|
Name |
Accession |
Description |
Interval |
E-value |
| yieM |
PRK10997 |
ATPase RavA stimulator ViaA; |
1-471 |
0e+00 |
|
ATPase RavA stimulator ViaA;
Pssm-ID: 236815 [Multi-domain] Cd Length: 487 Bit Score: 881.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 1 MTLDMLNVMLAVGEEGMIDEMLLALLAAPQLAVFFEKFPRLKNIIAADIPRWREAVRSRLKETNVPPELDAEVQCYQQSQ 80
Cdd:PRK10997 2 LTLDTLNLLLAISESGLIEEMIIALLASPQLAVFFEKFPRLKRALTKDLPRWREALRQRLKDACVPPELAEEFALYQQSQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 81 RLSTSQFIVQLPQILSQLHKLHSPFASQAQQLVDN----NSTFTPALHTLFLQRWRLSLVVQATSLNQQLLDEERDQLLS 156
Cdd:PRK10997 82 LLSTPQFIVQLPDILDKLHRLHSPFAEQARQLVDAnkgaNSPITSALHTLFLQRWRLSLVVQTTTLNQQLLEQEREQLLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 157 EVQERMTLSGQLEPVLVENDNAAGHLWDMSAGELKRGDYQLIVRYGDFLSQQPELMQLAEQLGRSREAKAVPKKDAPMET 236
Cdd:PRK10997 162 ELQQRMTLSGQLEPVLAENDEAAGRLWDMSAGQLKRGDYQLIVQYGEFLKQQPELQKLAEQLGRSREAKSVPRNDAPMET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 237 FRSLVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEFEFYRKLVEKQLLTYRLHGDAWKEKITERPVTRQDVDEQ 316
Cdd:PRK10997 242 FRTMVREPDTVPEQVVGIHQSDDILRLLPPELATLGIPELEYEFYRRLVEKRLLTYRLQGESWREKTVERPVVHQDQDEQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 317 PRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSSEVVHYELTGPQGLEQAIRFLSQRFRGGTDLAS 396
Cdd:PRK10997 322 PRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRIALAENRRCYIMLFSTEVVTYELTGPDGLEQAIRFLSQSFRGGTDLAP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730469733 397 CFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGELQHKHQHRFHAVAMSVHGKPGIMRVFDHIWRFDTG 471
Cdd:PRK10997 402 CLRAIIEKMQGREWFDADAVVISDFIAQRLPDELVAKVKELQRQHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTG 476
|
|
| VWA_YIEM_type |
cd01462 |
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
319-466 |
9.36e-56 |
|
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.
Pssm-ID: 238739 [Multi-domain] Cd Length: 152 Bit Score: 182.55 E-value: 9.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 319 GPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSSEVVHYELTGPQGLEQAIRFLS-QRFRGGTDLASC 397
Cdd:cd01462 1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVEFLSgVQLGGGTDINKA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730469733 398 FRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVgELQHKHQHRFHAVAMSVHGKPGIMRVFDHIW 466
Cdd:cd01462 81 LRYALELIERRDPRKADIVLITDGYEGGVSDELLREV-ELKRSRVARFVALALGDHGNPGYDRISAEDE 148
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
210-460 |
1.79e-48 |
|
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];
Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 167.55 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 210 ELMQLAEQLGRSREAKAVPKKDAPMETFRSLVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEFEFYRKLVEKQL 289
Cdd:COG2425 8 AARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 290 LTYRLHGDAWKEKITERPVTRQDVDEQP--RGPFIVCVDTSGSMGGFNEQCAKAFCLALMRvALADNRRCFIMLFSSEVV 367
Cdd:COG2425 88 LLLAVLLLALLLLAALLLLAAPASAAVPllEGPVVLCVDTSGSMAGSKEAAAKAAALALLR-ALRPNRRFGVILFDTEVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 368 -HYELTGPQGLEQAIRFLSQRF-RGGTDLASCFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGelQHKHQHRF 445
Cdd:COG2425 167 eDLPLTADDGLEDAIEFLSGLFaGGGTDIAPALRAALELLEEPDYRNADIVLITDGEAGVSPEELLREVR--AKESGVRL 244
|
250
....*....|....*
gi 1730469733 446 HAVAMSVHGKPGIMR 460
Cdd:COG2425 245 FTVAIGDAGNPGLLE 259
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
321-469 |
4.61e-14 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 70.18 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 321 FIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNR--RCFIMLFSSEVVHY----ELTGPQGLEQAIRFLSQRFRGGTDL 394
Cdd:smart00327 2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdRVGLVTFSDDARVLfplnDSRSKDALLEALASLSYKLGGGTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 395 ASCFRAVIERMQNPQ-----WVDADAVVISDFIAQRLPDEvINKVGELQHKHQHRFHAVAMSVHGKPGIMRVFDHIWRFD 469
Cdd:smart00327 82 GAALQYALENLFSKSagsrrGAPKVVILITDGESNDGPKD-LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
304-457 |
4.36e-08 |
|
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA (von Willebrand factor type A) domain. The exact function of this family is unknown. It is found as part of a CO oxidising (Cox) system operon is several bacteria.
