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Conserved domains on  [gi|1828683798|ref|WP_167572819|]
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VWA domain-containing protein [Aeromonas veronii]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

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|12579041|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 77-261 1.76e-50

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.


The actual alignment was detected with superfamily member cd01467:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 180  Bit Score: 165.58  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRTPDMLdngeQQARLTAVRQQIKALIAKRAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFDL 156
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGEAIQLARQHGDP--GRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDTFiqpydeagsgQ 234
Cdd:cd01467    79 AGQGTAIGDAIGLAIKRLKNseAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGP----------K 148

                         170       180
                  ....*....|....*....|....*..
gi 1828683798 235 ADPSSELDEPLLKELAQTGQGRYFRAR 261
Cdd:cd01467   149 PDGSTILDEDSLVEIADKTGGRIFRAL 175
 
Name Accession Description Interval E-value
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 77-261 1.76e-50

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: 165.58  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRTPDMLdngeQQARLTAVRQQIKALIAKRAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFDL 156
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGEAIQLARQHGDP--GRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDTFiqpydeagsgQ 234
Cdd:cd01467    79 AGQGTAIGDAIGLAIKRLKNseAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGP----------K 148

                         170       180
                  ....*....|....*....|....*..
gi 1828683798 235 ADPSSELDEPLLKELAQTGQGRYFRAR 261
Cdd:cd01467   149 PDGSTILDEDSLVEIADKTGGRIFRAL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-269 7.27e-42

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: 146.24  E-value: 7.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798   1 MILAWPWFALALVLPLLVRFGLPPLRRGYLAHPGFALLRPQAGLPLWHAMLLWCALILALCRPQWWGEPVIQYEG---SR 77
Cdd:COG1240    14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARpqrGR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRTPDmldngeqqaRLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDfdl 156
Cdd:COG1240    94 DVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP--- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGEAIQLARQH---GDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADpdtfiqpydeagsg 233
Cdd:COG1240   162 PGGGTPLGDALALALELlkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE-------------- 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1828683798 234 qadpssELDEPLLKELAQTGQGRYFRARTQSDLDTI 269
Cdd:COG1240   228 ------AVDEGLLREIAEATGGRYFRADDLSELAAI 257
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 78-266 5.43e-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: 93.67  E-value: 5.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798   78 DLLLAVDLSDSMRtpdmldngeqQARLTAVRQQIKALIAK----RAGDRVGLIVFADHAYLLSPL--TQEIPALLTLSDE 151
Cdd:smart00327   1 DVVFLLDGSGSMG----------GNRFELAKEFVLKLVEQldigPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALAS 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  152 LDFDLVGrTTALGEAIQLARQH-------GDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDTfi 224
Cdd:smart00327  71 LSYKLGG-GTNLGAALQYALENlfsksagSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDE-- 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1828683798  225 qpydeagsgqadpsseldePLLKELAQTGQGRYFRARTQSDL 266
Cdd:smart00327 148 -------------------EELKKLASAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
78-270 2.57e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 80.78  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRtpdmldngeqQARLTAVRQQIKALIAK----RAGDRVGLIVFADHAYLLSPLT--QEIPALLTLSDE 151
Cdd:pfam00092   1 DIVFLLDGSGSIG----------GDNFEKVKEFLKKLVESldigPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 152 LDFDLvGRTTALGEAIQLARQH-------GDPGRPTALLLVTDGRNTAGnaDPLQEAKLAAAQGIRLYTLGVGADpdtfi 224
Cdd:pfam00092  71 LRYLG-GGTTNTGKALKYALENlfssaagARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNA----- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1828683798 225 qpydeagsgqadpsselDEPLLKELAQT-GQGRYFRARTQSDLDTIN 270
Cdd:pfam00092 143 -----------------DDEELRKIASEpGEGHVFTVSDFEALEDLQ 172
PRK13685 PRK13685
hypothetical protein; Provisional
 80-273 1.03e-06

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 49.70  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  80 LLAVDLSDSMRTPDMLDNgeqqaRLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFdlvG 158
Cdd:PRK13685   92 MLVIDVSQSMRATDVEPN-----RLAAAQEAAKQFADElTPGINLGLIAFAGTATVLVSPTTNREATKNAIDKLQL---A 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 159 RTTALGEAIQLARQH----------GDPGRPTALLLVTDGRNTAGnADP------LQEAKLAAAQGIRLYTLGVGAdPDT 222
Cdd:PRK13685  164 DRTATGEAIFTALQAiatvgaviggGDTPPPARIVLMSDGKETVP-TNPdnprgaYTAARTAKDQGVPISTISFGT-PYG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1828683798 223 FIQPydeagSGQADPsSELDEPLLKELAQTGQGRYFRARTQSDLDTINVTL 273
Cdd:PRK13685  242 SVEI-----NGQRQP-VPVDDESLKKIAQLSGGEFYTAASLEELRAVYATL 286
 
