: 1.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCA 718
Cdd:cd20830     1 HRFVEQSFSTLQWCDKCGKFLFGLVHQGLQCQDCGLVCHRTCA 43
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 149-570 1.95e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.66  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   149 EIRAIAQRCQGDAELMEKSVdgfMVELENEKAELVQKLKEAQTI-------------IAQHVAENPR----SEEDRNYES 211
Cdd:TIGR00618  441 ELCAAAITCTAQCEKLEKIH---LQESAQSLKEREQQLQTKEQIhlqetrkkavvlaRLLELQEEPCplcgSCIHPNPAR 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   212 TIAQLKDEIQILNKRLEDE-ALAQQQQKPKDEIVAESEKKLKELKERnkqlvmEKSEIQRELdnINDHLDQVLVEKATVV 290
Cdd:TIGR00618  518 QDIDNPGPLTRRMQRGEQTyAQLETSEEDVYHQLTSERKQRASLKEQ------MQEIQQSFS--ILTQCDNRSKEDIPNL 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   291 QQRDDmqaELADVGDSLLTEKDSvKRLQDEAEKAKKQVA-----------DFEEKL---------------KEIETEKIA 344
Cdd:TIGR00618  590 QNITV---RLQDLTEKLSEAEDM-LACEQHALLRKLQPEqdlqdvrlhlqQCSQELalkltalhalqltltQERVREHAL 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   345 LIKKQEEVTIEARKSVETD-DHLSEEVVAAKNTIASLQATNEERETEIKKL-KQRMDEERASHTAQSEqemkqLEAHYER 422
Cdd:TIGR00618  666 SIRVLPKELLASRQLALQKmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASSSLGSD-----LAAREDA 740

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   423 AQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLheifnwvseekatREEMENLTRKITGEVESLKnnspL 502
Cdd:TIGR00618  741 LNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL-------------AAEIQFFNRLREEDTHLLK----T 803

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   503 TTSNYIQNTPSGWGSR---------RMNNVARKdgLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRM 570
Cdd:TIGR00618  804 LEAEIGQEIPSDEDILnlqcetlvqEEEQFLSR--LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 686-725 1.96e-06

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 46.16  E-value: 1.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 922581144  686 PTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20800    15 PTYCNVCREALSGVTSHGLSCEVCKFKAHKRCAVKAPNNC 54
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 674-728 2.05e-06

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 45.86  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144  674 RGHNFERMKIKTPTKCGHCtSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20821     1 RPHRFVSKTVIKPETCVVC-GKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPT 54
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 165-552 2.11e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.28  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   165 EKSVDGFMVELENEKAELVQKLKEA-QTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEI 243
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   244 VAESEKKLKELKERNKQLVMEKSEIQREL-----DNINDHLDQVLVEKATVVQQR----DDMQAELADVGDSLLTEKDSV 314
Cdd:TIGR00618  624 EQDLQDVRLHLQQCSQELALKLTALHALQltltqERVREHALSIRVLPKELLASRqlalQKMQSEKEQLTYWKEMLAQCQ 703

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   315 KRLQDEAEKAKKQVADFEE-------KLKEIETEKIALIKKQEEVTIEAR----KSVETDDHLSEEVVAAKNTIASLQAT 383
Cdd:TIGR00618  704 TLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARtvlkARTEAHFNNNEEVTAALQTGAELSHL 783

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   384 NEERETeikklKQRMDEERASHTAQSEQEMKQLEAHYERAqkmlqdnveqMNVENRGLRDEIEKLSQQMAAlprgglNEQ 463
Cdd:TIGR00618  784 AAEIQF-----FNRLREEDTHLLKTLEAEIGQEIPSDEDI----------LNLQCETLVQEEEQFLSRLEE------KSA 842

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   464 QLHEIFNWVSEEKATREEMENLTRKITGEVESLKNnspLTTSNYIQNTPSGWgsrRMNNVARKDGLDLQRQLQAEIDAKL 543
Cdd:TIGR00618  843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK---LNGINQIKIQFDGD---ALIKFLHEITLYANVRLANQSEGRF 916


                   ....*....
gi 922581144   544 KLKAELKNS 552
Cdd:TIGR00618  917 HGRYADSHV 925
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 2-77 2.28e-06

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: 50.69  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    2 LYGTTPFYSERLVD--TYGKIMSHQDMLDFPDdeidwVVSEEAKDLIRQLICSSD-VRFG--RNGLSDFQLHPFFEGIDW 76
Cdd:cd05572   186 LTGRPPFGGDDEDPmkIYNIILKGIDKIEFPK-----YIDKNAKNLIKQLLRRNPeERLGylKGGIRDIKKHKWFEGFDW 260


                  .
gi 922581144   77 N 77
Cdd:cd05572   261 E 261
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
 674-728 2.38e-06

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 45.93  E-value: 2.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20797     2 RPHVVEVEQYMTPTFCDYCGEMLTGLMKQGVKCKNCRCNFHKRCANAPRNNCAAA 56
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 173-447 2.78e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   173 VELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLK 252
Cdd:pfam02463  778 EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   253 ELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVgDSLLTEKDSVKRLQDEAEKAKKQvaDFE 332
Cdd:pfam02463  858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK-LNLLEEKENEIEERIKEEAEILL--KYE 934

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   333 EKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASH-TAQSEQ 411
Cdd:pfam02463  935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLiRAIIEE 1014

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 922581144   412 EMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEK 447
Cdd:pfam02463 1015 TCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRL 1050
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 200-592 2.98e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   200 NPRSEEDRNYESTIAQLKDEIqiLNKRLEDEALaQQQQKPKDEIVAESEKKLKELKER----NKQLVMEK---------- 265
Cdd:TIGR04523   29 NKQDTEEKQLEKKLKTIKNEL--KNKEKELKNL-DKNLNKDEEKINNSNNKIKILEQQikdlNDKLKKNKdkinklnsdl 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   266 SEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKial 345
Cdd:TIGR04523  106 SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK--- 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   346 IKKQEEVtiearksvetdDHLSEEVVAAKNTIASLQATNE---ERETEIKKLKQRmdeerashtaqseqemkqleahyer 422
Cdd:TIGR04523  183 LNIQKNI-----------DKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQ------------------------- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   423 aQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALprggLNEQ-----QLHEIFNWVSEEKATREEMENLTRKITGEVESLK 497
Cdd:TIGR04523  227 -NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL----KDEQnkikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   498 NnsplttsnyiqntpsgwgsrrmnnvarkdgldlqrqlQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREV 577
Cdd:TIGR04523  302 N-------------------------------------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344

                          410
                   ....*....|....*
gi 922581144   578 AMLKQQKNIENSSDS 592
Cdd:TIGR04523  345 SQLKKELTNSESENS 359
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 747-870 3.00e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 47.16  E-value: 3.00e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    747 YEGLVKTpRAGGVRKGWQTAYVVVCDFKLYLYDctvdrqNKMQDVKNEIRLVLDMRDpdftvCGVSEADviHAQKGDIPK 826
Cdd:smart00233    3 KEGWLYK-KSGGGKKSWKKRYFVLFNSTLLYYK------SKKDKKSYKPKGSIDLSG-----CTVREAP--DPDSSKKPH 68

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 922581144    827 IFRVTTTQilnssseyssSSKFYtlFMAETEEEKRKWVVALSEL 870
Cdd:smart00233   69 CFEIKTSD----------RKTLL--LQAESEEEREKWVEALRKA 100
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
174-360 3.14e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRnyeSTIAQLKDEIQILNKRLEDEALAQQQQKpkdEIVA-------- 245
Cdd:COG1340    75 ELKEERDELNEKLNELREELDELRKELAELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEK---ELVEkikeleke 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  246 --------ESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRL 317
Cdd:COG1340   149 lekakkalEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 922581144  318 QDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSV 360
Cdd:COG1340   229 HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
 673-725 3.27e-06

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410395  Cd Length: 66  Bit Score: 46.00  E-value: 3.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  673 ERGHNFERMK-IKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20845     4 DDGQHVWRLKhFNKPAYCNLCLNMLVGLGKQGLCCSFCKYTVHERCVQRAPASC 57
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 1-51 3.54e-06

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: 50.17  E-value: 3.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDEidW-VVSEEAKDLIRQLIC 51
Cdd:cd05117   194 LLCGYPPFYGETEQELFEKILKGK--YSFDSPE--WkNVSEEAKDLIKRLLV 241
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 747-867 4.84e-06

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 46.00  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  747 YEG-LVKtpRAGGVRKGWQTAYVVVCDFKLYLYDctvdrqnKMQDVKNEIRLVLDMRDpdftvcgvsEADVIHAQKGDIP 825
Cdd:cd00821     1 KEGyLLK--RGGGGLKSWKKRWFVLFEGVLLYYK-------SKKDSSYKPKGSIPLSG---------ILEVEEVSPKERP 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 922581144  826 KIFRVTTTQilnssseyssSSKFYtlFMAETEEEKRKWVVAL 867
Cdd:cd00821    63 HCFELVTPD----------GRTYY--LQADSEEERQEWLKAL 92
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
174-477 4.93e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 4.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIAQhvAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKE 253
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQ--LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  254 LKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDS-----VKRLQDEAEK-AKKQ 327
Cdd:COG4372   120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqaLDELLKEANRnAEKE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  328 VADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTA 407
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  408 QSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKA 477
Cdd:COG4372   280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 248-397 5.69e-06

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 50.02  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   248 EKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEkatVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQ 327
Cdd:pfam04849  170 QEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSD---CVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQ 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   328 VADFEEKLKEIETEKialikkqEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQR 397
Cdd:pfam04849  247 IVDLQHKCKELGIEN-------EELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
PRK12704 PRK12704
phosphodiesterase; Provisional
 184-372 6.89e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.16  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  184 QKLKEAQTIiAQHVAENPRSEEDRNYESTIAQLKDEIQILnkrledealaqqqqkpKDEIVAESEKKLKELKERNKQLVM 263
Cdd:PRK12704   31 AKIKEAEEE-AKRILEEAKKEAEAIKKEALLEAKEEIHKL----------------RNEFEKELRERRNELQKLEKRLLQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  264 EKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVgDSLLTEKdsVKRLQD----EAEKAKKQVadFEEKLKEIE 339
Cdd:PRK12704   94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQ--LQELERisglTAEEAKEIL--LEKVEEEAR 168

                         170       180       190
                  ....*....|....*....|....*....|...
gi 922581144  340 TEKIALIKKQEEvtiEARksvETDDHLSEEVVA 372
Cdd:PRK12704  169 HEAAVLIKEIEE---EAK---EEADKKAKEILA 195
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
 676-725 7.54e-06

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410410  Cd Length: 55  Bit Score: 44.54  E-value: 7.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20860     3 HNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFEC 52
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 237-425 7.78e-06

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 50.41  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   237 QKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEkatvVQQRDDMQAELADvgdSLLTEKDSVKR 316
Cdd:pfam05667  323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE----LEELKEQNEELEK---QYKVKKKTLDL 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   317 LQDEAE---KAKKQVADFEEKLKEIETE----KIALIKKQEEvtiearksvetddhLSEevvaakntiaslQATNEERET 389
Cdd:pfam05667  396 LPDAEEniaKLQALVDASAQRLVELAGQwekhRVPLIEEYRA--------------LKE------------AKSNKEDES 449

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 922581144   390 -----EIKKLKQRMdEERASHTAQSEQEMKQLEAHYERAQK 425
Cdd:pfam05667  450 qrkleEIKELREKI-KEVAEEAKQKEELYKQLVAEYERLPK 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
140-489 9.10e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  140 LSDARSLTDEIRAIAQRCQGDAELMEKSVDGF-----MVELENEKAELVQKLKEAQtiiAQHVAENPRSEEDRNYESTIA 214
Cdd:COG4717    97 LEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELE---ERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  215 QLKDEIQILNKRLEDEALAQQQQKPKDeiVAESEKKLKELKERNKQLVMEKSEIQRELDNIND---------HLDQVLV- 284
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEE--LEELQQRLAELEEELEEAQEELEELEEELEQLENeleaaaleeRLKEARLl 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  285 --------------------------------------------EKATVVQQRDDMQAE--------------LADVGDS 306
Cdd:COG4717   252 lliaaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALpaleeleeeeleelLAALGLP 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  307 LLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIalikKQEEVTIEARKSVETDDHLSEevvaakntIASLQATNEE 386
Cdd:COG4717   332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEEL----EQEIAALLAEAGVEDEEELRA--------ALEQAEEYQE 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  387 RETEIKKLKQRMDEERASHTAQSEQEMK-QLEAHYERAQKMLQDNVEQMNVenrgLRDEIEKLSQQMAALPRGGLNEQQL 465
Cdd:COG4717   400 LKEELEELEEQLEELLGELEELLEALDEeELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELL 475

                         410       420
                  ....*....|....*....|....
gi 922581144  466 HEIfnwvsEEKatREEMENLTRKI 489
Cdd:COG4717   476 QEL-----EEL--KAELRELAEEW 492
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 675-725 1.07e-05

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 43.79  E-value: 1.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVsQSC 725
Cdd:cd20810     2 GHSFELTTFKEPTTCSVCKKLLKGLFFQGYKCSVCGAAVHKECIAKV-KRC 51
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 282-418 1.15e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.07  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   282 VLVEKATVVQQRDDMQAELADVGDSlltEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIA-LIKKQEEvtiEARKSV 360
Cdd:TIGR02794   41 VLVDPGAVAQQANRIQQQKKPAAKK---EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAeKAAKQAE---QAAKQA 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   361 ETDDHLSEEvvaAKNTIASLQATNEERETEIKKLK--QRMDEERASHTAQSEQEMKQLEA 418
Cdd:TIGR02794  115 EEKQKQAEE---AKAKQAAEAKAKAEAEAERKAKEeaAKQAEEEAKAKAAAEAKKKAEEA 171
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
 676-726 1.55e-05

