|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-416 |
1.71e-105 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 324.64 E-value: 1.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 373
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13027660 374 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
214-414 |
4.62e-98 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 304.92 E-value: 4.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 373
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13027660 374 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 414
Cdd:cd04269 157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
510-652 |
1.04e-54 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 185.64 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13027660 590 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 652
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
510-620 |
1.33e-41 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 147.38 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|.
gi 13027660 590 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 620
Cdd:pfam08516 80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
60-159 |
4.79e-31 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 118.19 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTvilGHCYYHGHVRGYSDSAVSLSTCS 139
Cdd:pfam01562 19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT---DHCYYQGHVEGHPDSSVALSTCS 95
|
90 100
....*....|....*....|
gi 13027660 140 GLRGLIVFENESYVLEPMKS 159
Cdd:pfam01562 96 GLRGFIRTENEEYLIEPLEK 115
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
439-507 |
2.21e-29 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 111.63 E-value: 2.21e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13027660 439 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 507
Cdd:smart00050 7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
443-505 |
4.95e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 107.71 E-value: 4.95e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13027660 443 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 505
Cdd:pfam00200 11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
754-905 |
8.18e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 754 PSRPPRGFQPCQAHLGHLGKG--LMRKPPdSYPPKDNPRRLLQCQNVDISRPlnglnVPQPQSTQRVLPPLHRA-PRAPS 830
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGgdVRRRPP-SRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPErPPQPQ 2912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 831 VPARPLPAKPALRQAQGTckPNPPQKPLPADPLARTTRLTHAL------------ARTPGQWETGLRLAPlRPAPQYPHQ 898
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQ--PPPPPPPRPQPPLAPTTDPAGAGepsgavpqpwlgALVPGRVAVPRFRVP-QPAPSREAP 2989
|
....*..
gi 13027660 899 VPrSTHT 905
Cdd:PHA03247 2990 AS-STPP 2995
|
|
| SVAGG |
NF038115 |
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ... |
288-400 |
3.07e-04 |
|
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.
Pssm-ID: 468358 [Multi-domain] Cd Length: 407 Bit Score: 44.00 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 288 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 366
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197
|
90 100 110
....*....|....*....|....*....|....
gi 13027660 367 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 400
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
779-871 |
2.15e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 38.91 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 779 PPDSYPPKDNPrrllqcqNVDISRPLnGLNVPQPQSTQRVLPPLHrAPRAPSVPARPLPAKPALRQAQGTckPNPPQKPL 858
Cdd:pfam12526 31 PPESAHPDPPP-------PVGDPRPP-VVDTPPPVSAVWVLPPPS-EPAAPEPDLVPPVTGPAGPPSPLA--PPAPAQKP 99
|
90
....*....|...
gi 13027660 859 PADPLARTTRLTH 871
Cdd:pfam12526 100 PLPPPRPQRRLLH 112
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-416 |
1.71e-105 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 324.64 E-value: 1.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 373
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13027660 374 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
214-414 |
4.62e-98 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 304.92 E-value: 4.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 293
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 294 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 373
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13027660 374 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 414
Cdd:cd04269 157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
510-652 |
1.04e-54 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 185.64 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13027660 590 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 652
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
510-620 |
1.33e-41 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 147.38 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 510 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 589
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|.
gi 13027660 590 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 620
Cdd:pfam08516 80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
214-405 |
3.84e-34 |
|
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239795 Cd Length: 192 Bit Score: 129.46 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYR----PLNIRIVLVGVEVWN--DMDKcSVSQDPFTSLHEFL 287
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKgeQFAP-PIDSDASNTLNSFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 288 DWRKMKllpRKSHDNAQLVSGVYF-QGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAaVTLAHELGHNFGMNHDtlDRG 366
Cdd:cd04267 80 FWRAEG---PIRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTA-LTMAHELGHNLGAEHD--GGD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 13027660 367 CSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLE 405
Cdd:cd04267 154 ELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
214-413 |
3.53e-33 |
|
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.
