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Conserved domains on  [gi|1831508326|ref|NP_001367890|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

vWA domain-containing protein( domain architecture ID 10106694)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 375-534 2.82e-25

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 103.14  E-value: 2.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHY-TGGLT 453
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  454 NVTKAQLTAKNLFDTESNA--NRNKVLFILTDGVPTVDTYTDEVAagDKLKSISVISFFVGYSSYSDEVKTELGKVSEPK 531
Cdd:cd01450     81 NTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDGGDPKEAA--AKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1831508326  532 YIF 534
Cdd:cd01450    159 HVF 161
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 375-534 2.82e-25

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 103.14  E-value: 2.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHY-TGGLT 453
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  454 NVTKAQLTAKNLFDTESNA--NRNKVLFILTDGVPTVDTYTDEVAagDKLKSISVISFFVGYSSYSDEVKTELGKVSEPK 531
Cdd:cd01450     81 NTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDGGDPKEAA--AKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1831508326  532 YIF 534
Cdd:cd01450    159 HVF 161
VWA pfam00092
von Willebrand factor type A domain;
376-546 3.21e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.51  E-value: 3.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAID-TVHYTGGLTN 454
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  455 VTKA-QLTAKNLFDTESNA--NRNKVLFILTDGVPTVDTYTDEVaagDKLKSISVISFFVGyssYSDEVKTELGKVSEPK 531
Cdd:pfam00092   81 TGKAlKYALENLFSSAAGArpGAPKVVVLLTDGRSQDGDPEEVA---RELKSAGVTVFAVG---VGNADDEELRKIASEP 154

                          170       180
                   ....*....|....*....|
gi 1831508326  532 -----YIFGNMTFLPEITAQ 546
Cdd:pfam00092  155 geghvFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 376-549 5.71e-23

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: 96.75  E-value: 5.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326   376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYT-GGLTN 454
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326   455 VTKA-QLTAKNLFDTESNANRN--KVLFILTDGVPTvDTYTDEVAAGDKLKSISVISFFVGYSSYSDEvkTELGKVSEPK 531
Cdd:smart00327   81 LGAAlQYALENLFSKSAGSRRGapKVVILITDGESN-DGPKDLLKAAKELKRSGVKVFVVGVGNDVDE--EELKKLASAP 157

                           170
                    ....*....|....*...
gi 1831508326   532 yiFGNMTFLPEITAQILT 549
Cdd:smart00327  158 --GGVYVFLPELLDLLID 173
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 359-515 8.51e-10

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: 60.72  E-value: 8.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  359 LRTERDAVIDTPKCEVLDMIIAFDTSESLSSlivPQYVDFAK----KLVAQYKygnDNTRVGIITFSSDVVEVRKLTdgN 434
Cdd:COG1240     77 LALALAPLALARPQRGRDVVLVVDASGSMAA---ENRLEAAKgallDFLDDYR---PRDRVGLVAFGGEAEVLLPLT--R 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  435 TLDAVNAAIDTVHyTGGLTNVTKAQLTAKNLFDTESNaNRNKVLFILTDGVPTVDTyTDEVAAGDKLKSISVISFFVGYS 514
Cdd:COG1240    149 DREALKRALDELP-PGGGTPLGDALALALELLKRADP-ARRKVIVLLTDGRDNAGR-IDPLEAAELAAAAGIRIYTIGVG 225


                   .
gi 1831508326  515 S 515
Cdd:COG1240    226 T 226
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 375-534 2.82e-25

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 103.14  E-value: 2.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHY-TGGLT 453
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  454 NVTKAQLTAKNLFDTESNA--NRNKVLFILTDGVPTVDTYTDEVAagDKLKSISVISFFVGYSSYSDEVKTELGKVSEPK 531
Cdd:cd01450     81 NTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDGGDPKEAA--AKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1831508326  532 YIF 534
Cdd:cd01450    159 HVF 161
VWA pfam00092
von Willebrand factor type A domain;
376-546 3.21e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.51  E-value: 3.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAID-TVHYTGGLTN 454
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  455 VTKA-QLTAKNLFDTESNA--NRNKVLFILTDGVPTVDTYTDEVaagDKLKSISVISFFVGyssYSDEVKTELGKVSEPK 531
Cdd:pfam00092   81 TGKAlKYALENLFSSAAGArpGAPKVVVLLTDGRSQDGDPEEVA---RELKSAGVTVFAVG---VGNADDEELRKIASEP 154

                          170       180
                   ....*....|....*....|
gi 1831508326  532 -----YIFGNMTFLPEITAQ 546
Cdd:pfam00092  155 geghvFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 376-549 5.71e-23

