|
Name |
Accession |
Description |
Interval |
E-value |
| yieM |
PRK10997 |
ATPase RavA stimulator ViaA; |
1-473 |
0e+00 |
|
ATPase RavA stimulator ViaA;
Pssm-ID: 236815 [Multi-domain] Cd Length: 487 Bit Score: 898.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 1 MLTLDTLNTMLAVSEEGMVEEMILALLASPQLVIFFEKFPRLKNAVTADLPRWREALRSRLKDARVPPELTEEVMCYQQS 80
Cdd:PRK10997 1 MLTLDTLNLLLAISESGLIEEMIIALLASPQLAVFFEKFPRLKRALTKDLPRWREALRQRLKDACVPPELAEEFALYQQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 81 QLLSTPQFIVQLPQILALLHRLHSPYAAQAKQLTE----SNSTFTPALHTLFLQRWRLSLVVQATTLNQQLLEEEREQLL 156
Cdd:PRK10997 81 QLLSTPQFIVQLPDILDKLHRLHSPFAEQARQLVDankgANSPITSALHTLFLQRWRLSLVVQTTTLNQQLLEQEREQLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 157 SDVQERMTLSGQLEPTLAENDNAAGRLWDMSAGQLKRGDYQLIVKYGEFLAAQPELMQLAEQLGRSREAKSVPKKDAPME 236
Cdd:PRK10997 161 AELQQRMTLSGQLEPVLAENDEAAGRLWDMSAGQLKRGDYQLIVQYGEFLKQQPELQKLAEQLGRSREAKSVPRNDAPME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 237 TFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGEAWREKVTERPVVHQDVDE 316
Cdd:PRK10997 241 TFRTMVREPDTVPEQVVGIHQSDDILRLLPPELATLGIPELEYEFYRRLVEKRLLTYRLQGESWREKTVERPVVHQDQDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 317 QPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTDVVRYELSGPESIEQAIRFLSQRFRGGTDIA 396
Cdd:PRK10997 321 QPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRIALAENRRCYIMLFSTEVVTYELTGPDGLEQAIRFLSQSFRGGTDLA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879335 397 SCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGM 473
Cdd:PRK10997 401 PCLRAIIEKMQGREWFDADAVVISDFIAQRLPDELVAKVKELQRQHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGL 477
|
|
| VWA_YIEM_type |
cd01462 |
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
320-467 |
5.17e-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: 183.32 E-value: 5.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 320 GPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTDVVRYELSGPESIEQAIRFLS-QRFRGGTDIASC 398
Cdd:cd01462 1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVEFLSgVQLGGGTDINKA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879335 399 FRAIIERMQGREWFDADAVVISDFIAQRLPDDVVsKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIW 467
Cdd:cd01462 81 LRYALELIERRDPRKADIVLITDGYEGGVSDELL-REVELKRSRVARFVALALGDHGNPGYDRISAEDE 148
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
207-463 |
6.29e-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: 166.01 E-value: 6.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 207 AAQPELMQLAEQLGRSREAKSVPKKDAPMETFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLV 286
Cdd:COG2425 4 DAAAAARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 287 EKQLLTYRLHGEAWREKVTERPVVHQDVDEQP--RGPFIVCVDTSGSMGGFNEQCAKAFCLALMRvALADNRRCFIMLFS 364
Cdd:COG2425 84 LLDALLLAVLLLALLLLAALLLLAAPASAAVPllEGPVVLCVDTSGSMAGSKEAAAKAAALALLR-ALRPNRRFGVILFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 365 TDVV-RYELSGPESIEQAIRFLSQRF-RGGTDIASCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGelQRLH 442
Cdd:COG2425 163 TEVVeDLPLTADDGLEDAIEFLSGLFaGGGTDIAPALRAALELLEEPDYRNADIVLITDGEAGVSPEELLREVR--AKES 240
|
250 260
....*....|....*....|.