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 43.45  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20806     2 HNFKVHTFKGPHWCDYCGNFMWGLIAQGVKCEDCGFNAHKQCSKLVPHDCQ 52
46 PHA02562
endonuclease subunit; Provisional
 250-451 1.72e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  250 KLKELKERNKQLVMEKSEIQRELDNINDHLDQvlVEKATvvqqrDDMQAELADVGDSLLTEKDSVK----RLQDEAEKAK 325
Cdd:PHA02562  175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEE--QRKKN-----GENIARKQNKYDELVEEAKTIKaeieELTDELLNLV 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  326 KQVADFEEKLKEIETEKIALIKKQEEVTIEArKSVETDDH-------LSEE---VVAAKNTIASLQATNEERETEIKKLK 395
Cdd:PHA02562  248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-KMYEKGGVcptctqqISEGpdrITKIKDKLKELQHSLEKLDTAIDELE 326

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922581144  396 QRMDEERASHTAQSE-----QEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQ 451
Cdd:PHA02562  327 EIMDEFNEQSKKLLElknkiSTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
C1_Stac1 cd20880
protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich ...
 674-723 1.85e-05

protein kinase C conserved region 1 (C1 domain) found in SH3 and cysteine-rich domain-containing protein (Stac1) and similar proteins; Stac1, also called Src homology 3 and cysteine-rich domain-containing protein, promotes expression of the ion channel CACNA1H at the cell membrane, and thereby contributes to the regulation of channel activity. It plays a minor and redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. It slows down the inactivation rate of the calcium channel CACNA1C. Stac1 contains a cysteine-rich C1 domain and two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410430  Cd Length: 57  Bit Score: 43.39  E-value: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLD-RQGLFCQSCQYACHVSCAERVSQ 723
Cdd:cd20880     1 KAHSFQEYIFKKPTFCDVCNHMIVGTNaKHGLRCKACKMSIHHKCTDGIGQ 51
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 61-134 2.07e-05

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: 48.19  E-value: 2.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   61 GLSDFQLHPFFEGIDWNTI--RDSNPPYVPEVSSPEDTSNFDVDVCED--DFTPCEtqpPRVLAAFtgNHLPFVGFSY 134
Cdd:cd05588   255 GFADIQSHPFFRTIDWEQLeqKQVTPPYKPRIESERDLENFDPQFTNEpvQLTPDD---PDVIEKI--DQSEFEGFEY 327
PTZ00121 PTZ00121
MAEBL; Provisional
 223-587 2.28e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  223 LNKRLEDEALAQQQQKPKDEIVAESEKKLKELK---------ERNKQLVMEKSEIQRELDNINDHLDQVLVEKATvvQQR 293
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKktetgkaeeARKAEEAKKKAEDARKAEEARKAEDARKAEEAR--KAE 1149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  294 DDMQAELADVGDSllTEKDSVKRLQDEAEKAkkqvadfEEKLKEIETEKIALIKKQEEV-TIEARKSVETDDHLSEevva 372
Cdd:PTZ00121 1150 DAKRVEIARKAED--ARKAEEARKAEDAKKA-------EAARKAEEVRKAEELRKAEDArKAEAARKAEEERKAEE---- 1216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  373 akntiaSLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQM 452
Cdd:PTZ00121 1217 ------ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  453 AALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPlttsnyiqntpsgwGSRRMNNVARKDGLDLQ 532
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE--------------EAKKAAEAAKAEAEAAA 1356

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144  533 RQLQAeidAKLKLKA-ELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIE 587
Cdd:PTZ00121 1357 DEAEA---AEEKAEAaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
 674-732 2.29e-05

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 43.88  E-value: 2.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEER 732
Cdd:cd20841     9 RPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRR 67
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 225-583 2.68e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.80  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  225 KRLEDEAL-AQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVL---------------VEKAT 288
Cdd:COG3096   281 RELSERALeLRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalrqqekieryqedLEELT 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  289 VvqqRDDMQAE-LADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALikkQEEVTI--EARKSVETDDh 365
Cdd:COG3096   361 E---RLEEQEEvVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQY---QQAVQAleKARALCGLPD- 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  366 LSEEvvAAKNTIASLQATNEERETEIKKLKQRMDEERASHtAQSEQEMKQL---------EAHYERAQKMLQDNVEQMNV 436
Cdd:COG3096   434 LTPE--NAEDYLAAFRAKEQQATEEVLELEQKLSVADAAR-RQFEKAYELVckiageverSQAWQTARELLRRYRSQQAL 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  437 ENR--GLRDEIEKLSQQMAALPRGglnEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLknnsplttsnyiQNTPSG 514
Cdd:COG3096   511 AQRlqQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL------------EEQAAE 575

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144  515 WGSRRMNNVARKDGLD-LQRQLQAEIDAKLKLKAELKNSQEQY---LTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:COG3096   576 AVEQRSELRQQLEQLRaRIKELAARAPAWLAAQDALERLREQSgeaLADSQEVTAAMQQLLEREREATVERDE 648
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 674-732 2.86e-05

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 43.51  E-value: 2.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEER 732
Cdd:cd20840     9 RPHALNVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARKRR 67
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
311-567 3.38e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  311 KDSVKRLQDEAEKA----KKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETD--DHLSEEVVAAKNTIASLQATN 384
Cdd:COG3206   163 EQNLELRREEARKAleflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQqlSELESQLAEARAELAEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  385 EERETEIKKLKQRMDEERASHTAQS-EQEMKQLEAHYERAQKMLQDNVEQMnvenRGLRDEIEKLSQQMAALPRGGLNEQ 463
Cdd:COG3206   243 AALRAQLGSGPDALPELLQSPVIQQlRAQLAELEAELAELSARYTPNHPDV----IALRAQIAALRAQLQQEAQRILASL 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  464 QlheifnwvseekATREEMENLTRKITGEVESLKNNsplttsnyIQNTPsgwgsrrmnnvarkdglDLQRQLQAeidakl 543
Cdd:COG3206   319 E------------AELEALQAREASLQAQLAQLEAR--------LAELP-----------------ELEAELRR------ 355

                         250       260
                  ....*....|....*....|....
gi 922581144  544 kLKAELKNSQEQYLTSAARLDDTE 567
Cdd:COG3206   356 -LEREVEVARELYESLLQRLEEAR 378
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 178-458 3.51e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  178 EKAELVQKLKEAQTiiaqhvAENPRSEEdrnyesTIAQLKDEIQILNKRLEDEALAQQQQKPKDE---IVAESEKKLKEL 254
Cdd:PRK10929   24 DEKQITQELEQAKA------AKTPAQAE------IVEALQSALNWLEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  255 KERNKQL--VMEKSEIQRELDNINDHLdqvlVEKATVVQQRDDMQAELAdvgdslltekDSVKRLQDEAEKAKKQVADFE 332
Cdd:PRK10929   92 RDEPRSVppNMSTDALEQEILQVSSQL----LEKSRQAQQEQDRAREIS----------DSLSQLPQQQTEARRQLNEIE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  333 EKLKEIETEKIALIKKQeevtiearksvetddhlseevvaakntIASLQAtneeretEIKKLKQRMDE-ERASHTAQSEQ 411
Cdd:PRK10929  158 RRLQTLGTPNTPLAQAQ---------------------------LTALQA-------ESAALKALVDElELAQLSANNRQ 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  412 EMKQLEA-----HYERAQKMLQDNVEQMNVEnRGLRDEI-----EKLSQQMAALPRG 458
Cdd:PRK10929  204 ELARLRSelakkRSQQLDAYLQALRNQLNSQ-RQREAERalestELLAEQSGDLPKS 259
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
 676-728 3.57e-05

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, 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 (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 42.62  E-value: 3.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  676 HNFERMKIKTPTKCGHCtSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20814     5 HRFTTGLNMRATKCAVC-LDGVPFGRQASKCSECGIVCHPKCSSSLPNTCGLP 56
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-457 3.63e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  175 LENEKA-ELVQKLKEAQTI------IAQHVAENPRSEEDrnyestIAQLKDEIQILNkRLEDEALAQQQQKpkdeivaes 247
Cdd:COG4913   188 IGSEKAlRLLHKTQSFKPIgdlddfVREYMLEEPDTFEA------ADALVEHFDDLE-RAHEALEDAREQI--------- 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  248 eKKLKELKERNKQLVmeksEIQRELDNINDHLDQVLVEKAtvVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQ 327
Cdd:COG4913   252 -ELLEPIRELAERYA----AARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREE 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  328 VADFEEKLKEIETEKIALIKKQeevtIEARKsvETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTA 407
Cdd:COG4913   325 LDELEAQIRGNGGDRLEQLERE----IERLE--RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  408 QSEQEMKQL-EAHYERAQkmLQDNVEQmnvenrgLRDEIEKLSQQMAALPR 457
Cdd:COG4913   399 ELEALEEALaEAEAALRD--LRRELRE-------LEAEIASLERRKSNIPA 440
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 290-633 3.68e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   290 VQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKiALIKKQEEVTIEARKSVETDDHLSEE 369
Cdd:TIGR00606  185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSK 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   370 VVAAKNTIASLQATNEERETEIKKLKQRMDEERAShtaqSEQEMKQLEAH-------YERAQKMLQDNVEQMNVENRGLR 442
Cdd:TIGR00606  264 IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG----TDEQLNDLYHNhqrtvreKERELVDCQRELEKLNKERRLLN 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   443 DEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVEsLKNNSPLTTSNyiQNTPSGWGSRRMNN 522
Cdd:TIGR00606  340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQ-IKNFHTLVIER--QEDEAKTAAQLCAD 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   523 VA---------------RKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLT-SAARLDDTEKRMASLMREVAMLKQQKNI 586
Cdd:TIGR00606  417 LQskerlkqeqadeirdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgSSDRILELDQELRKAERELSKAEKNSLT 496

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 922581144   587 ENSSDSAFSSTMGRGDLMISM------NNDYEMSNSSLMRQEMISRQSTPSYE 633
Cdd:TIGR00606  497 ETLKKEVKSLQNEKADLDRKLrkldqeMEQLNHHTTTRTQMEMLTKDKMDKDE 549
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 675-726 3.92e-05

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 42.33  E-value: 3.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIG-LDRQGLFCQSCQYACHVSCAERVSQSCP 726
Cdd:cd20831     5 DHTFVATHFKGGPSCAVCNKLIPGrFGKQGYQCRDCGLICHKRCHVKVETHCP 57
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 178-497 4.13e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.89  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   178 EKAELVQKLKEAqtiiaqhvaenpRSEEDRNYESTIAQLKDEiqilNKRLEDEALAQQQQKpkdeivAESEKKLKELKER 257
Cdd:pfam10174  447 EKERIIERLKEQ------------REREDRERLEELESLKKE----NKDLKEKVSALQPEL------TEKESSLIDLKEH 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   258 NKQLV---MEKSEIQRELD-NINDHLDQV--LVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADF 331
Cdd:pfam10174  505 ASSLAssgLKKDSKLKSLEiAVEQKKEECskLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   332 EEKLKEIETEKIALIKKQEEV----------------------TIEARKSV-ETDDHLSEEVVAAKNtiaSLQATNEERE 388
Cdd:pfam10174  585 LGILREVENEKNDKDKKIAELesltlrqmkeqnkkvanikhgqQEMKKKGAqLLEEARRREDNLADN---SQQLQLEELM 661

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   389 TEIKKLKQRMDEERAsHTAQSEQEMKQLEAHyeraqkmlqdnVEQMNVENRGLRDEIEKLSQQ--MAALPRGGLNEQQLh 466
Cdd:pfam10174  662 GALEKTRQELDATKA-RLSSTQQSLAEKDGH-----------LTNLRAERRKQLEEILEMKQEalLAAISEKDANIALL- 728

                          330       340       350
                   ....*....|....*....|....*....|.
gi 922581144   467 EIFNwvSEEKATREEMENLTRKITGEVESLK 497
Cdd:pfam10174  729 ELSS--SKKKKTQEEVMALKREKDRLVHQLK 757
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 1-135 4.14e-05

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: 47.31  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLICSSDVRF---GRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05595   188 MMCGRLPFYNQDHERLFELILMEE--IRFPRT-----LSPEAKSLLAGLLKKDPKQRlggGPSDAKEVMEHRFFLSINWQ 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   78 TI--RDSNPPYVPEVSSPEDTSNFDvdvceDDFTPCE---TQPPR-----VLAAFTGNHLPfvGFSYT 135
Cdd:cd05595   261 DVvqKKLLPPFKPQVTSEVDTRYFD-----DEFTAQSitiTPPDRydsldLLESDQRTHFP--QFSYS 321
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 136-585 4.26e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.04  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   136 HGSLLSDARSLTDEIraIAQRCQGDAELMEKSV-------DGFMVELENEKAELVQKLKEAQ--TIIAQHVAENPRS-EE 205
Cdd:TIGR00618  117 RGRILAAKKSETEEV--IHDLLKLDYKTFTRVVllpqgefAQFLKAKSKEKKELLMNLFPLDqyTQLALMEFAKKKSlHG 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   206 DRNYESTIAQL------------KDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQR--- 270
Cdd:TIGR00618  195 KAELLTLRSQLltlctpcmpdtyHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEElra 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   271 ---ELDNINDHLDQ------VLVEKATVVQQRDDMQAELADvgdsLLTEKDSVKRLQDEAEKAKKQVADFEEKLK----- 336
Cdd:TIGR00618  275 qeaVLEETQERINRarkaapLAAHIKAVTQIEQQAQRIHTE----LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqtl 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   337 -------EIETEKIALIKKQEEVTIEARKSV-------ETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEER 402
Cdd:TIGR00618  351 hsqeihiRDAHEVATSIREISCQQHTLTQHIhtlqqqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   403 ASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRgLRDEIEKLSQQmaalprgglneQQLHEifnWVSEEKATREEM 482
Cdd:TIGR00618  431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS-LKEREQQLQTK-----------EQIHL---QETRKKAVVLAR 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   483 ENLTRKITGEVEslknnsplttsnyiqntpsgwGSRRMNNVARKDGLD---LQRQLQAEIDAKLKLKAELKNSQEQYLTS 559
Cdd:TIGR00618  496 LLELQEEPCPLC---------------------GSCIHPNPARQDIDNpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554