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: 96.75  E-value: 5.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326   376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYT-GGLTN 454
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326   455 VTKA-QLTAKNLFDTESNANRN--KVLFILTDGVPTvDTYTDEVAAGDKLKSISVISFFVGYSSYSDEvkTELGKVSEPK 531
Cdd:smart00327   81 LGAAlQYALENLFSKSAGSRRGapKVVILITDGESN-DGPKDLLKAAKELKRSGVKVFVVGVGNDVDE--EELKKLASAP 157

                           170
                    ....*....|....*...
gi 1831508326   532 yiFGNMTFLPEITAQILT 549
Cdd:smart00327  158 --GGVYVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 375-534 2.51e-20

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: 88.78  E-value: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYT-GGLT 453
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  454 NVTKAQLTAKNLFDTESNANRNKVLFILTDGVPTVDTYTDEVAAGD-KLKSISVISFFVGYSSYSDEVKtELGKVSEPKY 532
Cdd:cd00198     81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElRKLGITVYTIGIGDDANEDELK-EIADKTTGGA 159


                   ..
gi 1831508326  533 IF 534
Cdd:cd00198    160 VF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 376-512 2.35e-15

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 74.57  E-value: 2.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYTGGLTNV 455
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508326  456 TKA-QLTAKNLFDTESNA--NRNKVLFILTDGvptvdTYTDEVA-AGDKLKSISVISFFVG 512
Cdd:cd01472     82 GKAlKYVRENLFTEASGSreGVPKVLVVITDG-----KSQDDVEePAVELKQAGIEVFAVG 137
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 375-507 4.93e-10

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 59.71  E-value: 4.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLS-SLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDA-----VNAAIDTVHY 448
Cdd:cd01471      1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508326  449 TGGLTNVTKAQLTA-KNLFDT-ESNANRNKVLFILTDGVPTVDTYTDEVAAgdKLKSISVI 507
Cdd:cd01471     81 PNGSTNTTSALLVVeKHLFDTrGNRENAPQLVIIMTDGIPDSKFRTLKEAR--KLRERGVI 139
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 359-515 8.51e-10

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: 60.72  E-value: 8.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  359 LRTERDAVIDTPKCEVLDMIIAFDTSESLSSlivPQYVDFAK----KLVAQYKygnDNTRVGIITFSSDVVEVRKLTdgN 434
Cdd:COG1240     77 LALALAPLALARPQRGRDVVLVVDASGSMAA---ENRLEAAKgallDFLDDYR---PRDRVGLVAFGGEAEVLLPLT--R 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  435 TLDAVNAAIDTVHyTGGLTNVTKAQLTAKNLFDTESNaNRNKVLFILTDGVPTVDTyTDEVAAGDKLKSISVISFFVGYS 514
Cdd:COG1240    149 DREALKRALDELP-PGGGTPLGDALALALELLKRADP-ARRKVIVLLTDGRDNAGR-IDPLEAAELAAAAGIRIYTIGVG 225


                   .
gi 1831508326  515 S 515
Cdd:COG1240    226 T 226
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 376-530 1.02e-09

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 58.45  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYTGGLTNV 455
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  456 TKA-QLTAKNLFDTESNANRN--KVLFILTDGVPtvdtyTDEV-AAGDKLKSISVISFFVGyssYSDEVKTELGKV-SEP 530
Cdd:cd01482     82 GKAlTHVREKNFTPDAGARPGvpKVVILITDGKS-----QDDVeLPARVLRNLGVNVFAVG---VKDADESELKMIaSKP 153
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 375-514 4.31e-09

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 58.96  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYkygNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHyTGGLTN 454
Cdd:COG2304     92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AGGGTA 167

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831508326  455 VTKAQLTAKNLFDTESNANRNKVLFILTDGVPTVDTyTDEVAAGDKLKS-----ISVISFFVGYS 514
Cdd:COG2304    168 LGAGLELAYELARKHFIPGRVNRVILLTDGDANVGI-TDPEELLKLAEEareegITLTTLGVGSD 231
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 375-487 7.10e-09

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 56.62  E-value: 7.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQY------KYGNDNTRVGIITFSSDV-VEVRKLTDGNTLDAVNAAIDTVH 447
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQeVEAGFLRDIRNYTSLKEAVDNLE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1831508326  448 YTGGLTNVTKAQLTAKNLFDTESNANRNKVLFILTDGVPT 487
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSD 122
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 375-484 1.22e-08

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 55.44  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYTGGLTN 454
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1831508326  455 VTKAQLTA-KNLFDTESNANRN--KVLFILTDG 484
Cdd:cd01469     81 TATAIQYVvTELFSESNGARKDatKVLVVITDG 113
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 375-484 1.31e-08