gi 446879335 443 QHRFHAVAMSAHGKPGIMRIF 463
Cdd:COG2425 241 GVRLFTVAIGDAGNPGLLEAL 261
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
322-470 |
2.84e-17 |
|
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: 79.42 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 322 FIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNR--RCFIMLFSTDVVRY----ELSGPESIEQAIRFLSQRFRGGTDI 395
Cdd:smart00327 2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdRVGLVTFSDDARVLfplnDSRSKDALLEALASLSYKLGGGTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 396 ASCFRAIIE-----RMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRlHQHRFHAVAMSAHGKPGIMRIFDHIWRFD 470
Cdd:smart00327 82 GAALQYALEnlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKR-SGVKVFVVGVGNDVDEEELKKLASAPGGV 160
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
304-458 |
5.29e-09 |
|
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: 56.25 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 304 VTERPVVHQDVDEQPRgPFIVCVDTSGSMGGFNeqcakAFCLALMRVALADNRRCFIMLFSTDVVR----YELSGPESIE 379
Cdd:pfam05762 42 EPVELVRRKPRKRRPW-RLVLLLDVSGSMSDYS-----RVFLALMHALLRQRPRTRVFAFSTRLTDltrqLRERDPDEAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 380 QAIRFLSQRFRGGTDIASCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRlHQHRFHAV-AMSAHGKPG 458
Cdd:pfam05762 116 RRVSARVEDWGGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREELLAEVARLRR-RARRLVWLnPLPDLRWPG 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| yieM |
PRK10997 |
ATPase RavA stimulator ViaA; |
1-473 |
0e+00 |
|
ATPase RavA stimulator ViaA;
Pssm-ID: 236815 [Multi-domain] Cd Length: 487 Bit Score: 898.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 1 MLTLDTLNTMLAVSEEGMVEEMILALLASPQLVIFFEKFPRLKNAVTADLPRWREALRSRLKDARVPPELTEEVMCYQQS 80
Cdd:PRK10997 1 MLTLDTLNLLLAISESGLIEEMIIALLASPQLAVFFEKFPRLKRALTKDLPRWREALRQRLKDACVPPELAEEFALYQQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 81 QLLSTPQFIVQLPQILALLHRLHSPYAAQAKQLTE----SNSTFTPALHTLFLQRWRLSLVVQATTLNQQLLEEEREQLL 156
Cdd:PRK10997 81 QLLSTPQFIVQLPDILDKLHRLHSPFAEQARQLVDankgANSPITSALHTLFLQRWRLSLVVQTTTLNQQLLEQEREQLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 157 SDVQERMTLSGQLEPTLAENDNAAGRLWDMSAGQLKRGDYQLIVKYGEFLAAQPELMQLAEQLGRSREAKSVPKKDAPME 236
Cdd:PRK10997 161 AELQQRMTLSGQLEPVLAENDEAAGRLWDMSAGQLKRGDYQLIVQYGEFLKQQPELQKLAEQLGRSREAKSVPRNDAPME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 237 TFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGEAWREKVTERPVVHQDVDE 316
Cdd:PRK10997 241 TFRTMVREPDTVPEQVVGIHQSDDILRLLPPELATLGIPELEYEFYRRLVEKRLLTYRLQGESWREKTVERPVVHQDQDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 317 QPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTDVVRYELSGPESIEQAIRFLSQRFRGGTDIA 396
Cdd:PRK10997 321 QPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRIALAENRRCYIMLFSTEVVTYELTGPDGLEQAIRFLSQSFRGGTDLA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879335 397 SCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGM 473
Cdd:PRK10997 401 PCLRAIIEKMQGREWFDADAVVISDFIAQRLPDELVAKVKELQRQHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGL 477
|
|
| VWA_YIEM_type |
cd01462 |
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
320-467 |