                          490       500
                   ....*....|....*....|....*.
gi 922581144   560 AARLDDTEKRMASLMREVAMLKQQKN 585
Cdd:TIGR00618  555 RKQRASLKEQMQEIQQSFSILTQCDN 580
46 PHA02562
endonuclease subunit; Provisional
 181-430 4.31e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.70  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  181 ELVQKLKEAQTIiaqhvaenprSEEDRNYESTIAQLKDEIQILN--KRLEDEALAQQ------QQKPKDEIVAESEKKLK 252
Cdd:PHA02562  154 KLVEDLLDISVL----------SEMDKLNKDKIRELNQQIQTLDmkIDHIQQQIKTYnknieeQRKKNGENIARKQNKYD 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  253 ELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELA----------------------DVGDSLLTE 310
Cdd:PHA02562  224 ELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkvikmyekggvcptctqqiSEGPDRITK 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  311 -KDSVKRLQDEAEKAKKQVadfeEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERET 389
Cdd:PHA02562  304 iKDKLKELQHSLEKLDTAI----DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 922581144  390 EIKKLKQRMDEerashTAQSEQEMKQLEAHYERAQKMLQDN 430
Cdd:PHA02562  380 ELAKLQDELDK-----IVKTKSELVKEKYHRGIVTDLLKDS 415
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 223-494 4.55e-05

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 47.13  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   223 LNKRLEdeALAQQQQKPKDEIvaESEK-KLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELA 301
Cdd:pfam09755   26 LQKRIE--SLQQENRVLKMEL--ETYKlRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLAMNY 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   302 DVGDSLLTEKDSVKRLQDEAEKAKKQVAdfEEKLKEIETEKiaLIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIaslq 381
Cdd:pfam09755  102 EQEEEFLTNDLSRKLTQLRQEKVELEQT--LEQEQEYQVNK--LMRKIEKLEAETLNKQTNLEQLRREKVELENTL---- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   382 atNEERETEIKKLKQRMDE-ERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALprggl 460
Cdd:pfam09755  174 --EQEQEALVNRLWKRMDKlEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATA----- 246

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 922581144   461 nEQQLHE-IFNWVSEEKATREEMENLTRKITGEVE 494
Cdd:pfam09755  247 -QQEHTEkMAQYAQEERHIREENLRLQRKLQLEME 280
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 674-725 5.00e-05

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 42.70  E-value: 5.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  674 RGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20839     6 RPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 57
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 675-725 5.66e-05

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410436  Cd Length: 50  Bit Score: 41.98  E-value: 5.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  675 GHNFERMKIKtPTKCGHC-TSILigldRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20886     3 GHRFEPGALG-PGWCDLCgRYIL----SQALRCTNCKYTCHSECRDLVQLDC 49
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 274-415 5.79e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 45.83  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   274 NINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEietekiALIKKQEEVT 353
Cdd:pfam04012   12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQA------ALTKGNEELA 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   354 IEARKSVETDDH----LSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERA-SHTAQSEQEMKQ 415
Cdd:pfam04012   86 REALAEKKSLEKqaeaLETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKArLKAAKAQEAVQT 152
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 676-719 5.84e-05

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 41.95  E-value: 5.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAE 719
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGKGKVGVRCEDCHACFHLVCAK 44
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
173-342 6.40e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  173 VELENEKAELVQKLKEAQTIIAQHVAENPRSEED---RNYESTIAQLKDEIQILNKRLEDE-----ALAQQQQKPKDEIV 244
Cdd:COG3206   229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSpviQQLRAQLAELEAELAELSARYTPNhpdviALRAQIAALRAQLQ 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  245 AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVlvekatvvqqrDDMQAELAdvgdslltekdsvkRLQDEAEKA 324
Cdd:COG3206   309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELR--------------RLEREVEVA 363

                         170
                  ....*....|....*...
gi 922581144  325 KKQVADFEEKLKEIETEK 342
Cdd:COG3206   364 RELYESLLQRLEEARLAE 381
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 142-498 6.71e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.53  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   142 DARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENpRSEEDRNYESTIAQLKDEIQ 221
Cdd:pfam12128  654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA-RTEKQAYWQVVEGALDAQLA 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   222 ILnkrleDEALAQQQQKPKDEIVAESEKKLKELK------ERNKQLVMEKSEIQRELDNINDHLDQVL----VEKATVVQ 291
Cdd:pfam12128  733 LL-----KAAIAARRSGAKAELKALETWYKRDLAslgvdpDVIAKLKREIRTLERKIERIAVRRQEVLryfdWYQETWLQ 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   292 QRDDMQAELADVgdsllteKDSVKRLQDEaekAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKsveTDDHLSEevv 371
Cdd:pfam12128  808 RRPRLATQLSNI-------ERAISELQQQ---LARLIADTKLRRAKLEMERKASEKQQVRLSENLRG---LRCEMSK--- 871

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   372 aakntIASLQ--ATNEERETEIKKLKQRMDEERASHTAQSEQemkqleahyerAQKMLQDNVEQMNVENR-GLRDEIEKL 448
Cdd:pfam12128  872 -----LATLKedANSEQAQGSIGERLAQLEDLKLKRDYLSES-----------VKKYVEHFKNVIADHSGsGLAETWESL 935

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   449 SQQMAALPRGGLNE-------QQLHEIFNWVSEE--KATREEMENLTRKITGEVESLKN 498
Cdd:pfam12128  936 REEDHYQNDKGIRLldyrklvPYLEQWFDVRVPQsiMVLREQVSILGVDLTEFYDVLAD 994
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 174-341 7.09e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  174 ELENEKAELVQKLKEAQTIIA---------QHVAENPRSEEDRNYESTIAQLKDEI-QILNKRLEDEALAQQQQKPKdei 243
Cdd:PRK00409  531 ELEQKAEEAEALLKEAEKLKEeleekkeklQEEEDKLLEEAEKEAQQAIKEAKKEAdEIIKELRQLQKGGYASVKAH--- 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 vaESEKKLKELKERNKQLVMEKSEIQRELDNINDHlDQV----LVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQD 319
Cdd:PRK00409  608 --ELIEARKRLNKANEKKEKKKKKQKEKQEELKVG-DEVkylsLGQKGEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQK 684

                         170       180
                  ....*....|....*....|..
gi 922581144  320 EAEKAKKQVADFEEKLKEIETE 341
Cdd:PRK00409  685 PKKKKKKKPKTVKPKPRTVSLE 706
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 138-422 7.28e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.99  E-value: 7.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   138 SLLSDARSLTDEIRAIAQrCQGDAELMEKSVDGFMVELE--NEKAELVQKLKEAQTIIAQHVAEnpRSEEDRNYESTIAQ 215
Cdd:pfam05622  108 SLAEEAQALKDEMDILRE-SSDKVKKLEATVETYKKKLEdlGDLRRQVKLLEERNAEYMQRTLQ--LEEELKKANALRGQ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   216 L---KDEIQILNKRLEDEAlaqqqqKPKDEIVAEsekkLKELKERNKQLVMEKSEIQRELDNINDHLDQVlveKATVVQQ 292
Cdd:pfam05622  185 LetyKRQVQELHGKLSEES------KKADKLEFE----YKKLEEKLEALQKEKERLIIERDTLRETNEEL---RCAQLQQ 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   293 RDDMQAEL-----ADVGDSLLTE------KDSVKRLQDEAEKAK-KQVADFEEKLKEIET-------------------- 340
Cdd:pfam05622  252 AELSQADAllspsSDPGDNLAAEimpaeiREKLIRLQHENKMLRlGQEGSYRERLTELQQlledanrrkneletqnrlan 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   341 EKIALIKKQEEvtiEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQS----------- 409
Cdd:pfam05622  332 QRILELQQQVE---ELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLaqkidelqeal 408

                          330
                   ....*....|....*.
gi 922581144   410 ---EQEMKQLEAHYER 422
Cdd:pfam05622  409 rkkDEDMKAMEERYKK 424
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 1-136 7.45e-05

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: 46.53  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDDeidwvVSEEAKDLIRQLICSSDVR---FGRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05615   204 MLAGQPPFDGEDEDELFQSIMEHN--VSYPKS-----LSKEAVSICKGLMTKHPAKrlgCGPEGERDIREHAFFRRIDWD 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   78 TI--RDSNPPYVPEVSSpEDTSNFDvdvceDDFTPCETQ--PPRVLAAFTGNHLPFVGFSYTH 136
Cdd:cd05615   277 KLenREIQPPFKPKVCG-KGAENFD-----KFFTRGQPVltPPDQLVIANIDQADFEGFSYVN 333
PDCD7 pfam16021
Programmed cell death protein 7;
180-425 8.49e-05

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 46.26  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   180 AELVQKLKEAQTIIAQhvAENPRSEEDRNYEsTIAQLKDEIQILNKRLEDEALAQQQQKpkdEIVAESEKKLKeLKERNK 259
Cdd:pfam16021   14 ARLVSRLETLCLELRE--NVEDDSVWSESYS-RAAELKHELQEKLLLLEDPELLESLKR---KLERRQKKRLR-RKRRKE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   260 QLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRdDMQAELADVGDSLLTEkdsVKRLQDEaekAKKQVADFE--EKLKE 337
Cdd:pfam16021   87 ERKEEKKEEQERRAEREAKIDKWRRKQIQEVEEK-KRERELKLAADAVLSE---VRKKQAD---AKRMLDILRslEKLRK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   338 IetEKIALIKKQEEVTIEARKSVETD-DHLSEEvvaakntiasLQATNEERETEIKKLKQrMDEERASHTAQSEQEMKQL 416
Cdd:pfam16021  160 L--RKEAARRKGIKPESECDEAFESHlEKLRSV----------WKKRTEEYSAEEKALKV-MLEGEQEEERKRRREKRQK 226


                   ....*....
gi 922581144   417 EAHYERAQK 425
Cdd:pfam16021  227 KEREEFLQK 235
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
 673-725 8.88e-05

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 41.56  E-value: 8.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  673 ERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20857     3 EKAHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDC 55
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 139-337 8.93e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.21  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  139 LLSDARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPRSEedrnyestIAQLKD 218
Cdd:cd22656   115 AKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKE--------IKDLQK 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  219 EIQILNKRLEDEALAQQQQKpKDEIVAESEKKLKELKernkqlvmekseIQRELDNINDHLDQVL--VEKATVVQQR--- 293
Cdd:cd22656   187 ELEKLNEEYAAKLKAKIDEL-KALIADDEAKLAAALR------------LIADLTAADTDLDNLLalIGPAIPALEKlqg 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 922581144  294 --DDMQAELADVGDSL---LTEKDSVKRLQDEAEKAKKQVADFEEKLKE 337
Cdd:cd22656   254 awQAIATDLDSLKDLLeddISKIPAAILAKLELEKAIEKWNELAEKADK 302
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
181-452 9.28e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 45.20  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  181 ELVQKLKEAQTIIAQHVaenprseedRNYESTIAQLKDEI--QILNKRLEDEALAQQQQKpkdeiVAESEKKLKELKERN 258
Cdd:COG1842    16 ALLDKAEDPEKMLDQAI---------RDMEEDLVEARQALaqVIANQKRLERQLEELEAE-----AEKWEEKARLALEKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  259 kqlvmekseiqreldniNDHL-DQVLVEKATVVQQRDDMQAELAdvgdslltekdsvkRLQDEAEKAKKQVADFEEKLKE 337
Cdd:COG1842    82 -----------------REDLaREALERKAELEAQAEALEAQLA--------------QLEEQVEKLKEALRQLESKLEE 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  338 IETEKIALIKKQEEVtiEARKSVetddhlseevvaaKNTIASLQATNEERetEIKKLKQRMDEERASHTAQSEQEMKQ-L 416
Cdd:COG1842   131 LKAKKDTLKARAKAA--KAQEKV-------------NEALSGIDSDDATS--ALERMEEKIEEMEARAEAAAELAAGDsL 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 922581144  417 EAHYERAQKmlQDNVEqmnvenrglrDEIEKLSQQM 452
Cdd:COG1842   194 DDELAELEA--DSEVE----------DELAALKAKM 217
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 204-596 1.08e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   204 EEDRNYESTIAQLKDEIQI---LNKRLEDE-ALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHL 279
Cdd:pfam10174   67 EENQHLQLTIQALQDELRAqrdLNQLLQQDfTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRI 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   280 DqvlVEKATVVQqRDDMQAELADvgdsLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtekiALIKKQEEVTIEARKS 359
Cdd:pfam10174  147 E---TQKQTLGA-RDESIKKLLE----MLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLE----VLLDQKEKENIHLREE 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   360 VETDDHLSEE---------VVAAKNT-IASLQATNEERETEIKKLKQrmdeERASHTAQSEQEMKQLEAhYERAQKMLQD 429
Cdd:pfam10174  215 LHRRNQLQPDpaktkalqtVIEMKDTkISSLERNIRDLEDEVQMLKT----NGLLHTEDREEEIKQMEV-YKSHSKFMKN 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   430 NVEQmnvenrgLRDEIEKLSQQMAALprgglnEQQLHEIFNWVSEEKATREEM-ENLTRK------ITGEVESLKNN--- 499
Cdd:pfam10174  290 KIDQ-------LKQELSKKESELLAL------QTKLETLTNQNSDCKQHIEVLkESLTAKeqraaiLQTEVDALRLRlee 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   500 --SPLTT-SNYIQNTPSGWGSRRMNNVARKDGLDLQrqlqaeiDAKLK-LKAELKNSQEQyltsaarLDDTEKRMASLMR 575
Cdd:pfam10174  357 keSFLNKkTKQLQDLTEEKSTLAGEIRDLKDMLDVK-------ERKINvLQKKIENLQEQ-------LRDKDKQLAGLKE 422

                          410       420
                   ....*....|....*....|.
gi 922581144   576 EVAMLKQQkniENSSDSAFSS 596
Cdd:pfam10174  423 RVKSLQTD---SSNTDTALTT 440
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
 1-100 1.12e-04

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 46.13  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMshQDMLDFPDdeidwVVSEEAKDLIRQLIcSSDV--RFG--RNGLSDFQLHPFFEGIDW 76
Cdd:PTZ00426  221 ILVGCPPFYANEPLLIYQKIL--EGIIYFPK-----FLDNNCKHLMKKLL-SHDLtkRYGnlKKGAQNVKEHPWFGNIDW 292