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 55.10  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSSlIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSD---VVEVrKLTDGNTLDAVNAAIDTVHYTGG 451
Cdd:cd01476      1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGRgrqRVRF-NLPKHNDGEELLEKVDNLRFIGG 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1831508326  452 LTNVTKAQLTAKNLFDTESNANRN--KVLFILTDG 484
Cdd:cd01476     79 TTATGAAIEVALQQLDPSEGRREGipKVVVVLTDG 113
VWA_2 pfam13519
von Willebrand factor type A domain;
377-480 2.27e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 52.68  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  377 MIIAFDTSESLSS-LIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNtlDAVNAAIDTVHYTGGLTNV 455
Cdd:pfam13519    1 LVFVLDTSGSMRNgDYGPTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDR--AKILRALRRLEPKGGGTNL 78

                           90       100
                   ....*....|....*....|....*
gi 1831508326  456 TKAQLTAKNLFDTESNANRNKVLFI 480
Cdd:pfam13519   79 AAALQLARAALKHRRKNQPRRIVLI 103
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
403-534 2.22e-07

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 52.23  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  403 VAQYKYGNDNTRVGIITFSSDVVEVRKLTDgntldaVNAAIDTVHYTGGLTNVTKAQLTAKNLFDTESNANRNK------ 476
Cdd:COG4245     37 LRQDPYALETVEVSVITFDGEAKVLLPLTD------LEDFQPPDLSASGGTPLGAALELLLDLIERRVQKYTAEgkgdwr 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831508326  477 -VLFILTDGVPTVDTY---TDEVAAGDKLKSISVISFFVGyssysDEVKTE-LGKVSEPKYIF 534
Cdd:COG4245    111 pVVFLITDGEPTDSDWeaaLQRLKDGEAAKKANIFAIGVG-----PDADTEvLKQLTDPVRAL 168
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 373-512 1.23e-06

VWA BatA 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 are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 49.64  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  373 EVLDMIIAFDTSESLSS--LIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTdgNTLDAVNAAIDTVH--Y 448
Cdd:cd01467      1 EGRDIMIALDVSGSMLAqdFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLT--LDRESLKELLEDIKigL 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508326  449 TGGLTNVTKAQLTAKNLFDtESNAnRNKVLFILTDGVPTVDTyTDEVAAGD--KLKSISVISFFVG 512
Cdd:cd01467     79 AGQGTAIGDAIGLAIKRLK-NSEA-KERVIVLLTDGENNAGE-IDPATAAElaKNKGVRIYTIGVG 141
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 376-534 2.34e-06

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 48.86  E-value: 2.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYVDFAKKLVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAVNAAIDTVHYTGGL-TN 454
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  455 VTKA-QLTAKNLFdTESNANRnkvlfiLTDGVP------TVDTYTDEVA-AGDKLKSISVISFFVGySSYSDevKTELGK 526
Cdd:cd01481     82 TGSAlDYVVKNLF-TKSAGSR------IEEGVPqflvliTGGKSQDDVErPAVALKRAGIVPFAIG-ARNAD--LAELQQ 151


                   ....*....
gi 1831508326  527 VS-EPKYIF 534
Cdd:cd01481    152 IAfDPSFVF 160
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 376-535 2.05e-04

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 43.27  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  376 DMIIAFDTSESLSSLIVPQYvDFAKKLVaqYKYGNDNTRVGIITFSSDVVEVRKLTDGNT--------LDAVNAAIDTvH 447
Cdd:cd01474      6 DLYFVLDKSGSVAANWIEIY-DFVEQLV--DRFNSPGLRFSFITFSTRATKILPLTDDSSaiikglevLKKVTPSGQT-Y 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  448 YTGGLTNVTKaQLTAKNLFDTESnanrNKVLFILTDGVPTVDTYTDEVAAGDKLKSISVISFFVGYSSYSdevKTELGKV 527
Cdd:cd01474     82 IHEGLENANE-QIFNRNGGGRET----VSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFL---KSQLINI 153


                   ....*....
gi 1831508326  528 -SEPKYIFG 535
Cdd:cd01474    154 aDSKEYVFP 162
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 375-535 4.61e-04

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 42.66  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  375 LDMIIAFDTSESLSslivPQYVDFAKK----LVAQYKYGNDNTRVGIITFSSDVVEVRKLTDGNTLDAV-------NAAI 443
Cdd:cd01470      1 LNIYIALDASDSIG----EEDFDEAKNaiktLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADdvikrleDFNY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508326  444 DTVHYTGGlTNVTKA-----------QLTAKNLFDTESNanrnkVLFILTDGVPTVdtytdevaAGDKLKSISVISFFVG 512
Cdd:cd01470     77 DDHGDKTG-TNTAAAlkkvyermaleKVRNKEAFNETRH-----VIILFTDGKSNM--------GGSPLPTVDKIKNLVY 142

                          170       180
                   ....*....|....*....|...
gi 1831508326  513 YSSYSDEVKTELGKVsepkYIFG 535
Cdd:cd01470    143 KNNKSDNPREDYLDV----YVFG 161
 
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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