Name Accession Description Interval E-value
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 77-261 1.76e-50

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: 165.58  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRTPDMLdngeQQARLTAVRQQIKALIAKRAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFDL 156
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFV----KPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGEAIQLARQHGDP--GRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDTFiqpydeagsgQ 234
Cdd:cd01467    79 AGQGTAIGDAIGLAIKRLKNseAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGP----------K 148

                         170       180
                  ....*....|....*....|....*..
gi 1828683798 235 ADPSSELDEPLLKELAQTGQGRYFRAR 261
Cdd:cd01467   149 PDGSTILDEDSLVEIADKTGGRIFRAL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-269 7.27e-42

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: 146.24  E-value: 7.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798   1 MILAWPWFALALVLPLLVRFGLPPLRRGYLAHPGFALLRPQAGLPLWHAMLLWCALILALCRPQWWGEPVIQYEG---SR 77
Cdd:COG1240    14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARpqrGR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRTPDmldngeqqaRLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDfdl 156
Cdd:COG1240    94 DVVLVVDASGSMAAEN---------RLEAAKGALLDFLDDyRPRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP--- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGEAIQLARQH---GDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADpdtfiqpydeagsg 233
Cdd:COG1240   162 PGGGTPLGDALALALELlkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE-------------- 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1828683798 234 qadpssELDEPLLKELAQTGQGRYFRARTQSDLDTI 269
Cdd:COG1240   228 ------AVDEGLLREIAEATGGRYFRADDLSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 77-269 1.96e-28

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 111.35  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRtpdmldngeqQARLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLT--QEIPALLTLSDELD 153
Cdd:COG2304    92 LNLVFVIDVSGSMS----------GDKLELAKEAAKLLVDQlRPGDRVSIVTFAGDARVLLPPTpaTDRAKILAAIDRLQ 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 154 fdlVGRTTALGEAIQLA----RQHGDPGRPTALLLVTDGRNTAGNADP---LQEAKLAAAQGIRLYTLGVGADpdtfiqp 226
Cdd:COG2304   162 ---AGGGTALGAGLELAyelaRKHFIPGRVNRVILLTDGDANVGITDPeelLKLAEEAREEGITLTTLGVGSD------- 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1828683798 227 YDEAgsgqadpsseldepLLKELAQTGQGRYFRARTQSDLDTI 269
Cdd:COG2304   232 YNED--------------LLERLADAGGGNYYYIDDPEEAEKV 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 77-222 8.06e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 98.41  E-value: 8.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRTPDMldngeqQARLTAVRQQIKALIAKRAGDRVGLIVFADHAYLLSPLTQEIPA--LLTLSDELDF 154
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKL------DKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKadLLEAIDALKK 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828683798 155 DLVGRTtALGEAIQLARQH----GDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDT 222
Cdd:cd00198    75 GLGGGT-NIGAALRLALELlksaKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANE 145
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 78-266 5.43e-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: 93.67  E-value: 5.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798   78 DLLLAVDLSDSMRtpdmldngeqQARLTAVRQQIKALIAK----RAGDRVGLIVFADHAYLLSPL--TQEIPALLTLSDE 151
Cdd:smart00327   1 DVVFLLDGSGSMG----------GNRFELAKEFVLKLVEQldigPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALAS 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  152 LDFDLVGrTTALGEAIQLARQH-------GDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQGIRLYTLGVGADPDTfi 224
Cdd:smart00327  71 LSYKLGG-GTNLGAALQYALENlfsksagSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDE-- 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1828683798  225 qpydeagsgqadpsseldePLLKELAQTGQGRYFRARTQSDL 266
Cdd:smart00327 148 -------------------EELKKLASAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
78-270 2.57e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 80.78  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRtpdmldngeqQARLTAVRQQIKALIAK----RAGDRVGLIVFADHAYLLSPLT--QEIPALLTLSDE 151
Cdd:pfam00092   1 DIVFLLDGSGSIG----------GDNFEKVKEFLKKLVESldigPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 152 LDFDLvGRTTALGEAIQLARQH-------GDPGRPTALLLVTDGRNTAGnaDPLQEAKLAAAQGIRLYTLGVGADpdtfi 224
Cdd:pfam00092  71 LRYLG-GGTTNTGKALKYALENlfssaagARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNA----- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1828683798 225 qpydeagsgqadpsselDEPLLKELAQT-GQGRYFRARTQSDLDTIN 270
Cdd:pfam00092 143 -----------------DDEELRKIASEpGEGHVFTVSDFEALEDLQ 172
VWA_2 pfam13519
von Willebrand factor type A domain;
79-185 1.62e-16