Pssm-ID: 399053 [Multi-domain] Cd Length: 221 Bit Score: 53.55 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 304 TERPVTRQDVDEQPRgPFIVCVDTSGSMGGFNeqcakAFCLALMRVALADNRRCFIMLFSSEVVhyELTG---PQGLEQA 380
Cdd:pfam05762 43 PVELVRRKPRKRRPW-RLVLLLDVSGSMSDYS-----RVFLALMHALLRQRPRTRVFAFSTRLT--DLTRqlrERDPDEA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 381 IRFLSQRFR---GGTDLASCFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGELqHKHQHRFHAV-AMSVHGKP 456
Cdd:pfam05762 115 LRRVSARVEdwgGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREELLAEVARL-RRRARRLVWLnPLPDLRWP 193
|
.
gi 1730469733 457 G 457
Cdd:pfam05762 194 G 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| yieM |
PRK10997 |
ATPase RavA stimulator ViaA; |
1-471 |
0e+00 |
|
ATPase RavA stimulator ViaA;
Pssm-ID: 236815 [Multi-domain] Cd Length: 487 Bit Score: 881.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 1 MTLDMLNVMLAVGEEGMIDEMLLALLAAPQLAVFFEKFPRLKNIIAADIPRWREAVRSRLKETNVPPELDAEVQCYQQSQ 80
Cdd:PRK10997 2 LTLDTLNLLLAISESGLIEEMIIALLASPQLAVFFEKFPRLKRALTKDLPRWREALRQRLKDACVPPELAEEFALYQQSQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 81 RLSTSQFIVQLPQILSQLHKLHSPFASQAQQLVDN----NSTFTPALHTLFLQRWRLSLVVQATSLNQQLLDEERDQLLS 156
Cdd:PRK10997 82 LLSTPQFIVQLPDILDKLHRLHSPFAEQARQLVDAnkgaNSPITSALHTLFLQRWRLSLVVQTTTLNQQLLEQEREQLLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 157 EVQERMTLSGQLEPVLVENDNAAGHLWDMSAGELKRGDYQLIVRYGDFLSQQPELMQLAEQLGRSREAKAVPKKDAPMET 236
Cdd:PRK10997 162 ELQQRMTLSGQLEPVLAENDEAAGRLWDMSAGQLKRGDYQLIVQYGEFLKQQPELQKLAEQLGRSREAKSVPRNDAPMET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 237 FRSLVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEFEFYRKLVEKQLLTYRLHGDAWKEKITERPVTRQDVDEQ 316
Cdd:PRK10997 242 FRTMVREPDTVPEQVVGIHQSDDILRLLPPELATLGIPELEYEFYRRLVEKRLLTYRLQGESWREKTVERPVVHQDQDEQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 317 PRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSSEVVHYELTGPQGLEQAIRFLSQRFRGGTDLAS 396
Cdd:PRK10997 322 PRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRIALAENRRCYIMLFSTEVVTYELTGPDGLEQAIRFLSQSFRGGTDLAP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730469733 397 CFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGELQHKHQHRFHAVAMSVHGKPGIMRVFDHIWRFDTG 471
Cdd:PRK10997 402 CLRAIIEKMQGREWFDADAVVISDFIAQRLPDELVAKVKELQRQHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTG 476
|
|
| VWA_YIEM_type |
cd01462 |
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
319-466 |
9.36e-56 |
|
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.