                          90       100
                  ....*....|....*....|....*.
gi 922581144   77 NTIRDSN--PPYVPEVSSPEDTSNFD 100
Cdd:PTZ00426  293 VSLLHKNveVPYKPKYKNVFDSSNFE 318
COG5022 COG5022
Myosin heavy chain [General function prediction only];
137-484 1.28e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.61  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  137 GSLLSDARSLTDEIRAIAQRCQGDAelmeksvdgfmVELENEKAELVQKLKeaqtiiaqhvaenpRSEEDRnyESTIAQL 216
Cdd:COG5022   813 RSYLACIIKLQKTIKREKKLRETEE-----------VEFSLKAEVLIQKFG--------------RSLKAK--KRFSLLK 865

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  217 KDEIQILNKRLEDEALAQQQQKpKDEIvaeseKKLKELKERNKQLVMEKSEIQRELDNindhldqVLVEKatvVQQRDDM 296
Cdd:COG5022   866 KETIYLQSAQRVELAERQLQEL-KIDV-----KSISSLKLVNLELESEIIELKKSLSS-------DLIEN---LEFKTEL 929

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  297 QAELADVGDSLLTEKDSVKRLQDEAEKAKKQvaDFEEKLKEIETEKIALIKKQEEVTIEARKSvetddhlSEEVvaaKNT 376
Cdd:COG5022   930 IARLKKLLNNIDLEEGPSIEYVKLPELNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKA-------NSEL---KNF 997

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  377 IASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALP 456
Cdd:COG5022   998 KKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSL 1077

                         330       340
                  ....*....|....*....|....*...
gi 922581144  457 RGGLNEQQLHEIFNWVSEEKATREEMEN 484
Cdd:COG5022  1078 LDDKQLYQLESTENLLKTINVKDLEVTN 1105
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 245-452 1.29e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 45.02  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   245 AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQV--LVEKATVVQQRDDMQAELADVG-----DSLLTEKDSVKRL 317
Cdd:pfam00261   18 KEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeeRLAEALEKLEEAEKAADESERGrkvleNRALKDEEKMEIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   318 QDEAEKAKKQVADFEEKLKEIEtEKIALIKKQEEVTIE-ARKSVETDDHLSEEVVAAKNTIASLQATNEE-------RET 389
Cdd:pfam00261   98 EAQLKEAKEIAEEADRKYEEVA-RKLVVVEGDLERAEErAELAESKIVELEEELKVVGNNLKSLEASEEKaseredkYEE 176

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   390 EIKKLKQRmdeerashtaqseqeMKQLEAHYERAQKM---LQDNVEQMNVENRGLRDEIEKLSQQM 452
Cdd:pfam00261  177 QIRFLTEK---------------LKEAETRAEFAERSvqkLEKEVDRLEDELEAEKEKYKAISEEL 227
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 675-728 1.42e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 41.01  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVP 728
Cdd:cd20888     2 APHTHTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPCVPA 55
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 254-434 1.45e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 43.79  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   254 LKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRddMQAELADVGDSLLTEKDSVK-RLQDEAEKAKKQVADFE 332
Cdd:pfam01442    2 LEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRER--LQKDLEEVRAKLEPYLEELQaKLGQNVEELRQRLEPYT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   333 EKLKEIETEKI-ALIKKQEEVTIEARKSVETddHLSEevvaakntiasLQATNEERETEIK-KLKQRMDEERASHTAQSE 410
Cdd:pfam01442   80 EELRKRLNADAeELQEKLAPYGEELRERLEQ--NVDA-----------LRARLAPYAEELRqKLAERLEELKESLAPYAE 146

                          170       180
                   ....*....|....*....|....
gi 922581144   411 QEMKQLEAHYERAQKMLQDNVEQM 434
Cdd:pfam01442  147 EVQAQLSQRLQELREKLEPQAEDL 170
Filament pfam00038
Intermediate filament protein;
175-446 1.52e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.30  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   175 LENEKAELVQKLKEAQtiiAQHVAEnpRSEEDRNYESTIAQLKDEIQIL---NKRLEDE------ALAQQQQKPKDEIV- 244
Cdd:pfam00038   23 LEQQNKLLETKISELR---QKKGAE--PSRLYSLYEKEIEDLRRQLDTLtveRARLQLEldnlrlAAEDFRQKYEDELNl 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   245 -AESEKKLKELKERNKQLVMEKSEIQRELDNINDHL--------------------DQVLVEKATVVQQrdDMQAELADV 303
Cdd:pfam00038   98 rTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELaflkknheeevrelqaqvsdTQVNVEMDAARKL--DLTSALAEI 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   304 gdslltekdsvkRLQDE--AEKAKKQV-ADFEEKLKEIETE----KIALIKKQEEVTiEARKSVETddhLSEEVVAAKNT 376
Cdd:pfam00038  176 ------------RAQYEeiAAKNREEAeEWYQSKLEELQQAaarnGDALRSAKEEIT-ELRRTIQS---LEIELQSLKKQ 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   377 IASLQATNEEreteikkLKQRMDEERASHT---AQSEQEMKQLEAHYERaqkMLQDNVEQMNVEnrgLRDEIE 446
Cdd:pfam00038  240 KASLERQLAE-------TEERYELQLADYQeliSELEAELQETRQEMAR---QLREYQELLNVK---LALDIE 299
PRK01156 PRK01156
chromosome segregation protein; Provisional
 264-417 1.55e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.05  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  264 EKSEIQRELDNINDHLDQVLVEKATVvqqrDDMQAELADVGDSllteKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKi 343
Cdd:PRK01156  150 QRKKILDEILEINSLERNYDKLKDVI----DMLRAEISNIDYL----EEKLKSSNLELENIKKQIADDEKSHSITLKEI- 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144  344 alikkqEEVTIEARKSVETDDHLSEEVvaakNTIASLQATNEERETEIKKLKQR--MDEERASHTAQSEQEMKQLE 417
Cdd:PRK01156  221 ------ERLSIEYNNAMDDYNNLKSAL----NELSSLEDMKNRYESEIKTAESDlsMELEKNNYYKELEERHMKII 286
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 161-448 1.55e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   161 AELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENpRSEEDRNYESTIAQlKDEIQILNKRLEDEALAQQQQKpk 240
Cdd:pfam13868   46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER-EQKRQEEYEEKLQE-REQMDEIVERIQEEDQAEAEEK-- 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   241 deivAESEKKLKELKERNKQLVMEKSEIQRELDNIND-HLDQVLVEKATVVQQRDDMQAELADvgdslltEKDSV-KRLQ 318
Cdd:pfam13868  122 ----LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKAEREEEREAEREEIEE-------EKEREiARLR 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   319 DEAEKAKKQVADFEEKLKEIEtekialikkQEEVTIEARKsvetddhlsEEVVAAKNTIASLQATNEERETEIKkLKQRM 398
Cdd:pfam13868  191 AQQEKAQDEKAERDELRAKLY---------QEEQERKERQ---------KEREEAEKKARQRQELQQAREEQIE-LKERR 251

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 922581144   399 DEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVEnrgLRDEIEKL 448
Cdd:pfam13868  252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE---HRRELEKQ 298
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 199-452 1.82e-04

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 45.89  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  199 ENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDH 278
Cdd:COG5192   427 ELSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFY 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  279 LDQVLVEKATvvqqrDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIAliKKQEEV-TIEAR 357
Cdd:COG5192   507 DESLSPEECI-----EEYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELK--KKWSSLaQLKSR 579

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  358 -------KSVETDDHLS---EEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKML 427
Cdd:COG5192   580 fqkdatlDSIEGEEELIqddEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNFEL 659

                         250       260
                  ....*....|....*....|....*
gi 922581144  428 QDNVEQMNVENRGLRDEIEKLSQQM 452
Cdd:COG5192   660 EERGDPEKKDVDWYTEEKRKIEEQL 684
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 215-585 1.83e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   215 QLKDEIQILNKRLED------------EALAQQQQKPKDEIVAES----------EKKLKELKERNKQLvmeKSEIQREL 272
Cdd:TIGR00606  688 QTEAELQEFISDLQSklrlapdklkstESELKKKEKRRDEMLGLApgrqsiidlkEKEIPELRNKLQKV---NRDIQRLK 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   273 DNINDHLDQVlvekATVVQQRDDMQAELADVGdslltekdSVKRLQDEAEKAKKQVADFEEKLKEIETEKialikkqeeV 352
Cdd:TIGR00606  765 NDIEEQETLL----GTIMPEEESAKVCLTDVT--------IMERFQMELKDVERKIAQQAAKLQGSDLDR---------T 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   353 TIEARKSVETDDHLSEEVVAaknTIASLQATNEERETEIKKLKQRMDEERaSHTAQSEQEMKQLEAHYERAQKMLQDnVE 432
Cdd:TIGR00606  824 VQQVNQEKQEKQHELDTVVS---KIELNRKLIQDQQEQIQHLKSKTNELK-SEKLQIGTNLQRRQQFEEQLVELSTE-VQ 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   433 QMNVENRGLRDEIEKLSQQMAALprgglnEQQLHEIFNWVSEE-KATREEMENLTRKITGEVESLKNnspltTSNYIQNT 511
Cdd:TIGR00606  899 SLIREIKDAKEQDSPLETFLEKD------QQEKEELISSKETSnKKAQDKVNDIKEKVKNIHGYMKD-----IENKIQDG 967

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581144   512 PSGWGSRRMNNVARKDG-LDLQRQLQAEIDAKLKLKAELKNS---QEQYLTSAARLDDTEKRMASLMREVAMLKQQKN 585
Cdd:TIGR00606  968 KDDYLKQKETELNTVNAqLEECEKHQEKINEDMRLMRQDIDTqkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMG 1045
C1_alphaCHN cd20856
protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; ...
 673-725 1.98e-04

protein kinase C conserved region 1 (C1 domain) found in alpha-chimaerin and similar proteins; Alpha-chimaerin, also called A-chimaerin, N-chimaerin (CHN), alpha-chimerin, N-chimerin (NC), or Rho GTPase-activating protein 2 (ARHGAP2), is a GTPase-activating protein (GAP) for p21-rac and a phorbol ester receptor. It is involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. Alpha-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410406  Cd Length: 57  Bit Score: 40.44  E-value: 1.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  673 ERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20856     3 EKVHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDC 55
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 1-89 2.21e-04

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: 44.83  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPF--YSERLVDTYGKIMSHQDMLDFPDDeidwvVSEEAKDLIRQLICSS-DVRFGRNGLS--DFQLHPFFEGID 75
Cdd:cd05577   188 MIAGRSPFrqRKEKVDKEELKRRTLEMAVEYPDS-----FSPEARSLCEGLLQKDpERRLGCRGGSadEVKEHPFFRSLN 262

                          90
                  ....*....|....*.
gi 922581144   76 WNTIRDS--NPPYVPE 89
Cdd:cd05577   263 WQRLEAGmlEPPFVPD 278
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 675-725 2.24e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; 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. 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. 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. 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. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 40.33  E-value: 2.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20794     2 GHLFQAKRFNRRAVCAYCSDRIWGLGRQGYKCINCKLLVHKKCHKLVKVAC 52
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
262-460 2.39e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.62  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  262 VMEKSEIQRELDNINDHldqvlvekatvvqQRDDMQAEL---------------------------ADV--GDSL----- 307
Cdd:COG2433   317 VEEKLHLAREYGYDNDH-------------ERDALAAALkaydayknkfervekkvppdvdrdevkARVirGLSIeeale 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  308 -LTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtekialiKKQEEVtiearksvetdDHLSEEVVAAKNTIASLQATNEE 386
Cdd:COG2433   384 eLIEKELPEEEPEAEREKEHEERELTEEEEEIR-------RLEEQV-----------ERLEAEVEELEAELEEKDERIER 445

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144  387 RETEIKKLKQRMDEErashtAQSEQEMKQLEAHYERAQKMLQDnvEQMNVENrgLRDEIEKLSQQMAALPRGGL 460
Cdd:COG2433   446 LERELSEARSEERRE-----IRKDREISRLDREIERLERELEE--ERERIEE--LKRKLERLKELWKLEHSGEL 510
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 234-586 2.53e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   234 QQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQrELDNINDHLDQVLVEKatvvqQRDDMQAELADVGDSLLTE--- 310
Cdd:TIGR00606  230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM-KLDNEIKALKSRKKQM-----EKDNSELELKMEKVFQGTDeql 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   311 KDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIE-ARKSVETDDHlseevvaakntiaslQATNEERET 389
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEqGRLQLQADRH---------------QEHIRARDS 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   390 EIKKLKQRMDEERASHTAQSEQEMKQLeahyeraqkmlqdnveqMNVENRGLRDEIEKLSQQMAAL-PRGGLNEQQLHEI 468
Cdd:TIGR00606  369 LIQSLATRLELDGFERGPFSERQIKNF-----------------HTLVIERQEDEAKTAAQLCADLqSKERLKQEQADEI 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   469 FNwvsEEKATREEMENLTRKITGEVESLKNnsplTTSNYIQNTPSGWGSRRMNNVARKDGLDLQR-QLQAEIDAKLKLKA 547
Cdd:TIGR00606  432 RD---EKKGLGRTIELKKEILEKKQEELKF----VIKELQQLEGSSDRILELDQELRKAERELSKaEKNSLTETLKKEVK 504