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 73.87  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  79 LLLAVDLSDSMRTPDMldngeQQARLTAVRQQIKALIAKRAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFDlvG 158
Cdd:pfam13519   1 LVFVLDTSGSMRNGDY-----GPTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPK--G 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1828683798 159 RTTALGEAIQLAR---QHGDPGRPTALLLV 185
Cdd:pfam13519  74 GGTNLAAALQLARaalKHRRKNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 79-269 7.96e-16

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 73.85  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  79 LLLAVDLSDSMRTPDmLDNGeQQARLTAVRQQikaliakRAGDRVGLIVFADHAYLLSPLT--QEIPALLTLSDELDfdl 156
Cdd:cd01465     3 LVFVIDRSGSMDGPK-LPLV-KSALKLLVDQL-------RPDDRLAIVTYDGAAETVLPATpvRDKAAILAAIDRLT--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 157 VGRTTALGE----AIQLARQHGDPGRPTALLLVTDGRNTAGNADPLQEAKLAAAQ---GIRLYTLGVGadpdtfiqpyde 229
Cdd:cd01465    71 AGGSTAGGAgiqlGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKresGITLSTLGFG------------ 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1828683798 230 agsgqadpsSELDEPLLKELAQTGQGRYFRARTQSDLDTI 269
Cdd:cd01465   139 ---------DNYNEDLMEAIADAGNGNTAYIDNLAEARKV 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 78-218 1.53e-12

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: 64.62  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRTPDMldngeQQARlTAVRQQIKAL-IAKRaGDRVGLIVFADHAYLLSPLT--QEIPALLTLSDELDF 154
Cdd:cd01450     2 DIVFLLDGSESVGPENF-----EKVK-DFIEKLVEKLdIGPD-KTRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKY 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 155 DlVGRTTALGEAIQLARQH------GDPGRPTALLLVTDGRNTAGNaDPLQEAKLAAAQGIRLYTLGVGA 218
Cdd:cd01450    75 L-GGGGTNTGKALQYALEQlfsesnARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGP 142
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
83-222 1.25e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 56.86  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  83 VDLSDSMRTPDM--LDNGEQQArLTAVRQQIKALiakrAGDRVGLIVFADHAYLLSPLTqeipallTLSdelDFDL---- 156
Cdd:COG4245    12 LDTSGSMSGEPIeaLNEGLQAL-IDELRQDPYAL----ETVEVSVITFDGEAKVLLPLT-------DLE---DFQPpdls 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828683798 157 VGRTTALGEAIQLA-----------RQHGDPGRPTALLLVTDGRNTAGN-ADPLQEAK-LAAAQGIRLYTLGVGADPDT 222
Cdd:COG4245    77 ASGGTPLGAALELLldlierrvqkyTAEGKGDWRPVVFLITDGEPTDSDwEAALQRLKdGEAAKKANIFAIGVGPDADT 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 76-247 1.65e-09

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: 56.07  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  76 SRDLLLAVDLSDSMRTPDMldngeQQARlTAVRQQIKALiakRAGDRVGLIVFADHAYLLSP----LTQEipallTLSDE 151
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKI-----EQTK-EALLTALKDL---PPGDYFNIIGFSDTVEEFSPssvsATAE-----NVAAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 152 LDF----DLVGRT---TALGEAIQLarQHGDPGRPTALLLVTDGRNTagnaDP---LQEAKLAAAQGIRLYTLGVGADPD 221
Cdd:cd01461    68 IEYvnrlQALGGTnmnDALEAALEL--LNSSPGSVPQIILLTDGEVT----NEsqiLKNVREALSGRIRLFTFGIGSDVN 141

                         170       180
                  ....*....|....*....|....*..
gi 1828683798 222 T-FIQPYDEAGSGQADPSSELDEPLLK 247
Cdd:cd01461   142 TyLLERLAREGRGIARRIYETDDIESQ 168
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 79-259 1.43e-07