Pssm-ID: 238739 [Multi-domain] Cd Length: 152 Bit Score: 182.55 E-value: 9.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 319 GPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSSEVVHYELTGPQGLEQAIRFLS-QRFRGGTDLASC 397
Cdd:cd01462 1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVEFLSgVQLGGGTDINKA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730469733 398 FRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVgELQHKHQHRFHAVAMSVHGKPGIMRVFDHIW 466
Cdd:cd01462 81 LRYALELIERRDPRKADIVLITDGYEGGVSDELLREV-ELKRSRVARFVALALGDHGNPGYDRISAEDE 148
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
210-460 |
1.79e-48 |
|
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];
Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 167.55 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 210 ELMQLAEQLGRSREAKAVPKKDAPMETFRSLVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEFEFYRKLVEKQL 289
Cdd:COG2425 8 AARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 290 LTYRLHGDAWKEKITERPVTRQDVDEQP--RGPFIVCVDTSGSMGGFNEQCAKAFCLALMRvALADNRRCFIMLFSSEVV 367
Cdd:COG2425 88 LLLAVLLLALLLLAALLLLAAPASAAVPllEGPVVLCVDTSGSMAGSKEAAAKAAALALLR-ALRPNRRFGVILFDTEVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 368 -HYELTGPQGLEQAIRFLSQRF-RGGTDLASCFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGelQHKHQHRF 445
Cdd:COG2425 167 eDLPLTADDGLEDAIEFLSGLFaGGGTDIAPALRAALELLEEPDYRNADIVLITDGEAGVSPEELLREVR--AKESGVRL 244
|
250
....*....|....*
gi 1730469733 446 HAVAMSVHGKPGIMR 460
Cdd:COG2425 245 FTVAIGDAGNPGLLE 259
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
321-469 |
4.61e-14 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 70.18 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 321 FIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNR--RCFIMLFSSEVVHY----ELTGPQGLEQAIRFLSQRFRGGTDL 394
Cdd:smart00327 2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdRVGLVTFSDDARVLfplnDSRSKDALLEALASLSYKLGGGTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 395 ASCFRAVIERMQNPQ-----WVDADAVVISDFIAQRLPDEvINKVGELQHKHQHRFHAVAMSVHGKPGIMRVFDHIWRFD 469
Cdd:smart00327 82 GAALQYALENLFSKSagsrrGAPKVVILITDGESNDGPKD-LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
322-449 |
6.62e-09 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 54.88 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 322 IVCVDTSGSMGGFNEQCAKAFCLALMR--VALADNRRCFIMLFSSEV-VHYELTGPQG---LEQAIRFLSQRFRGGTDLA 395
Cdd:cd00198 4 VFLLDVSGSMGGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNArVVLPLTTDTDkadLLEAIDALKKGLGGGTNIG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730469733 396 SCFRAVIERMQNPQWVDADAVVI--SDFIAQRLPDEVINKVGELQhKHQHRFHAVA 449
Cdd:cd00198 84 AALRLALELLKSAKRPNARRVIIllTDGEPNDGPELLAEAARELR-KLGITVYTIG 138
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
304-457 |
4.36e-08 |
|
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA (von Willebrand factor type A) domain. The exact function of this family is unknown. It is found as part of a CO oxidising (Cox) system operon is several bacteria.
Pssm-ID: 399053 [Multi-domain] Cd Length: 221 Bit Score: 53.55 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 304 TERPVTRQDVDEQPRgPFIVCVDTSGSMGGFNeqcakAFCLALMRVALADNRRCFIMLFSSEVVhyELTG---PQGLEQA 380
Cdd:pfam05762 43 PVELVRRKPRKRRPW-RLVLLLDVSGSMSDYS-----RVFLALMHALLRQRPRTRVFAFSTRLT--DLTRqlrERDPDEA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 381 IRFLSQRFR---GGTDLASCFRAVIERMQNPQWVDADAVVISDFIAQRLPDEVINKVGELqHKHQHRFHAV-AMSVHGKP 456
Cdd:pfam05762 115 LRRVSARVEdwgGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREELLAEVARL-RRRARRLVWLnPLPDLRWP 193
|
.