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 922581144   548 ELKNSQEQYLTSAARLDdteKRMASLMREVAMLKQQKNI 586
Cdd:TIGR00606  505 SLQNEKADLDRKLRKLD---QEMEQLNHHTTTRTQMEML 540
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 675-725 2.55e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; 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. 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. 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. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 40.35  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd21095     2 GHLFQAKRFNRRAYCGQCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTC 52
PRK11281 PRK11281
mechanosensitive channel MscK;
265-585 2.60e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.67  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  265 KSEIQRELDNINDHLDQVlVEKATVVQQRDDMQAELadvgdslltekDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIA 344
Cdd:PRK11281   38 EADVQAQLDALNKQKLLE-AEDKLVQQDLEQTLALL-----------DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  345 LIKKQEEVTIEA----------RKSVETDDHLS---EEVVAAKNTIASLQ----------ATNEERETEI-KKLKQRMDE 400
Cdd:PRK11281  106 LKDDNDEETRETlstlslrqleSRLAQTLDQLQnaqNDLAEYNSQLVSLQtqperaqaalYANSQRLQQIrNLLKGGKVG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  401 ERASHTAQSEQ---EMKQLEAHYERAQKMLQDNVE-QMNVENRglRDE----IEKLSQQMAALpRGGLNEQQLHEifnwv 472
Cdd:PRK11281  186 GKALRPSQRVLlqaEQALLNAQNDLQRKSLEGNTQlQDLLQKQ--RDYltarIQRLEHQLQLL-QEAINSKRLTL----- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  473 SEEKATREEMENLTRKITGE---VESLKNNSPLttSNY-IQNTpsgwgsRRMN-----NVARKDGLD----LQRQLQAEI 539
Cdd:PRK11281  258 SEKTVQEAQSQDEAARIQANplvAQELEINLQL--SQRlLKAT------EKLNtltqqNLRVKNWLDrltqSERNIKEQI 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 922581144  540 DAkLK---LKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKN 585
Cdd:PRK11281  330 SV-LKgslLLSRILYQQQQALPSADLIEGLADRIADLRLEQFEINQQRD 377
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 166-489 2.89e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.42  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   166 KSVDGFMVELENEKAELVQKLKEAQTIIAQHVAE--NPRSEEDRNYESTIAQLKDEIQILNKrlEDEALAQQQ------- 236
Cdd:TIGR00606  272 KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDlyHNHQRTVREKERELVDCQRELEKLNK--ERRLLNQEKtellveq 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   237 ---QKPKDEIVAESEKKLKELKERNKQLVMEKSE----IQRELDN---------------INDHLDQVLVEKATVVQQRD 294
Cdd:TIGR00606  350 grlQLQADRHQEHIRARDSLIQSLATRLELDGFErgpfSERQIKNfhtlvierqedeaktAAQLCADLQSKERLKQEQAD 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   295 DMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVT-IEARKSVETddhLSEEVVAA 373
Cdd:TIGR00606  430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSkAEKNSLTET---LKKEVKSL 506

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   374 KNTIASLQAT-------NEERETEIKKLKQRM---------DEERASHTAQSEQEMKQLeAHYERAQKMLQDNVEQMNVE 437
Cdd:TIGR00606  507 QNEKADLDRKlrkldqeMEQLNHHTTTRTQMEmltkdkmdkDEQIRKIKSRHSDELTSL-LGYFPNKKQLEDWLHSKSKE 585

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 922581144   438 NRGLRDEIEKLSQQMAALprgglnEQQLHEIFNwvsEEKATREEMENLTRKI 489
Cdd:TIGR00606  586 INQTRDRLAKLNKELASL------EQNKNHINN---ELESKEEQLSSYEDKL 628
PRK01156 PRK01156
chromosome segregation protein; Provisional
 147-402 2.92e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.28  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  147 TDEIRAIAQRCQGDAELMEKSVDgfmvELENEKAELVQKLKEAQTIIAQHVAENPRS--EEDRNYESTIAQLKD----EI 220
Cdd:PRK01156  464 EEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIVDLKKRKEYLESEEINKsiNEYNKIESARADLEDikikIN 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  221 QILNKRLEDEALAQQQQKPKDEIV-AESEKKLKELKERN----KQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDD 295
Cdd:PRK01156  540 ELKDKHDKYEEIKNRYKSLKLEDLdSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK 619

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  296 MQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtekiALIKKQEEVTIEARKSVETDDHLSEEVVAAKN 375
Cdd:PRK01156  620 SIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID----SIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695

                         250       260
                  ....*....|....*....|....*..
gi 922581144  376 TIASLQATNEERETEIKKLKQRMDEER 402
Cdd:PRK01156  696 NRARLESTIEILRTRINELSDRINDIN 722
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
 675-727 3.51e-04

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 39.84  E-value: 3.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRqGLFCQSCQYACHVSCAERVSQSCPV 727
Cdd:cd20884     5 GHVFTSYQVNIMQSCEQCSSYIWAMEK-ALLCSVCKMTCHKKCLSKIQSHCSS 56
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 330-467 3.56e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.07  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  330 DFEEKLKEIETEKIALIKKQEEVTIEARKSvetddhLSEEVVAAKNTIASLQAT-NEERE--TEIKKLKQRMdEERASHT 406
Cdd:COG0542   415 ELERRLEQLEIEKEALKKEQDEASFERLAE------LRDELAELEEELEALKARwEAEKEliEEIQELKEEL-EQRYGKI 487

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922581144  407 AQSEQEMKQLEAHYERAQKMLQDNVEQMNVE-----------NRGLRDEIEKLsQQMaalprgglnEQQLHE 467
Cdd:COG0542   488 PELEKELAELEEELAELAPLLREEVTEEDIAevvsrwtgipvGKLLEGEREKL-LNL---------EEELHE 549
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 164-403 3.70e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   164 MEKSVDGFMVELENEKAELVQKL-KEAQTIIAQHVAENP--RSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKpk 240
Cdd:pfam17380  385 MERQQKNERVRQELEAARKVKILeEERQRKIQQQKVEMEqiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV-- 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   241 dEIVAESE-----KKLKELKERNKQLVMEKseiqreldnindhldqvlvekatvvQQRDDMQAELADVGDSLLTEKDSVK 315
Cdd:pfam17380  463 -ERLRQQEeerkrKKLELEKEKRDRKRAEE-------------------------QRRKILEKELEERKQAMIEEERKRK 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   316 RLQDEAEKAKKQVADfEEKLKEIETEKialiKKQEEvtIEARKSVEtddhlsEEVVAAKNTIASLQATNEERETeikkLK 395
Cdd:pfam17380  517 LLEKEMEERQKAIYE-EERRREAEEER----RKQQE--MEERRRIQ------EQMRKATEERSRLEAMEREREM----MR 579


                   ....*...
gi 922581144   396 QRMDEERA 403
Cdd:pfam17380  580 QIVESEKA 587
mukB PRK04863
chromosome partition protein MukB;
173-455 4.02e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  173 VELENEKAELVQKLKEAQTiiaQHVAENPR---SEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQkpkDEIVAESEK 249
Cdd:PRK04863  310 VEMARELAELNEAESDLEQ---DYQAASDHlnlVQTALRQQEKIERYQADLEELEERLEEQNEVVEEA---DEQQEENEA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  250 KLKELKERNKQLVMEKSEIQRELD-----NINDHLDQVLVEKATVVQQRDDMQAELADvgdslltekDSVKRLQDEAEKA 324
Cdd:PRK04863  384 RAEAAEEEVDELKSQLADYQQALDvqqtrAIQYQQAVQALERAKQLCGLPDLTADNAE---------DWLEEFQAKEQEA 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  325 KKQVADFEEKL------KEIETEKIALIKK---------QEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERET 389
Cdd:PRK04863  455 TEELLSLEQKLsvaqaaHSQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR 534

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  390 EIKKLKQRmdEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQmNVENR-GLRDEIEKLSQQMAAL 455
Cdd:PRK04863  535 AERLLAEF--CKRLGKNLDDEDELEQLQEELEARLESLSESVSE-ARERRmALRQQLEQLQARIQRL 598
C1_DGKeta_rpt1 cd20848
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 676-725 4.31e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410398  Cd Length: 86  Bit Score: 40.53  E-value: 4.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20848    30 HNWYACSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNC 79
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-306 5.18e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  138 SLLSDARSLTDEIRAIaqrcQGDAELMEKSVDgfmvELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTI---- 213
Cdd:COG3883    41 ALQAELEELNEEYNEL----QAELEALQAEID----KLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLlgse 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  214 --------AQLKDEI-----QILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLD 280
Cdd:COG3883   113 sfsdfldrLSALSKIadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192

                         170       180
                  ....*....|....*....|....*.
gi 922581144  281 QVLVEKATVVQQRDDMQAELADVGDS 306
Cdd:COG3883   193 AAEAQLAELEAELAAAEAAAAAAAAA 218
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 205-467 5.19e-04

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 44.51  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   205 EDRNYESTIA-----QLKDEIQILNKRLEDEaLAQQQQKpkdeIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHL 279
Cdd:pfam15964  345 EEANFEKTKAliqceQLKSELERQKERLEKE-LASQQEK----RAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQV 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   280 DQVLVEKATVVQQRDDMQAELA-------DVGDSLLTEKDSVKRLQDEAEK-----AKKQVADFEEKLKEIETEKIALIK 347
Cdd:pfam15964  420 EKVTREKNSLVSQLEEAQKQLAsqemdvtKVCGEMRYQLNQTKMKKDEAEKehreyRTKTGRQLEIKDQEIEKLGLELSE 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   348 KQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETeikkLKQRMDEERASHTAQSE-------QEMKQLEAHY 420
Cdd:pfam15964  500 SKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKES----IQQSFSNEAKAQALQAQqreqeltQKMQQMEAQH 575

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922581144   421 ERA-----------------------------QKMLQDN---VEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHE 467
Cdd:pfam15964  576 DKTvneqyslltsqntfiaklkeecctlakklEEITQKSrseVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHE 654
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 374-454 5.38e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 5.38e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    374 KNTIASLQATNEERETEIKKLKQRMDEERASHTAQS----EQEMKQLEAHYERAQKMLQDNVEQM-NVENRGLRDEIEKL 448
Cdd:smart00935   24 EKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAArekkEKELQKKVQEFQRKQQKLQQDLQKRqQEELQKILDKINKA 103


                    ....*.
gi 922581144    449 SQQMAA 454
Cdd:smart00935  104 IKEVAK 109
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
 1-100 5.39e-04

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: 43.92  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidwVVSEEAKDLIRQLICSSDVRF---GRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05593   208 MMCGRLPFYNQDHEKLFELILMED--IKFPR-----TLSADAKSLLSGLLIKDPNKRlggGPDDAKEIMRHSFFTGVNWQ 280

                          90       100
                  ....*....|....*....|....*
gi 922581144   78 TIRDSN--PPYVPEVSSPEDTSNFD 100
Cdd:cd05593   281 DVYDKKlvPPFKPQVTSETDTRYFD 305
C1_VAV1 cd20867
protein kinase C conserved region 1 (C1 domain) found in VAV1 protein; VAV1 is expressed ...
 670-721 5.53e-04

protein kinase C conserved region 1 (C1 domain) found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410417  Cd Length: 57  Bit Score: 39.16  E-value: 5.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 922581144  670 SAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERV 721
Cdd:cd20867     1 NATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCHRCRAPAHKECLGRV 52
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 675-725 5.54e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota type; 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. 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. 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. Members of this family contain C1 domain found in aPKC isoform iota. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410447  Cd Length: 55  Bit Score: 39.22  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922581144  675 GHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd21094     2 GHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIEC 52
C1_DGKdelta_rpt1 cd20847
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 676-725 5.67e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. DAG kinase delta contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410397  Cd Length: 85  Bit Score: 40.08  E-value: 5.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC 725
Cdd:cd20847    25 HNWYACSHARPTYCNVCREALSGVTSHGLSCEVCKFKAHKRCAVRATNNC 74
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 246-498 6.04e-04

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 44.25  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   246 ESEKKLKELKERNKQLV---MEKSEIQRELDNINDHLDQVL--VEKAtvvqQRDDMQA----ELADV-------GdslLT 309
Cdd:pfam05701   43 ELEKVQEEIPEYKKQSEaaeAAKAQVLEELESTKRLIEELKlnLERA----QTEEAQAkqdsELAKLrveemeqG---IA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   310 EKDSV-KRLQDEAEKA--KKQVADFEEKLKEIET----------EKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNT 376
Cdd:pfam05701  116 DEASVaAKAQLEVAKArhAAAVAELKSVKEELESlrkeyaslvsERDIAIKRAEEAVSASKEIEKTVEELTIELIATKES 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   377 IASLQATNeeRETEIKKLKQRMDEERASHtaQSEQEMKQLEAHYER------AQKMLQDNVEQMNVENRGLRDEiekLSQ 450
Cdd:pfam05701  196 LESAHAAH--LEAEEHRIGAALAREQDKL--NWEKELKQAEEELQRlnqqllSAKDLKSKLETASALLLDLKAE---LAA 268

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 922581144   451 QM-AALPRGGLNEQQLHEIFNWVSEEKA-TREEMENLTRKI---TGEVESLKN 498
Cdd:pfam05701  269 YMeSKLKEEADGEGNEKKTSTSIQAALAsAKKELEEVKANIekaKDEVNCLRV 321
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
 341-549 6.40e-04

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 43.82  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  341 EKIALIKKQEEVTIE---ARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMD------EERASHTAQSEQ 411
Cdd:PRK10361   30 QKAEQLAEREEMVAElsaAKQQITQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEaaqqhaDDKIRQMINSEQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  412 emkQLEAHYER-AQKMLQDNVEQMNVENR-GLRDEIEKLSQQMAALPRG-----GLNEQQ----LHEIFNWVSEEKATRE 480
Cdd:PRK10361  110 ---RLSEQFENlANRIFEHSNRRVDEQNRqSLNSLLSPLREQLDGFRRQvqdsfGKEAQErhtlAHEIRNLQQLNAQMAQ 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144  481 EMENLTRKITGEveslknnsplttsnyiQNTPSGWG----SRRMNNVARKDGLDLQRQLQAEIDAKLKLKAEL 549
Cdd:PRK10361  187 EAINLTRALKGD----------------NKTQGNWGevvlTRVLEASGLREGYEYETQVSIENDARSRMQPDV 243
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
175-371 6.75e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  175 LENEKAELVQKLKEAQTIIAQHVAENPRSEED--RNYESTIAQLKDEIQILNKRLEDealaqqqqkpKDEIVAESEKKLK 252
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEeiRRLEEQVERLEAEVEELEAELEE----------KDERIERLERELS 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  253 ELKERNKQLVMEKSEIQReLDNINDHLdqvlvekatvvqqrddmqaeladvgdsllteKDSVKRLQDEAEKAKKQVADFE 332
Cdd:COG2433   452 EARSEERREIRKDREISR-LDREIERL-------------------------------ERELEEERERIEELKRKLERLK 499