5.17e-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: 183.32 E-value: 5.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 320 GPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTDVVRYELSGPESIEQAIRFLS-QRFRGGTDIASC 398
Cdd:cd01462 1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVEFLSgVQLGGGTDINKA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879335 399 FRAIIERMQGREWFDADAVVISDFIAQRLPDDVVsKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIW 467
Cdd:cd01462 81 LRYALELIERRDPRKADIVLITDGYEGGVSDELL-REVELKRSRVARFVALALGDHGNPGYDRISAEDE 148
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
207-463 |
6.29e-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: 166.01 E-value: 6.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 207 AAQPELMQLAEQLGRSREAKSVPKKDAPMETFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLV 286
Cdd:COG2425 4 DAAAAARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 287 EKQLLTYRLHGEAWREKVTERPVVHQDVDEQP--RGPFIVCVDTSGSMGGFNEQCAKAFCLALMRvALADNRRCFIMLFS 364
Cdd:COG2425 84 LLDALLLAVLLLALLLLAALLLLAAPASAAVPllEGPVVLCVDTSGSMAGSKEAAAKAAALALLR-ALRPNRRFGVILFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 365 TDVV-RYELSGPESIEQAIRFLSQRF-RGGTDIASCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGelQRLH 442
Cdd:COG2425 163 TEVVeDLPLTADDGLEDAIEFLSGLFaGGGTDIAPALRAALELLEEPDYRNADIVLITDGEAGVSPEELLREVR--AKES 240
|
250 260
....*....|....*....|.
gi 446879335 443 QHRFHAVAMSAHGKPGIMRIF 463
Cdd:COG2425 241 GVRLFTVAIGDAGNPGLLEAL 261
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
322-470 |
2.84e-17 |
|
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: 79.42 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 322 FIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNR--RCFIMLFSTDVVRY----ELSGPESIEQAIRFLSQRFRGGTDI 395
Cdd:smart00327 2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdRVGLVTFSDDARVLfplnDSRSKDALLEALASLSYKLGGGTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 396 ASCFRAIIE-----RMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRlHQHRFHAVAMSAHGKPGIMRIFDHIWRFD 470
Cdd:smart00327 82 GAALQYALEnlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKR-SGVKVFVVGVGNDVDEEELKKLASAPGGV 160
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
323-464 |
3.60e-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: 55.65 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 323 IVCVDTSGSMGGFNEQCAKAFCLALMR--VALADNRRCFIMLFSTDVVRY----ELSGPESIEQAIRFLSQRFRGGTDIA 396
Cdd:cd00198 4 VFLLDVSGSMGGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVlpltTDTDKADLLEAIDALKKGLGGGTNIG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 397 SCFRAIIERMQGREWFDADAVVI--SDFIAQRLPDDVVSKVGELQRLhQHRFHAVAMSAHGKPGIMRIFD 464
Cdd:cd00198 84 AALRLALELLKSAKRPNARRVIIllTDGEPNDGPELLAEAARELRKL-GITVYTIGIGDDANEDELKEIA 152
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
304-458 |
5.29e-09 |
|
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: 56.25 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 304 VTERPVVHQDVDEQPRgPFIVCVDTSGSMGGFNeqcakAFCLALMRVALADNRRCFIMLFSTDVVR----YELSGPESIE 379
Cdd:pfam05762 42 EPVELVRRKPRKRRPW-RLVLLLDVSGSMSDYS-----RVFLALMHALLRQRPRTRVFAFSTRLTDltrqLRERDPDEAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 380 QAIRFLSQRFRGGTDIASCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRlHQHRFHAV-AMSAHGKPG 458