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 50.74  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  79 LLLAVDLSDSMRTpdmldngeqQARLTAVRQQIKALI--AKRAGDRVGLIVFA-DHAYLLSPLTQEIpallTLSD-ELDf 154
Cdd:cd01451     3 VIFVVDASGSMAA---------RHRMAAAKGAVLSLLrdAYQRRDKVALIAFRgTEAEVLLPPTRSV----ELAKrRLA- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 155 DLV--GRT---TALGEAIQLAR-QHGDPGRPTALLLVTDGRNTAGNaDPLQEAKLAAAQGIRlyTLGVGA-DPDTfiqpy 227
Cdd:cd01451    69 RLPtgGGTplaAGLLAAYELAAeQARDPGQRPLIVVITDGRANVGP-DPTADRALAAARKLR--ARGISAlVIDT----- 140

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1828683798 228 deagsgqadPSSELDEPLLKELAQTGQGRYFR 259
Cdd:cd01451   141 ---------EGRPVRRGLAKDLARALGGQYVR 163
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 78-223 2.02e-07

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: 50.09  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRtpdmldnGEQQARLTAVRQQIKALIAKRAGDRVGLIVFAdhayllSPLTQEIP----------ALLT 147
Cdd:cd01476     2 DLLFVLDSSGSVR-------GKFEKYKKYIERIVEGLEIGPTATRVALITYS------GRGRQRVRfnlpkhndgeELLE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 148 LSDELDFdlVGRTTALGEAIQLARQHGDP------GRPTALLLVTDGRNtagNADPLQEAKLAAAQ-GIRLYTLGVGaDP 220
Cdd:cd01476    69 KVDNLRF--IGGTTATGAAIEVALQQLDPsegrreGIPKVVVVLTDGRS---HDDPEKQARILRAVpNIETFAVGTG-DP 142


                  ...
gi 1828683798 221 DTF 223
Cdd:cd01476   143 GTV 145
PRK13685 PRK13685
hypothetical protein; Provisional
 80-273 1.03e-06

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 49.70  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  80 LLAVDLSDSMRTPDMLDNgeqqaRLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEIPALLTLSDELDFdlvG 158
Cdd:PRK13685   92 MLVIDVSQSMRATDVEPN-----RLAAAQEAAKQFADElTPGINLGLIAFAGTATVLVSPTTNREATKNAIDKLQL---A 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 159 RTTALGEAIQLARQH----------GDPGRPTALLLVTDGRNTAGnADP------LQEAKLAAAQGIRLYTLGVGAdPDT 222
Cdd:PRK13685  164 DRTATGEAIFTALQAiatvgaviggGDTPPPARIVLMSDGKETVP-TNPdnprgaYTAARTAKDQGVPISTISFGT-PYG 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1828683798 223 FIQPydeagSGQADPsSELDEPLLKELAQTGQGRYFRARTQSDLDTINVTL 273
Cdd:PRK13685  242 SVEI-----NGQRQP-VPVDDESLKKIAQLSGGEFYTAASLEELRAVYATL 286
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 76-266 1.10e-06

VWA ywmD 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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 48.58  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  76 SRDLLLAVDLSDSMRTPDmldnGEQQARLTAVRQQIKALI-AKRAGDRVGLIVF-ADHAY-----LLSPLTQEI------ 142
Cdd:cd01456    20 PPNVAIVLDNSGSMREVD----GGGETRLDNAKAALDETAnALPDGTRLGLWTFsGDGDNpldvrVLVPKGCLTapvngf 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 143 -----PALLTLSDELDFDLVGrtTALGEAIQLARQHGDPGRPTALLLVTDGRNTAGNADPLQEAKLAA----AQGIRLYT 213
Cdd:cd01456    96 psaqrSALDAALNSLQTPTGW--TPLAAALAEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAKrrtpAPPIKVNV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1828683798 214 LGVGADPDTfiqpydeagsgqadpsseldePLLKELAQTGQGRYfrARTQSDL 266
Cdd:cd01456   174 IDFGGDADR---------------------AELEAIAEATGGTY--AYNQSDL 203
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
67-227 6.23e-06

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 47.12  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  67 GEPVI---QYEGSRDLLLAVDLSDSMRTPDMLDN-GEQQARLTAVRqqikALIAKRAGDRVGLIVFADHAYLLSPLTQEI 142
Cdd:COG1721   135 GELYVrefEEERELTVVLLLDTSASMRFGSGGPSkLDLAVEAAASL----AYLALRQGDRVGLLTFGDRVRRYLPPRRGR 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 143 PALLTLSDELDFDLVGRTTALGEAIQLARQHgdPGRPTALLLVTDGRNtagnadplqeaklAAAQGIRLYTLGVGADPDT 222
Cdd:COG1721   211 RHLLRLLEALARLEPAGETDLAAALRRLARR--LPRRSLVVLISDFLD-------------PEELGIDVVDVRTDEPLVA 275