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 922581144  333 EKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVV 371
Cdd:COG2433   500 ELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDV 538
mukB PRK04863
chromosome partition protein MukB;
155-450 7.83e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  155 QRCQGDAElmeksvdgfmvELENEKAELVQKLKEAQTIIAQHVAENPRSEEDrnYESTIAQLKDEIQILNKrLEDEALAQ 234
Cdd:PRK04863  351 ERYQADLE-----------ELEERLEEQNEVVEEADEQQEENEARAEAAEEE--VDELKSQLADYQQALDV-QQTRAIQY 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  235 QQQK----------PKDEIVAES-EKKLKELKERNKQLVMEKSEIQREL---DNINDHLDQV--LVEKAT---------- 288
Cdd:PRK04863  417 QQAVqalerakqlcGLPDLTADNaEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAyqLVRKIAgevsrseawd 496

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  289 --------------VVQQRDDMQAELADVGDSLLTEKDsVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIkkqeevti 354
Cdd:PRK04863  497 varellrrlreqrhLAEQLQQLRMRLSELEQRLRQQQR-AERLLAEFCKRLGKNLDDEDELEQLQEELEARL-------- 567

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  355 earksvetdDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRmdeERASHTAQ----------------SEQEMKQLEA 418
Cdd:PRK04863  568 ---------ESLSESVSEARERRMALRQQLEQLQARIQRLAAR---APAWLAAQdalarlreqsgeefedSQDVTEYMQQ 635

                         330       340       350
                  ....*....|....*....|....*....|..
gi 922581144  419 HYERaQKMLQDNVEQMNVENRGLRDEIEKLSQ 450
Cdd:PRK04863  636 LLER-ERELTVERDELAARKQALDEEIERLSQ 666
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 315-402 7.99e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.67  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   315 KRLQDEAEKAKKQVAD-------FEEKLKEIETEKIALIKKQEEVTIE-------ARKSVETDDHLSEEVVAAKNTIASL 380
Cdd:pfam20492   16 KQYEEETKKAQEELEEseetaeeLEEERRQAEEEAERLEQKRQEAEEEkerleesAEMEAEEKEQLEAELAEAQEEIARL 95

                           90       100
                   ....*....|....*....|..
gi 922581144   381 QATNEERETEIKKLKQRMDEER 402
Cdd:pfam20492   96 EEEVERKEEEARRLQEELEEAR 117
Fungal_TACC pfam12709
Fungal Transforming acidic coiled-coil (TACC) proteins; TACC proteins are present in different ...
 392-454 8.54e-04

Fungal Transforming acidic coiled-coil (TACC) proteins; TACC proteins are present in different organizms, ranging from yeasts to mammals. Schizosaccharomyces pombe has one TACC protein, known as Alp7 or Mia1p. Alp7/TACC consists of two domains: the N-terminal half that contains the nuclear localization signal (NLS) and has no homology to the other TACC members, and the C-terminal half, which consists of the conserved coiled-coil TACC domain. Alp7/TACC forms a complex with Alp14/TOG and localizes to microtubules, SPBs and kinetochores. This complex is necessary for mitotic and meiotic spindle assembly and proper chromosome segregation. The homolog from S. cerevisiae, Slk19, also has a role in spindle assembly and stability, and it is required for proper chromosome segregation.


Pssm-ID: 403801 [Multi-domain]  Cd Length: 77  Bit Score: 39.19  E-value: 8.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581144   392 KKLKQRMDEERASHTAQSEQEMKQLEAHYERAqkmLQDNVEQMNVENRGLRDEIEKLSQQMAA 454
Cdd:pfam12709    4 KRLQLLAEDLYIQYSSKHEQKVKLLKKGYESK---YQKKLDKLSLENKGLRQEIEQLKKQLET 63
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 182-497 1.03e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.58  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   182 LVQKLKEAQTIIAQHVAENPRSEED-RNYESTIAQLKDEIQILNKRLEDEalaqqqqkpkdeivaesEKKLKELKERNKQ 260
Cdd:pfam05557  281 LSRRIEQLQQREIVLKEENSSLTSSaRQLEKARRELEQELAQYLKKIEDL-----------------NKKLKRHKALVRR 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   261 LvmekseiQRELdnindhldqvlvekATVVQQRDDMQAELADVgDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEt 340
Cdd:pfam05557  344 L-------QRRV--------------LLLTKERDGYRAILESY-DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME- 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   341 ekIALIKKQEEVTIEarksvetddhlseevvaakntiaSLQATNEEREteIKKLKQRMDEERASHTAQSEQEMKQleahy 420
Cdd:pfam05557  401 --AQLSVAEEELGGY-----------------------KQQAQTLERE--LQALRQQESLADPSYSKEEVDSLRR----- 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   421 eraqkmlqdNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQ----LHEIFNWVSE-EKATREEMENLTRkitgEVES 495
Cdd:pfam05557  449 ---------KLETLELERQRLREQKNELEMELERRCLQGDYDPKktkvLHLSMNPAAEaYQQRKNQLEKLQA----EIER 515


                   ..
gi 922581144   496 LK 497
Cdd:pfam05557  516 LK 517
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
184-583 1.04e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 43.36  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  184 QKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVM 263
Cdd:COG5278   118 QWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  264 EKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEK- 342
Cdd:COG5278   198 RALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLAl 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  343 IALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYER 422
Cdd:COG5278   278 AAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAA 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  423 AQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPL 502
Cdd:COG5278   358 AAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEE 437

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  503 TTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQ 582
Cdd:COG5278   438 EALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517


                  .
gi 922581144  583 Q 583
Cdd:COG5278   518 A 518
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
 146-281 1.08e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 40.81  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   146 LTDEIRAIaqrCQGDAELMEksvdgfmvELENEKAELVQKLKEAQTIIAQHVAENPRSEEdrnyESTIAQLkdeiqiLNK 225
Cdd:pfam05130   21 LEEEQEAL---KAGDIEALE--------ELTEEKQELLQKLAQLEKERRELLAELGLSPE----EATLSEL------LAK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   226 RLEDEALAQQQQKpkdeiVAESEKKLKELKERNKQLVMEKSE-IQRELDNINDHLDQ 281
Cdd:pfam05130   80 EEEDPELRELWQE-----LLELLERLKELNELNGELIEQSLEfNNRSLNILQGAANG 131
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 219-454 1.09e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 42.29  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   219 EIQILNKRLEDEAlaqQQQKPKDEI---------VAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEK--- 286
Cdd:pfam12795    1 KLDELEKAKLDEA---AKKKLLQDLqqalslldkIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlas 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   287 ---ATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETeKIALIKKQEEVTIEARKsvetd 363
Cdd:pfam12795   78 lslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN-RLNGPAPPGEPLSEAQR----- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   364 dhlseevVAAKNTIASLQATNEERETEIKKLKQRMDeerashTAQSEQEmkQLEAHYERAQKMLQDNVEQMNVENRGLRD 443
Cdd:pfam12795  152 -------WALQAELAALKAQIDMLEQELLSNNNRQD------LLKARRD--LLTLRIQRLEQQLQALQELLNEKRLQEAE 216

                          250
                   ....*....|.
gi 922581144   444 EIEKLSQQMAA 454
Cdd:pfam12795  217 QAVAQTEQLAE 227
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 310-482 1.12e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.02  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   310 EKDSVKRLQdeAEKAKKQVADFEEKLKEIETEKialiKKQEEvtiearkSVETDDHLSEEvvaakntiasLQATNEERET 389
Cdd:pfam15709  331 EKASRDRLR--AERAEMRRLEVERKRREQEEQR----RLQQE-------QLERAEKMREE----------LELEQQRRFE 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   390 EIKKLKQRMDEERAShtaQSEQEMKQleahyERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAAlPRGGLNEQQLHEIF 469
Cdd:pfam15709  388 EIRLRKQRLEEERQR---QEEEERKQ-----RLQLQAAQERARQQQEEFRRKLQELQRKKQQEEA-ERAEAEKQRQKELE 458

                          170
                   ....*....|...
gi 922581144   470 NWVSEEKATREEM 482
Cdd:pfam15709  459 MQLAEEQKRLMEM 471
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 213-411 1.14e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   213 IAQLKDEIQILNKRLEdealaqqqqkpkdeivaESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQvlvekatvvQQ 292
Cdd:pfam13851   28 IKSLKEEIAELKKKEE-----------------RNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN---------YE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   293 RDDMqaeladvgdSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVEtddhLSEEVVA 372
Cdd:pfam13851   82 KDKQ---------SLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTG----LKNLLLE 148

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 922581144   373 AKntIASLQATNEERETEIKKLKQRMDEERASHTAQSEQ 411
Cdd:pfam13851  149 KK--LQALGETLEKKEAQLNEVLAAANLDPDALQAVTEK 185
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 229-417 1.27e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  229 DEALAQQQQKPKDEIVAEsEKKLKELKERNKQLVMEKSEIQREldniNDHLDQVLVEKATVVQQRDDMQAELADVGDSLL 308
Cdd:PRK09510   73 SAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQ----EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  309 TEKDSVKRLQDEAEKA----KKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATN 384
Cdd:PRK09510  148 KAEAEAKRAAAAAKKAaaeaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227

                         170       180       190
                  ....*....|....*....|....*....|...
gi 922581144  385 EERETEIKKLKQRMDEERASHTAQSEQEMKQLE 417
Cdd:PRK09510  228 AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 176-449 1.32e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  176 ENEKAELVQKLKEAQTIIAQHVAENPRseedrnYESTIAQLKDEIQILNK------RLEDEALAQQQQKPKDEI------ 243
Cdd:COG3096   835 EAELAALRQRRSELERELAQHRAQEQQ------LRQQLDQLKEQLQLLNKllpqanLLADETLADRLEELREELdaaqea 908

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  244 ---VAESEKKLKELK----------ERNKQLVMEKSEIQRELDNindhLDQVLVEKATVVQQRD--------DMQAELAD 302
Cdd:COG3096   909 qafIQQHGKALAQLEplvavlqsdpEQFEQLQADYLQAKEQQRR----LKQQIFALSEVVQRRPhfsyedavGLLGENSD 984

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  303 VGDSL---LTEKDSVKRLQDEA-EKAKKQVADF--------------EEKLKEIETEkIALIKKQEEVTIEARKSVETDD 364
Cdd:COG3096   985 LNEKLrarLEQAEEARREAREQlRQAQAQYSQYnqvlaslkssrdakQQTLQELEQE-LEELGVQADAEAEERARIRRDE 1063

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  365 hLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQeMKQLEAHYERAQKMLQDNveqmNVENRGLRDE 444
Cdd:COG3096  1064 -LHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ-VVQAKAGWCAVLRLARDN----DVERRLHRRE 1137


                  ....*
gi 922581144  445 IEKLS 449
Cdd:COG3096  1138 LAYLS 1142
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 215-337 1.51e-03

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 41.05  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   215 QLKDEIQILNKRLE--DEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKS--EIQRELDNINDHLDQVLVEKATVV 290
Cdd:pfam13870   46 QLQIENQALNEKIEerNKELKRLKLKVTNTVHALTHLKEKLHFLSAELSRLKKElrERQELLAKLRKELYRVKLERDKLR 125

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 922581144   291 QQRDDMQAELADVG-DSLLT----EKDSVKRLQDEAEKAKKQVADFEEKLKE 337
Cdd:pfam13870  126 KQNKKLRQQGGLLHvPALLHdydkTKAEVEEKRKSVKKLRRKVKILEMRIKE 177
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 39-89 1.69e-03

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: 41.96  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581144   39 SEEAKDLIRQLIC-SSDVRFG--RNGLSDFQLHPFFEGIDWNTIRDS--NPPYVPE 89
Cdd:cd05605   229 SEEAKSICSQLLQkDPKTRLGcrGEGAEDVKSHPFFKSINFKRLEAGllEPPFVPD 284
PRK12704 PRK12704
phosphodiesterase; Provisional
 307-489 1.73e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  307 LLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIalIKKQEEVtIEARKSVEtddhlsEEVVAAKNTIASLQATNEE 386
Cdd:PRK12704   23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL--LEAKEEI-HKLRNEFE------KELRERRNELQKLEKRLLQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  387 RE-------TEIKKLKQRMDEERASHTAQsEQEMKQLEAHYERAQKMLQDNVEQ---MNVE---NRGLRDEIEKLSQQMA 453
Cdd:PRK12704   94 KEenldrklELLEKREEELEKKEKELEQK-QQELEKKEEELEELIEEQLQELERisgLTAEeakEILLEKVEEEARHEAA 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 922581144  454 ALprgglneqqLHEIfnwvsEEKAtREEMENLTRKI 489
Cdd:PRK12704  173 VL---------IKEI-----EEEA-KEEADKKAKEI 193
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 140-434 1.78e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   140 LSDARSLTDEIRaiaqrcqgdaELMEKsVDGFMVELENEkaeLVQKLKEAQTIIAQHVAENPRSEEDrNYESTIAQLKDE 219
Cdd:pfam06160  181 LEKLEEETDALE----------ELMED-IPPLYEELKTE---LPDQLEELKEGYREMEEEGYALEHL-NVDKEIQQLEEQ 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   220 IQILNKRLED---EALAQQQQKPKDEIVA-------------ESEKKLKELKERNKQLVMEKSEIQRELDNIND--HLDQ 281
Cdd:pfam06160  246 LEENLALLENlelDEAEEALEEIEERIDQlydllekevdakkYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsyTLNE 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   282 VLVEKATVVQ-QRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIEtEKIALIKKQEEvtiEARKSV 360
Cdd:pfam06160  326 NELERVRGLEkQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK-ESLQSLRKDEL---EAREKL 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   361 etdDHLSEEVVAAKNTI---------ASLQATNEERETEIKKLKQRMDEERAshtaqseqEMKQLEAHYERAQKM---LQ 428
Cdd:pfam06160  402 ---DEFKLELREIKRLVeksnlpglpESYLDYFFDVSDEIEDLADELNEVPL--------NMDEVNRLLDEAQDDvdtLY 470