gi 1730469733 457 G 457
Cdd:pfam05762 194 G 194
|
|
| YeaD2 |
COG1721 |
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown]; |
304-422 |
1.24e-06 |
|
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
Pssm-ID: 441327 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 304 TERPVTRQDVDEQPRgPFIVCVDTSGSMGGFNEQCAK-----AFCLALMRVALADNRRCFIMLFSSEVVHY--ELTGPQG 376
Cdd:COG1721 134 TGELYVREFEEEREL-TVVLLLDTSASMRFGSGGPSKldlavEAAASLAYLALRQGDRVGLLTFGDRVRRYlpPRRGRRH 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1730469733 377 LEQAIRFLSQ-RFRGGTDLASCFRAVIERMQNpqwvDADAVVISDFI 422
Cdd:COG1721 213 LLRLLEALARlEPAGETDLAAALRRLARRLPR----RSLVVLISDFL 255
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
321-418 |
2.00e-05 |
|
von Willebrand factor type A domain;
Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 43.43 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 321 FIVCVDTSGSMGG-----FNEQCAKAFCLALMrvALADNRRCFIMLFSSEV-VHYELT-GPQGLEQAIRFLsQRFRGGTD 393
Cdd:pfam13519 1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALL--KSLPGDRVGLVTFGDGPeVLIPLTkDRAKILRALRRL-EPKGGGTN 77
|
90 100
....*....|....*....|....*.
gi 1730469733 394 LASCFRAVIERMQ-NPQWVDADAVVI 418
Cdd:pfam13519 78 LAAALQLARAALKhRRKNQPRRIVLI 103
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
231-420 |
2.44e-04 |
|
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];
Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 42.62 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 231 DAPMETFRSLVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEFEFYRKLVEKQLLTYRLHGDAWKEKITERPVTR 310
Cdd:COG1240 6 LLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 311 QDVDEQPRgPFIVCVDTSGSMGGFNE-QCAKAFCLALMRvALADNRRCFIMLFSSEV-VHYELTgpQGLEQAIRFLSQ-R 387
Cdd:COG1240 86 LARPQRGR-DVVLVVDASGSMAAENRlEAAKGALLDFLD-DYRPRDRVGLVAFGGEAeVLLPLT--RDREALKRALDElP 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1730469733 388 FRGGTDLASCFRAVIERMQNpqwVDADA----VVISD 420
Cdd:COG1240 162 PGGGTPLGDALALALELLKR---ADPARrkviVLLTD 195
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
262-395 |
2.14e-03 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 40.08 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 262 RLLPPELATLGITELEFEFYRKLVEKQLLTYRLHGDAWKEKITErpVTRQDVDEQPRGP--FIVCVDTSGSMGGFN-EQC 338
Cdd:COG2304 35 GEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRLLLVG--LQPPKAAAEERPPlnLVFVIDVSGSMSGDKlELA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730469733 339 AKAFCLALMRvaLADNRRCFIMLFSSEV-VHYELTGPQGLEQAIRFLSQ-RFRGGTDLA 395
Cdd:COG2304 113 KEAAKLLVDQ--LRPGDRVSIVTFAGDArVLLPPTPATDRAKILAAIDRlQAGGGTALG 169
|
|
| vWA_interalpha_trypsin_inhibitor |
cd01461 |
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
318-403 |
4.80e-03 |
|
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.
Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 37.96 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730469733 318 RGPFIVCVDTSGSMGGFNEQCAKafclALMRVALAD-NRRC-F-IMLFSSEV-------VHYEltgPQGLEQAIRFLSQR 387
Cdd:cd01461 2 PKEVVFVIDTSGSMSGTKIEQTK----EALLTALKDlPPGDyFnIIGFSDTVeefspssVSAT---AENVAAAIEYVNRL 74
|
90
....*....|....*..
gi 1730469733 388 F-RGGTDLASCFRAVIE 403
Cdd:cd01461 75 QaLGGTNMNDALEAALE 91
|
|
| |