Pssm-ID: 239801 Cd Length: 207 Bit Score: 127.35 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFQRQGKdlEKVKQRLIEIANHVDKFYR-PL---NIRIVLVGVEVWNDMDK-CSVSQDPFTSLHEFLD 288
Cdd:cd04273 1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 289 WRKmKLLPR-----KSHDNAQLVSGVYFQG-----TTIGMAPIMSMCTADQSGGIVmdhSDNPLGAAVTLAHELGHNFGM 358
Cdd:cd04273 79 WQK-KLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELGHVLGM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13027660 359 NHDTLDRGCScqmAVEKGGCIMNASTGYPF-PMVFSSCSRKDLETSLEKGMGVCLF 413
Cdd:cd04273 155 PHDGDGNSCG---PEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
60-159 |
4.79e-31 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 118.19 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTvilGHCYYHGHVRGYSDSAVSLSTCS 139
Cdd:pfam01562 19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT---DHCYYQGHVEGHPDSSVALSTCS 95
|
90 100
....*....|....*....|
gi 13027660 140 GLRGLIVFENESYVLEPMKS 159
Cdd:pfam01562 96 GLRGFIRTENEEYLIEPLEK 115
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
439-507 |
2.21e-29 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 111.63 E-value: 2.21e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13027660 439 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 507
Cdd:smart00050 7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
443-505 |
4.95e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 107.71 E-value: 4.95e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13027660 443 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 505
Cdd:pfam00200 11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
212-385 |
3.59e-19 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 86.32 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 212 ATKYVELVIVADNrEFqRQGKDLEKVKQRLIEIANHVD-KFYRPLNIRIVLVGVEVWNDMD----KCSVSQDPFTSLHEF 286
Cdd:pfam13688 1 STRTVALLVAADC-SY-VAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 287 LD---WRKmkllpRKSHDNAQLVSGVYFQGTtiGMAPIMSMCTADQSGGIVMDHSDN-----PLGAAVTLAHELGHNFGM 358
Cdd:pfam13688 79 QDfsaWRG-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNnvvvsTATEWQVFAHEIGHNFGA 151
|
170 180 190
....*....|....*....|....*....|...
gi 13027660 359 NHD----TLDRGCSCQMAVEKGG--CIMNASTG 385
Cdd:pfam13688 152 VHDcdssTSSQCCPPSNSTCPAGgrYIMNPSSS 184
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
214-398 |
8.87e-18 |
|
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.
Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 81.80 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 214 KYVELVIVADNREFqrqgkDLEKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwndmdkcsvsqdpftslhefldwrkm 292
Cdd:cd00203 1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 293 kllprKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMA 372
Cdd:cd00203 50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDH-DRKDRDDYP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13027660 373 VEK---------GGCIMNA-----STGYPFPmvFSSCSRK 398
Cdd:cd00203 124 TIDdtlnaedddYYSVMSYtkgsfSDGQRKD--FSQCDID 161
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
241-361 |
2.24e-13 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 67.40 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 241 LIEIANHVdkFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMkllpRKSHDNA---QLVSGVYFQGTTiG 317
Cdd:pfam13582 6 LVNRANTI--YERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-G 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 13027660 318 MAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHD 361
Cdd:pfam13582 79 IAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
218-411 |
1.92e-10 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 62.01 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 218 LVIVADNREFQRQGKDLEK-VKQRLIEIANHVDKFYRPL--------NIRIVLVGVEVwNDMDKCSVSQDPFTSlHEFLD 288
Cdd:cd04270 5 LLLVADHRFYKYMGRGEEEtTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRI-HTTPDEVDPGNKFYN-KSFPN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 289 WRKMKLLPRKSHDN-------AQLVSGVYFQGTTIGMAPIMSMcTADQSGGIVMDHSDNPLG------------------ 343
Cdd:cd04270 83 WGVEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGSP-RDNSAGGICEKAYYYSNGkkkylntgltttvnygkr 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13027660 344 -----AAVTLAHELGHNFGMNHDTldRGCSCQMAVEKGG-CIMNAS--TGY-PFPMVFSSCSRKDLETSLEKGMGVC 411
Cdd:cd04270 162 vptkeSDLVTAHELGHNFGSPHDP--DIAECAPGESQGGnYIMYARatSGDkENNKKFSPCSKKSISKVLEVKSNSC 236
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
215-399 |
3.47e-10 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 60.83 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 215 YVELVIVADnREFQRQGKDLEKVKQRLIEIANHVDKFYRPLN---IRIVLVGVEVWNDMDKCSVSQ-------DPFTSLH 284
Cdd:cd04272 2 YPELFVVVD-YDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHpinygyiDAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 285 EFLDWRKMKLLPRKShDNAQLVSG----VYFQGT----TIGMAPIMSMCTADqsgGIVMDHsDNP--LGAAVTLAHELGH 354
Cdd:cd04272 81 NFNEYVKKKRDYFNP-DVVFLVTGldmsTYSGGSlqtgTGGYAYVGGACTEN---RVAMGE-DTPgsYYGVYTMTHELAH 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13027660 355 NFGMNHDTLDRGCSCQMAVEKGGC------IMNASTGYPFPMVFSSCSRKD 399
Cdd:cd04272 156 LLGAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQ 206
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
213-396 |
2.82e-08 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 404471 Cd Length: 203 Bit Score: 54.93 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 213 TKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFY-RPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRK 291
Cdd:pfam13583 1 TRRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 292 MKL---LPRKSHDNAQLVSGVYFQGTTIGMAPIMSMC-TADQS--GGIVMDHSDNPlgaaVTLAHELGHNFGMNHDTLDR 365
Cdd:pfam13583 81 ATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakASGVARSRDEW----DIFAHEIGHTFGAVHDCSSQ 156
|
170 180 190
....*....|....*....|....*....|...