                   ....*.
gi 922581144   429 DNVEQM 434
Cdd:pfam06160  471 EKTEEL 476
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 169-409 1.92e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 42.90  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  169 DGFMVELENEKAELVQKLKEAQtiIAQHVAENP----------RSEEDRN-YESTIAQLKDEIQILNKRLED---EALAQ 234
Cdd:NF012221 1525 DGLGYILDNVVATSESSQQADA--VSKHAKQDDaaqnaladkeRAEADRQrLEQEKQQQLAAISGSQSQLEStdqNALET 1602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  235 QQQKPKDEIVAESEKKLKELKERNKQLVM---------EKSEIQRE------LDNINDHLD---QVLVEKATVVQQRddM 296
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTTLAQGLDAldsqatyagESGDQWRNpfagglLDRVQEQLDdakKISGKQLADAKQR--H 1680

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  297 QAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEkiALIKKQEEvtiearKSVETDDHLSEEVVAAKNT 376
Cdd:NF012221 1681 VDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDD--ALAKQNEA------QQAESDANAAANDAQSRGE 1752

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 922581144  377 IASLQATNE--ERETEIKKLKQRMDEERASHTAQS 409
Cdd:NF012221 1753 QDASAAENKanQAQADAKGAKQDESDKPNRQGAAG 1787
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 234-414 2.15e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  234 QQQQKPKDEIVAEsekklkelKERNKQLVMEKSEIQRELDNINDHLDQVlvEKATVVQQRDDMQAELAdVGDSLLTEKDS 313
Cdd:PRK09510   66 RQQQQQKSAKRAE--------EQRKKKEQQQAEELQQKQAAEQERLKQL--EKERLAAQEQKKQAEEA-AKQAALKQKQA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  314 VKRLQDEAEKAKKQvADFEEKLKEIETEKI-ALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIK 392
Cdd:PRK09510  135 EEAAAKAAAAAKAK-AEAEAKRAAAAAKKAaAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213

                         170       180
                  ....*....|....*....|..
gi 922581144  393 KLKQRMDEERASHTAQSEQEMK 414
Cdd:PRK09510  214 EAKKKAAAEAKAAAAKAAAEAK 235
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 338-501 2.17e-03

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 42.18  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  338 IETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEER----------ETEIKKLKQRMDEErashta 407
Cdd:COG5259   368 VQSEKQRAIIKSGKISHINRESQEHIEEVIEYALDSGKEKAKLQATNEERkmerlrnvliQAQLEKLKMKLGHL------ 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  408 qseqemKQLEAHYERAQKML-------QDNVEQMNVENRGLRDEIEKLSQQMaalprgglneqQLHEIFNWVSEEKATR- 479
Cdd:COG5259   442 ------KELEKSTSLERQELdanlllrRLNAEEKLFAIDEVLSKCLNLISDD-----------QGKNPDNKPSTETGENh 504

                         170       180
                  ....*....|....*....|....
gi 922581144  480 --EEMENLTrkitgEVESLKNNSP 501
Cdd:COG5259   505 lgQEISNET-----DVKPISKEAP 523
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 162-468 2.18e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  162 ELMEKsVDGFMVELENEkaeLVQKLKEAQTIIAQHVAENPRSEEDrNYESTIAQLKDEIQILNKRLEDEALaqqqqkpkd 241
Cdd:PRK04778  212 QIMEE-IPELLKELQTE---LPDQLQELKAGYRELVEEGYHLDHL-DIEKEIQDLKEQIDENLALLEELDL--------- 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  242 eivAESEKKLKELKERNKQL--VME-----KSEIQRELDNINDHLDQVLvekatvvQQRDDMQAELADVGDS-LLTEkds 313
Cdd:PRK04778  278 ---DEAEEKNEEIQERIDQLydILErevkaRKYVEKNSDTLPDFLEHAK-------EQNKELKEEIDRVKQSyTLNE--- 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  314 vkrlqDEAEKAKKqvadFEEKLKEIETEKIALIKKqeevtIEARKSVETDdhLSEEVVAAKNTIASLQATNEERETEIKK 393
Cdd:PRK04778  345 -----SELESVRQ----LEKQLESLEKQYDEITER-----IAEQEIAYSE--LQEELEEILKQLEEIEKEQEKLSEMLQG 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  394 LkqRMDEERASHTAqseQEMKQ-LEAHYERAQKM-L----QDNVEQMNVenrgLRDEIEKLSQQMAALPrggLN----EQ 463
Cdd:PRK04778  409 L--RKDELEAREKL---ERYRNkLHEIKRYLEKSnLpglpEDYLEMFFE----VSDEIEALAEELEEKP---INmeavNR 476


                  ....*
gi 922581144  464 QLHEI 468
Cdd:PRK04778  477 LLEEA 481
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 148-376 2.33e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  148 DEIRAIAQRCQGDAELMEKSVDGFMvELENEKAELVQKLKEAQTiiaqhvaenprseedRNYestiaQLKDEIQILNK-- 225
Cdd:PRK04778  282 EKNEEIQERIDQLYDILEREVKARK-YVEKNSDTLPDFLEHAKE---------------QNK-----ELKEEIDRVKQsy 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  226 RLEDEALAQQQQkpkdeivaeSEKKLKELKERNKQLVMEK-------SEIQRELDNINDHLDQvlVEKatvvqQRDDMQA 298
Cdd:PRK04778  341 TLNESELESVRQ---------LEKQLESLEKQYDEITERIaeqeiaySELQEELEEILKQLEE--IEK-----EQEKLSE 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  299 ELADVGDSLLTEKDSVKRLQDEAEKAKKQV---------ADFEEKLKEIETEKIALIKKQEEVTIEarksVETDDHLSEE 369
Cdd:PRK04778  405 MLQGLRKDELEAREKLERYRNKLHEIKRYLeksnlpglpEDYLEMFFEVSDEIEALAEELEEKPIN----MEAVNRLLEE 480


                  ....*..
gi 922581144  370 VVAAKNT 376
Cdd:PRK04778  481 ATEDVET 487
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 676-728 2.46e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410437  Cd Length: 53  Bit Score: 37.45  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  676 HNFermKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSC-PVP 728
Cdd:cd20887     3 HSF---KEKTFKKKRACAVCREPVGGQGLVCRVCKVASHKKCEAKVTSACqPPP 53
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 172-429 2.51e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   172 MVELENEKA-ELVQKLKEAQTIiaQHVAENPRSEEDRNYESTIA---QLKDEIQILNKRL------------EDEALAQQ 235
Cdd:pfam13868   82 IEEREQKRQeEYEEKLQEREQM--DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQaewkelekeeerEEDERILE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   236 QQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSlLTEKDSVK 315
Cdd:pfam13868  160 YLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK-ARQRQELQ 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   316 RLQDEAEKAKKQVADFEEKLKEIETEKIaLIKKQEEVTIEARKSvetddhlSEEVVAAKNTIASLQATNEERETEIKKLK 395
Cdd:pfam13868  239 QAREEQIELKERRLAEEAEREEEEFERM-LRKQAEDEEIEQEEA-------EKRRMKRLEHRRELEKQIEEREEQRAAER 310

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 922581144   396 QRMDEERashtaqseQEMKQLEAHYER-----AQKMLQD 429
Cdd:pfam13868  311 EEELEEG--------ERLREEEAERRErieeeRQKKLKE 341
growth_prot_Scy NF041483
polarized growth protein Scy;
139-468 2.62e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  139 LLSDARSLTDEIRAIAQrcqGDAElmeksvdgfMVELEN-EKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLK 217
Cdd:NF041483  485 LLTKAKADADELRSTAT---AESE---------RVRTEAiERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAE 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  218 DEIQILNKRLEdEALAQQQQKPKDEIV---AESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRD 294
Cdd:NF041483  553 RAARELREETE-RAIAARQAEAAEELTrlhTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQA 631

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  295 DMQAEladvgdslltekdsvkRLQDEA-EKAKKQVADFEEKLKEIETEKIAlikKQEEVTIEARksvETDDHLSEEVVAA 373
Cdd:NF041483  632 EQEAE----------------RLRTEAaADASAARAEGENVAVRLRSEAAA---EAERLKSEAQ---ESADRVRAEAAAA 689

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  374 KNTIAS-----LQATNEE-----RETE--IKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGL 441
Cdd:NF041483  690 AERVGTeaaeaLAAAQEEaarrrREAEetLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATEL 769

                         330       340
                  ....*....|....*....|....*..
gi 922581144  442 RDEIEKLSQQMAAlPRGGLNEQQLHEI 468
Cdd:NF041483  770 VSAAEQTAQQVRD-SVAGLQEQAEEEI 795
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 312-455 2.67e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   312 DSVKRLQDEAEKAKKQVADFEEKLKEIETEkialIKKQEEVTIEARKSVEtddhlsEEVVAAKNTIASLQATNEEREtei 391
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAADAEAQLQKLQED----LEKQAEIAREAQQNYE------RELVLHAEDIKALQALREELN--- 67

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581144   392 kklkqrmdeerashtaQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAAL 455
Cdd:pfam07926   68 ----------------ELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIEDL 115
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 366-453 2.88e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 38.32  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  366 LSEEVVAAKNTIASLQATNEERETEIKKLKQRMDE-ERASHTAQSEQEMKQLEAhyeraqKMLQDNVEQMNVENRGLrde 444
Cdd:cd22887     2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEkNKANEILNDELIALQIEN------NLLEEKLRKLQEENDEL--- 72


                  ....*....
gi 922581144  445 IEKLSQQMA 453
Cdd:cd22887    73 VERWMAKKQ 81
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 291-583 2.94e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   291 QQRDDMQAEladvgdsllteKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALikkQEEVTIEARKSVEtddhlseev 370
Cdd:pfam01576    2 RQEEEMQAK-----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNAL---QEQLQAETELCAE--------- 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   371 vaAKNTIASLQATNEERETEIKKLKQRMDEE--RASHTAQSEQEMKQ----LEAHY---ERAQKMLQdnVEQMNVEN--R 439
Cdd:pfam01576   59 --AEEMRARLAARKQELEEILHELESRLEEEeeRSQQLQNEKKKMQQhiqdLEEQLdeeEAARQKLQ--LEKVTTEAkiK 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   440 GLRDEIEKLSQQMAALPRgglneqqlheifnwvsEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTP------- 512
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSK----------------ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDleerlkk 198

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144   513 SGWGSRRMNNVARK---DGLDLQRQ---LQAEIDaklKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQ 583
Cdd:pfam01576  199 EEKGRQELEKAKRKlegESTDLQEQiaeLQAQIA---ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQ 272
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 207-596 3.46e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.76  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   207 RNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKdeiVAESEKKLKELKERNKQLVmekseiQRELDNINDHLDQVlvek 286
Cdd:pfam06160    6 KKIYKEIDELEERKNELMNLPVQEELSKVKKLNL---TGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA---- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   287 atvvqqrddmqAELADvgdsllteKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHL 366
Cdd:pfam06160   73 -----------EELND--------KYRFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYREL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   367 SEEvVAAKN-----TIASLQATNEERETEIKKLKQRMD-----------EERASHTAQSEQEMKQLEAHYERAQKMLQDN 430
Cdd:pfam06160  134 RKT-LLANRfsygpAIDELEKQLAEIEEEFSQFEELTEsgdylearevlEKLEEETDALEELMEDIPPLYEELKTELPDQ 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   431 VEQmnvenrgLRDEIEKLSQQMAALPRGGLnEQQLHEIFNWVSE-----EKATREEMENLTRKITGEVESLknnspltts 505
Cdd:pfam06160  213 LEE-------LKEGYREMEEEGYALEHLNV-DKEIQQLEEQLEEnlallENLELDEAEEALEEIEERIDQL--------- 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   506 nYIQntpsgwgsrrMNN--VARKDGLDLQRQLQAEID----AKLKLKAELKNSQEQYLTS---AARLDDTEKRMASLMRE 576
Cdd:pfam06160  276 -YDL----------LEKevDAKKYVEKNLPEIEDYLEhaeeQNKELKEELERVQQSYTLNeneLERVRGLEKQLEELEKR 344

                          410       420
                   ....*....|....*....|
gi 922581144   577 VAMLkqQKNIENSSdSAFSS 596
Cdd:pfam06160  345 YDEI--VERLEEKE-VAYSE 361
C1_VAV2 cd20868
protein kinase C conserved region 1 (C1 domain) found in VAV2 protein; VAV2 is widely ...
 676-723 5.04e-03

protein kinase C conserved region 1 (C1 domain) found in VAV2 protein; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410418  Cd Length: 58  Bit Score: 36.78  E-value: 5.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 922581144  676 HNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQ 723
Cdd:cd20868     6 HNFQMYTFDKTTNCKACKMLLRGTFYQGYYCSKCGAGAHKECLEVIPP 53
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 209-327 5.09e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 5.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    209 YESTIAQLKDEIQILNKRLEDEAlaQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKAT 288
Cdd:smart00787  166 ELELLNSIKPKLRDRKDALEEEL--RQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 922581144    289 VVQQRDDMQAELADVGDSLLTEK----DSVKRLQDEAEKAKKQ 327
Cdd:smart00787  244 LTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQSL 286
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 209-490 5.16e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  209 YESTIAQLKDEIQILNkrledealaqQQQKPKDEIVAESEKKLKELKERnkqlVMEKS--------EIQRELDNINDHLD 280
Cdd:PRK04778  117 IEEDIEQILEELQELL----------ESEEKNREEVEQLKDLYRELRKS----LLANRfsfgpaldELEKQLENLEEEFS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  281 Q--VLVEKATVVQQRD---DMQAELADVGDSLLTEKDSVKRLQDEAekaKKQVADFEEKLKEIETEKIALIKKQEEVTIE 355
Cdd:PRK04778  183 QfvELTESGDYVEAREildQLEEELAALEQIMEEIPELLKELQTEL---PDQLQELKAGYRELVEEGYHLDHLDIEKEIQ 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  356 ArksvetddhLSEEVVAAKNTIASLQAtnEERETEIKKLKQRMDEerasHTAQSEQEMKqleAHY--ERAQKMLQDNVEQ 433
Cdd:PRK04778  260 D---------LKEQIDENLALLEELDL--DEAEEKNEEIQERIDQ----LYDILEREVK---ARKyvEKNSDTLPDFLEH 321