                  ....*
gi 1828683798 223 FIQPY 227
Cdd:COG1721   276 ALLRY 280
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 122-216 3.24e-05

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: 44.04  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 122 RVGLIVFADHAYLLSPLTQEIPALLTLSDELDFDLVGRTTALGEAIQLARQH----GDPGRPTA--LLLVTDGRNTA-GN 194
Cdd:cd01474    41 RFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQifnrNGGGRETVsvIIALTDGQLLLnGH 120

                          90       100
                  ....*....|....*....|..
gi 1828683798 195 ADPLQEAKLAAAQGIRLYTLGV 216
Cdd:cd01474   121 KYPEHEAKLSRKLGAIVYCVGV 142
VWA_3 pfam13768
von Willebrand factor type A domain;
78-257 1.55e-04

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 41.61  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRtpdmldngeqqARLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEI-----PALLTLSDE 151
Cdd:pfam13768   2 DVVIVVDVSSSMS-----------GEPKLQKDALSVALRQlPTGDKFAVLGFGTLPRPLFPGWRVVsprslQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 152 LDFDLvGRTTALGEAIQLARQHGDPGRPTALLLVTDGrNTAGNADPLQEAKLAAAQGIRLYTLGVGADpdtfiqpydeag 231
Cdd:pfam13768  71 LQPPL-GGSDLLGALKEAVRAPASPGYIRHVLLLTDG-SPMQGETRVSDLISRAPGKIRFFAYGLGAS------------ 136

                         170       180
                  ....*....|....*....|....*.
gi 1828683798 232 sgqadpsseLDEPLLKELAQTGQGRY 257
Cdd:pfam13768 137 ---------ISAPMLQLLAEASNGTY 153
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 78-221 4.07e-04

VWA C3HC4-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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 40.07  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMrtpdmldngeQQARLTAVRQQIKALIAK-RAGDRVGLIVFADHAYLLSPLTQEIP-ALLTLSDELDFD 155
Cdd:cd01466     2 DLVAVLDVSGSM----------AGDKLQLVKHALRFVISSlGDADRLSIVTFSTSAKRLSPLRRMTAkGKRSAKRVVDGL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 156 LVGRTT----ALGEAIQLARQHGDPGRPTALLLVTDGRNTAGNADPlqeakLAAAQGIRLYTLGVGADPD 221
Cdd:cd01466    72 QAGGGTnvvgGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVL-----RADNAPIPIHTFGLGASHD 136
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 78-222 1.07e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 39.68  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  78 DLLLAVDLSDSMRTpdmlDNGEQQARLtaVRQQIKALIAKRAGDRVGLIVFAdhayllSPLTQEIPaLLTLSDELDF--- 154
Cdd:cd01475     4 DLVFLIDSSRSVRP----ENFELVKQF--LNQIIDSLDVGPDATRVGLVQYS------STVKQEFP-LGRFKSKADLkra 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798 155 ----DLVGRTTALGEAIQLARQH----------GDPGRPTALLLVTDGRNTagnaDPLQE-AKLAAAQGIRLYTLGVG-A 218
Cdd:cd01475    71 vrrmEYLETGTMTGLAIQYAMNNafseaegarpGSERVPRVGIVVTDGRPQ----DDVSEvAAKARALGIEMFAVGVGrA 146


                  ....
gi 1828683798 219 DPDT 222
Cdd:cd01475   147 DEEE 150
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 77-221 2.98e-03

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: 37.98  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828683798  77 RDLLLAVDLSDSMRtpdmLDNGEQQARLtaVRQQIKALIAKRAGDRVGLIVFADH----AYLLSPLTQEipALLTLSDEL 152
Cdd:cd01472     1 ADIVFLVDGSESIG----LSNFNLVKDF--VKRVVERLDIGPDGVRVGVVQYSDDprteFYLNTYRSKD--DVLEAVKNL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828683798 153 DFdlVGRTTALGEAIQLARQ---HGDPGRPTA----LLLVTDGRNTAGNADPLQEAKLAaaqGIRLYTLGVG-ADPD 221
Cdd:cd01472    73 RY--IGGGTNTGKALKYVREnlfTEASGSREGvpkvLVVITDGKSQDDVEEPAVELKQA---GIEVFAVGVKnADEE 144
 
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.
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