gi 13027660 366 GCSCQMAVE--KGGCIMNASTGYPFPMvFSSCS 396
Cdd:pfam13583 157 GEGLSSSTEdgSGQTIMSYASTASQTA-FSPCT 188
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
237-405 |
7.94e-07 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 372637 Cd Length: 193 Bit Score: 50.32 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 237 VKQRLIEIANHVDKFYRP--LNIRIVLVGV----------EVWNDmdKCSVSQDPFTSLHEFLDWRKmkllpRKSHDNAQ 304
Cdd:pfam13574 3 VTENLVNVVNRVNQIYEPddININGGLVNPgeipattsasDSGNN--YCNSPTTIVRRLNFLSQWRG-----EQDYCLAH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 305 LVSGVYFQGTTIGMAPIMSMCTADQS---------GGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMAVEK 375
Cdd:pfam13574 76 LVTMGTFSGGELGLAYVGQICQKGASspktntglsTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDC-DGSQYASSGCER 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 13027660 376 GGCIMNASTGYPFPM---------VFSSCSRKDLETSLE 405
Cdd:pfam13574 155 NAATSVCSANGSFIMnpasksnndLFSPCSISLICDVLG 193
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
754-905 |
8.18e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 754 PSRPPRGFQPCQAHLGHLGKG--LMRKPPdSYPPKDNPRRLLQCQNVDISRPlnglnVPQPQSTQRVLPPLHRA-PRAPS 830
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGgdVRRRPP-SRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPErPPQPQ 2912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 831 VPARPLPAKPALRQAQGTckPNPPQKPLPADPLARTTRLTHAL------------ARTPGQWETGLRLAPlRPAPQYPHQ 898
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQ--PPPPPPPRPQPPLAPTTDPAGAGepsgavpqpwlgALVPGRVAVPRFRVP-QPAPSREAP 2989
|
....*..
gi 13027660 899 VPrSTHT 905
Cdd:PHA03247 2990 AS-STPP 2995
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
750-892 |
2.93e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 750 RCVRPSRPPRGFQP--CQAHLGHLgKGLMRKPPDSYPPKDNPRRLLQcqnvdiSRPLNglnvPQPQSTQRVLPPLHRAPR 827
Cdd:PHA03247 2672 RAAQASSPPQRPRRraARPTVGSL-TSLADPPPPPPTPEPAPHALVS------ATPLP----PGPAAARQASPALPAAPA 2740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13027660 828 APSVPARPL----PAKPALRQA-QGTCKPNPPQKPlPADPLARTTR-----LTHALARTPGQWETGLRLAPLRPA 892
Cdd:PHA03247 2741 PPAVPAGPAtpggPARPARPPTtAGPPAPAPPAAP-AAGPPRRLTRpavasLSESRESLPSPWDPADPPAAVLAP 2814
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
235-412 |
1.51e-05 |
|
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.
Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 47.03 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 235 EKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwNDMDKCS--VSQDPFTS-----------LHEFLDWRKmkllPRKSH 300
Cdd:cd04271 21 EEARRNILNNVNSASQLYEsSFNISLGLRNLTI-SDASCPStaVDSAPWNLpcnsrididdrLSIFSQWRG----QQPDD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 301 DNA--QLVSGVYfQGTTIGMAPIMSMCTADQSGGIVMDHSdNPLGAAVT------LAHELGHNFGMNHDTlDRGCSCQMA 372
Cdd:cd04271 96 GNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDC-TSGTCSDGS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13027660 373 VEKGGC--------------IMNASTGYPFpMVFSSCSRKDLETSLEKG--MGVCL 412
Cdd:cd04271 173 VGSQQCcplststcdangqyIMNPSSSSGI-TEFSPCTIGNICSLLGRNpvRTSCL 227
|
|
| SVAGG |
NF038115 |
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ... |
288-400 |
3.07e-04 |
|
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.
Pssm-ID: 468358 [Multi-domain] Cd Length: 407 Bit Score: 44.00 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 288 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 366
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197
|
90 100 110
....*....|....*....|....*....|....
gi 13027660 367 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 400
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
750-893 |
4.24e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 750 RCVRPSRPPRGFQPcQAHLGHLGKGLMRKPPDSYPPKDNPRR------------LLQCQNVDISRPLNGLNVPQPQ--ST 815
Cdd:PHA03247 2585 RARRPDAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPDppppspspaanePDPHPPPTVPPPERPRDDPAPGrvSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 816 QRVLPPLHRAPRAPSVPARPLPakPALRQAQGTCK-----PNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLR 890
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP 2741
|
...
gi 13027660 891 PAP 893
Cdd:PHA03247 2742 PAV 2744
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
779-871 |
2.15e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 38.91 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027660 779 PPDSYPPKDNPrrllqcqNVDISRPLnGLNVPQPQSTQRVLPPLHrAPRAPSVPARPLPAKPALRQAQGTckPNPPQKPL 858
Cdd:pfam12526 31 PPESAHPDPPP-------PVGDPRPP-VVDTPPPVSAVWVLPPPS-EPAAPEPDLVPPVTGPAGPPSPLA--PPAPAQKP 99
|
90
....*....|...
gi 13027660 859 PADPLARTTRLTH 871
Cdd:pfam12526 100 PLPPPRPQRRLLH 112
|
|
| |