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  434 MNVENRGLRDEIEKLSQQMAalprggLNEQQLHEIFNWVSEEKATREEMENLTRKIT 490
Cdd:PRK04778  322 AKEQNKELKEEIDRVKQSYT------LNESELESVRQLEKQLESLEKQYDEITERIA 372
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
207-455 5.36e-03

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 39.92  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  207 RNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLvmekseiqreldnindhldQVLVEK 286
Cdd:NF033927   10 RKSAAKIANKLDDLSQINLREATLDLLAQLQEQIAELEAQIAALESKLNELAEDR-------------------KVIIEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  287 ATVVQQRDdmqaeLADVGDSLLTEKDSVKRLQDEaeKAKKQVADFeeklkeieteKIALIKKQEEVTIEARKS---VETD 363
Cdd:NF033927   71 IDLIEKYN-----IADLFKDLLPTAEEIDSLGLP--PPEKDLVKA----------AIERLKKLLGKISEGLTYidlVEAR 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  364 DHLSEEVVAAKNTIASLQatneereTEIKKLKQRMDEERASHTAQSE-----QEMKQLEAHYERaqkmLQDNVEQMNVEN 438
Cdd:NF033927  134 DKLRDRINALLAESRTLD-------KDIKALAGKLEELTAIAAIDEEratwvAEARKVEQAWES----FLDQLTELTSDS 202

                         250
                  ....*....|....*..
gi 922581144  439 RGLRDEIEKLSQQMAAL 455
Cdd:NF033927  203 ANLAQLITQLNGFIKFL 219
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 179-262 5.74e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.14  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   179 KAELVQKLKEAQTiiAQHVAENpRSEEDrnyESTIAQLKDEIQILNKRLED--------EALAQQQQkpkDEIVA----- 245
Cdd:pfam08614   73 RGELAQRLVDLNE--ELQELEK-KLRED---ERRLAALEAERAQLEEKLKDreeelrekRKLNQDLQ---DELVAlqlql 143

                           90
                   ....*....|....*...
gi 922581144   246 -ESEKKLKELKERNKQLV 262
Cdd:pfam08614  144 nMAEEKLRKLEKENRELV 161
PRK12705 PRK12705
hypothetical protein; Provisional
 184-370 5.75e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.85  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  184 QKLKEAQTIIAQHVAENPRSEED---RNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQ 260
Cdd:PRK12705   30 RLAKEAERILQEAQKEAEEKLEAallEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  261 LVMEKSEIQRELDNINDHLDQVLVEKATvvQQRDDMQAELAdvgdslltekdsvKRLQDEAEKAKKQV--ADFEEKLKEI 338
Cdd:PRK12705  110 REKALSARELELEELEKQLDNELYRVAG--LTPEQARKLLL-------------KLLDAELEEEKAQRvkKIEEEADLEA 174

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 922581144  339 ETEKIALIKK---QEEVTIEARKSVETDDHLSEEV 370
Cdd:PRK12705  175 ERKAQNILAQamqRIASETASDLSVSVVPIPSDAM 209
mS26_Tt cd23695
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ...
 158-437 6.35e-03

Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.


Pssm-ID: 467909 [Multi-domain]  Cd Length: 496  Bit Score: 40.58  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  158 QGDAELMEKSVDGfMVELENEKAELVQKLKEAQTIIaQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLED--EALAQQ 235
Cdd:cd23695   151 QGDHEEMDKLLDE-NEEIEYKNSLLMPIYQDLKSLI-KHLKYTELFKLLKEYQDAKAIIIEDFRESSEEGAEklEKLEKA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  236 QQ---KPKDEIVAESEKKLKELKER-----------NKQLVMEKSEIQRELDNINDhlDQVLVEKATVVQQRDDMQAELA 301
Cdd:cd23695   229 FAtllKNYKEELEEPEKQLEFMQKRlldlynllrlwGQYITIVKMPDSVVRDIMNK--TQARPEVAKLNSKQELEDAKNR 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  302 DVgDSLLTEKDSVKRLQDEAEKAKKQVaDFEEKLKEIETEKialiKKQEEvtIEARKSVETDDHLSEEVVAAKNTIaslQ 381
Cdd:cd23695   307 KR-DTEENEFDDDYESADEGETSDEED-EIEEENFQLQKEK----KKEEE--LNAEFNIAKNSLYKFSPQNDKNVV---D 375

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581144  382 ATNEERETEIKKLKQRMDEERASHTAQSE-QEMKQLEAHYERaQKMLQDNVEQMNVE 437
Cdd:cd23695   376 DRDFYSGVDLENVFPRALLNNLNDFTGLDfQNVKEILNNEEK-LKIIQGEDDQNDQE 431
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 1-100 6.60e-03

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: 40.40  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLYGTTPFYSERLVDTYGKIMSHQdmLDFPDdeidwVVSEEAKDLIRQLICSSDVRF---GRNGLSDFQLHPFFEGIDWN 77
Cdd:cd05594   219 MMCGRLPFYNQDHEKLFELILMEE--IRFPR-----TLSPEAKSLLSGLLKKDPKQRlggGPDDAKEIMQHKFFAGIVWQ 291

                          90       100
                  ....*....|....*....|....*
gi 922581144   78 TIRDSN--PPYVPEVSSPEDTSNFD 100
Cdd:cd05594   292 DVYEKKlvPPFKPQVTSETDTRYFD 316
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 138-499 7.50e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.97  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  138 SLLSDARSLTDEIraIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIiaqhVAENPRSEEDrnYESTIAQLK 217
Cdd:PTZ00440  464 TLISIMKSFYDLI--ISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNI----VNNNFKNIED--YYITIEGLK 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  218 DEIQILNKRLEDealaqqqqkpkdeivaeSEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQV--LVEKATVVQQRDD 295
Cdd:PTZ00440  536 NEIEGLIELIKY-----------------YLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIkdIISLNDEIDNIIQ 598

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  296 MQAELadVGDSLLTEKDSVKRLQDEAEKAKKQVADF-EEKLKEIETEKIALIKKQEEVTIEArKSVETDDHLSEEVVAAK 374
Cdd:PTZ00440  599 QIEEL--INEALFNKEKFINEKNDLQEKVKYILNKFyKGDLQELLDELSHFLDDHKYLYHEA-KSKEDLQTLLNTSKNEY 675

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  375 NTIASLQATN-----EERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDE----I 445
Cdd:PTZ00440  676 EKLEFMKSDNidniiKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYkhqiI 755

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 922581144  446 EKLSQQMAALPRgglNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNN 499
Cdd:PTZ00440  756 NRKNEFILHLYE---NDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKEN 806
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 256-435 7.70e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 38.05  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   256 ERNKQLVMEK-SEIQRELDNINDHLDqvlvekatvvqqrdDMQAELADVGDSLltekdsvKRLQDEAEKAKKQVADFEEK 334
Cdd:pfam10473    2 EKKQLHVLEKlKESERKADSLKDKVE--------------NLERELEMSEENQ-------ELAILEAENSKAEVETLKAE 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   335 LKEIETEKIALikKQEEVTIEARKsvetdDHLSEEVVAAKNTIASLQATNEERETEIKKLkqrmdeerashtaqsEQEMK 414
Cdd:pfam10473   61 IEEMAQNLRDL--ELDLVTLRSEK-----ENLTKELQKKQERVSELESLNSSLENLLEEK---------------EQEKV 118

                          170       180
                   ....*....|....*....|.
gi 922581144   415 QLEAHYERAQKMLQDNVEQMN 435
Cdd:pfam10473  119 QMKEESKTAVEMLQTQLKELN 139
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 59-141 7.89e-03

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: 40.02  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   59 RNGLSDFQLHPFFEGIDWNTIRDSN--PPYVPEVSSPEDTSNFDVDVCEDdftPCETQPPRVLAAFTGNHLPFVGFSYTH 136
Cdd:cd05618   278 QTGFADIQGHPFFRNVDWDLMEQKQvvPPFKPNISGEFGLDNFDSQFTNE---PVQLTPDDDDIVRKIDQSEFEGFEYIN 354


                  ....*
gi 922581144  137 GSLLS 141
Cdd:cd05618   355 PLLMS 359
Caldesmon pfam02029
Caldesmon;
151-431 8.02e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   151 RAIAQRCQGDAELMEKSVD-GFMVELENEKAELVQK---LKEAQTIIAQHVAE------NPRSEEDRNYESTIAQLKDEI 220
Cdd:pfam02029   77 KRLQEALERQKEFDPTIADeKESVAERKENNEEEENsswEKEEKRDSRLGRYKeeeteiREKEYQENKWSTEVRQAEEEG 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   221 QilnkrLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMeKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAEL 300
Cdd:pfam02029  157 E-----EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYES-KVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGL 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   301 ADVGDsllTEKDSVKRLqdEAEKAKKQVADFEEKLKEIETEKiaLIKKQEEVTIEarksvetddhlseevvaakntIASL 380
Cdd:pfam02029  231 SQSQE---REEEAEVFL--EAEQKLEELRRRRQEKESEEFEK--LRQKQQEAELE---------------------LEEL 282

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   381 QATNEERETEIKKLKQRMDEERASHTAQSEQE---MKQ------LEAhYERAQKMLQDNV 431
Cdd:pfam02029  283 KKKREERRKLLEEEEQRRKQEEAERKLREEEEkrrMKEeierrrAEA-AEKRQKLPEDSS 341
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 215-466 8.20e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.05  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   215 QLKDEIQilnkRLEDeaLAQQQQKpkdEIVAESEKKLkELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRD 294
Cdd:pfam15742   17 QLRQNLQ----RLQI--LCTSAEK---ELRYERGKNL-DLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   295 DMQAELADVGDSLLTEKDSVKR---LQDEAEKAKKQVADFEEKLKEIETE-KIALIKKQEEVTIEARKSVEtddhlsEEV 370
Cdd:pfam15742   87 HCQQKIRELELEVLKQAQSIKSqnsLQEKLAQEKSRVADAEEKILELQQKlEHAHKVCLTDTCILEKKQLE------ERI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   371 VAAKNTIASLQATNEERETEIKKLKQRMDE--------------------ERASHTAQSEQEMKQLEAH---YERAQKML 427
Cdd:pfam15742  161 KEASENEAKLKQQYQEEQQKRKLLDQNVNElqqqvrslqdkeaqlemtnsQQQLRIQQQEAQLKQLENEkrkSDEHLKSN 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 922581144   428 QDNVEQMNV---ENRGLRDEIEKLSQQMAALPRgGLNEQQLH 466
Cdd:pfam15742  241 QELSEKLSSlqqEKEALQEELQQVLKQLDVHVR-KYNEKHHH 281
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 209-455 9.36e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 9.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   209 YESTIAQLK-------DEIQILNKRLEDEALA-----------QQQQKpkdEIVAESEKKLKELKERNkqlvMEKSE--I 268
Cdd:pfam02841   52 YEQQMAQKVklptetlQELLDLHRDCEKEAIAvfmkrsfkdenQEFQK---ELVELLEAKKDDFLKQN----EEASSkyC 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   269 QRELDNINDHLDQVLVEKATVVQ--QRDDMQAEladvgDSLLTEKDSVKRlqdeaeKAKKQVADFEEKLKEIETEKIALI 346
Cdd:pfam02841  125 SALLQDLSEPLEEKISQGTFSKPggYKLFLEER-----DKLEAKYNQVPR------KGVKAEEVLQEFLQSKEAVEEAIL 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   347 KKQEEVTIEARKSvetddhlseEVVAAKNtiASLQATNEERETEIKKLKQRMDEERAS---HTAQSEQEMKQLEAHYERA 423
Cdd:pfam02841  194 QTDQALTAKEKAI---------EAERAKA--EAAEAEQELLREKQKEEEQMMEAQERSyqeHVKQLIEKMEAEREQLLAE 262

                          250       260       270
                   ....*....|....*....|....*....|....
gi 922581144   424 QKMLQDNVEQMNVE--NRGLRDEIEKLSQQMAAL 455
Cdd:pfam02841  263 QERMLEHKLQEQEEllKEGFKTEAESLQKEIQDL 296
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
 59-146 9.50e-03

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: 40.00  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144   59 RNGLSDFQLHPFFEGIDWNTIRDSN--PPYVPEVSSPEDTSNFDVDVCEDdftPCETQPPRVLAAFTGNHLPFVGFSYTH 136
Cdd:cd05617   271 QTGFSDIKSHTFFRSIDWDLLEKKQvtPPFKPQITDDYGLENFDTQFTSE---PVQLTPDDEDVIKRIDQSEFEGFEYIN 347

                          90
                  ....*....|
gi 922581144  137 GSLLSDARSL 146
Cdd:cd05617   348 PLLLSTEETV 357
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 265-450 9.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  265 KSEIQRELDNINDhldqvLVEKatVVQQRDDMQAELADVgdslltekdsvKRLQDEAEKAKKQVADFEEKLKEIETEkia 344
Cdd:PRK00409  508 KKLIGEDKEKLNE-----LIAS--LEELERELEQKAEEA-----------EALLKEAEKLKEELEEKKEKLQEEEDK--- 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144  345 LIKKQEEvtiEARKSVEtddhlseevvAAKntiaslqatnEERETEIKKLKQRMDEERASHTAQSEQEM-KQLEAHYERA 423
Cdd:PRK00409  567 LLEEAEK---EAQQAIK----------EAK----------KEADEIIKELRQLQKGGYASVKAHELIEArKRLNKANEKK 623

                         170       180
                  ....*....|....*....|....*..
gi 922581144  424 QKMLQDNVEQMNVENRGLRDEIEKLSQ 450
Cdd:PRK00409  624 EKKKKKQKEKQEELKVGDEVKYLSLGQ 650
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
 1-88 9.94e-03

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: 39.34  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581144    1 MLY----GTTPFYSERLVDTYgKI--MSHQDMLDFPDDeidwvVSEEAKDLIRQLIcSSDV--RFG--RNGLSDFQLHPF 70
Cdd:cd05606   186 MLYkllkGHSPFRQHKTKDKH-EIdrMTLTMNVELPDS-----FSPELKSLLEGLL-QRDVskRLGclGRGATEVKEHPF 258

                          90       100
                  ....*....|....*....|
gi 922581144   71 FEGIDWNTI--RDSNPPYVP 88
Cdd:cd05606   259 FKGVDWQQVylQKYPPPLIP 278
 
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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