Cdd:pfam05762 116 RRVSARVEDWGGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREELLAEVARLRR-RARRLVWLnPLPDLRWPG 194
|
|
| YeaD2 |
COG1721 |
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown]; |
305-423 |
1.56e-05 |
|
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
Pssm-ID: 441327 [Multi-domain] Cd Length: 287 Bit Score: 46.74 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 305 TERPVVHQDVDEQPRgPFIVCVDTSGSMGGFNEQCAK-----AFCLALMRVALADNRRCFIMLFSTDVVRY--ELSGPES 377
Cdd:COG1721 134 TGELYVREFEEEREL-TVVLLLDTSASMRFGSGGPSKldlavEAAASLAYLALRQGDRVGLLTFGDRVRRYlpPRRGRRH 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446879335 378 IEQAIRFLSQ-RFRGGTDIASCFRAIIERMQGRewfdADAVVISDFI 423
Cdd:COG1721 213 LLRLLEALARlEPAGETDLAAALRRLARRLPRR----SLVVLISDFL 255
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
322-419 |
1.34e-04 |
|
von Willebrand factor type A domain;
Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 41.12 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 322 FIVCVDTSGSMGG-----FNEQCAKAFCLALMrvALADNRRCFIMLFSTDVVRyEL---SGPESIEQAIRFLsQRFRGGT 393
Cdd:pfam13519 1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALL--KSLPGDRVGLVTFGDGPEV-LIpltKDRAKILRALRRL-EPKGGGT 76
|
90 100
....*....|....*....|....*.
gi 446879335 394 DIASCFRAIIERMQGReWFDADAVVI 419
Cdd:pfam13519 77 NLAAALQLARAALKHR-RKNQPRRIV 101
|
|
| vWA_interalpha_trypsin_inhibitor |
cd01461 |
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
319-404 |
2.22e-04 |
|
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: 41.82 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 319 RGPFIVCVDTSGSMGGFNEQCAKafclALMRVALAD-NRRC-F-IMLFSTDVvrYELSG------PESIEQAIRFLSQRF 389
Cdd:cd01461 2 PKEVVFVIDTSGSMSGTKIEQTK----EALLTALKDlPPGDyFnIIGFSDTV--EEFSPssvsatAENVAAAIEYVNRLQ 75
|
90
....*....|....*.
gi 446879335 390 -RGGTDIASCFRAIIE 404
Cdd:cd01461 76 aLGGTNMNDALEAALE 91
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
232-440 |
7.33e-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: 41.46 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 232 DAPMETFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGEAWREKVTERPVVH 311
Cdd:COG1240 2 LALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 312 QDVDEQPRGP---FIVCVDTSGSMGGFNE-QCAKAFCLALMRvALADNRRCFIMLFSTDVvrYELSGP-ESIEQAIRFLS 386
Cdd:COG1240 82 APLALARPQRgrdVVLVVDASGSMAAENRlEAAKGALLDFLD-DYRPRDRVGLVAFGGEA--EVLLPLtRDREALKRALD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879335 387 Q-RFRGGTDIAScfrAIierMQGREWFDADA-------VVISDFIAQRLPDDVVSKVGELQR 440
Cdd:COG1240 159 ElPPGGGTPLGD---AL---ALALELLKRADparrkviVLLTDGRDNAGRIDPLEAAELAAA 214
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
261-396 |
6.38e-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: 38.54 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879335 261 ILRLLPPELATLGITELEYEFYRRLV-EKQLLTYRLHGEAWR-EKVTERPvvhQDVDEQPRGP--FIVCVDTSGSMGGFN 336
Cdd:COG2304 32 LVGGEPPPAAAVRLEELVNFFPYDYPlPTGRLAQSPWNPQTRlLLVGLQP---PKAAAEERPPlnLVFVIDVSGSMSGDK 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446879335 337 -EQCAKAFCLALMRvaLADNRRCFIMLFSTDV-VRYELSGPESIEQAIRFLSQ-RFRGGTDIA 396
Cdd:COG2304 109 lELAKEAAKLLVDQ--LRPGDRVSIVTFAGDArVLLPPTPATDRAKILAAIDRlQAGGGTALG 169
|
|
| |
