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Conserved domains on  [gi|2513403868|ref|WP_284155567|]
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VWA domain-containing protein [Pantoea sp. YR343]

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 ...
 35-206 9.91e-47

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: 154.02  E-value: 9.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMeKSSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMIGQ 114
Cdd:cd01467     3 RDIMIALDVSGSM-LAQDFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 115 QTAIGDALGVAVKLLDNSLETDaaKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSE----EDKVDTGL 190
Cdd:cd01467    82 GTAIGDAIGLAIKRLKNSEAKE--RVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGPkpdgSTILDEDS 159

                         170
                  ....*....|....*.
gi 2513403868 191 LTDIAAITGGHAWQAA 206
Cdd:cd01467   160 LVEIADKTGGRIFRAL 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 ...
 35-206 9.91e-47

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: 154.02  E-value: 9.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMeKSSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMIGQ 114
Cdd:cd01467     3 RDIMIALDVSGSM-LAQDFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 115 QTAIGDALGVAVKLLDNSLETDaaKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSE----EDKVDTGL 190
Cdd:cd01467    82 GTAIGDAIGLAIKRLKNSEAKE--RVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGPkpdgSTILDEDS 159

                         170
                  ....*....|....*.
gi 2513403868 191 LTDIAAITGGHAWQAA 206
Cdd:cd01467   160 LVEIADKTGGRIFRAL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 3-220 1.16e-44

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: 151.24  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   3 PQLLFWTLWILLVSALARPEYLLPPKTLIKPMRNIVLILDVSGSMEkssgqnEQTRLQAVQQTARTFISQ-RKNDRIGLV 81
Cdd:COG1240    61 LLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMA------AENRLEAAKGALLDFLDDyRPRDRVGLV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  82 IFASQAWPFAPISEDKQALQSRIDQLAPGmigQQTAIGDALGVAVKLLDNSlETDAAKMAILLTDGNDTASKLDPKVAAQ 161
Cdd:COG1240   135 AFGGEAEVLLPLTRDREALKRALDELPPG---GGTPLGDALALALELLKRA-DPARRKVIVLLTDGRDNAGRIDPLEAAE 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2513403868 162 LAAAHHVMVHTIAFGDENsseedkVDTGLLTDIAAITGGHAWQaATHRDALAQVWQQID 220
Cdd:COG1240   211 LAAAAGIRIYTIGVGTEA------VDEGLLREIAEATGGRYFR-ADDLSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-200 5.22e-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: 92.52  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQA---WPFaPISEDKQALQSRIDQLAPGMi 112
Cdd:smart00327   1 DVVFLLDGSGSM---GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDArvlFPL-NDSRSKDALLEALASLSYKL- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  113 GQQTAIGDALGVAVKLLDNSLET---DAAKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDEnsseedkVDTG 189
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAGsrrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND-------VDEE 148

                          170
                   ....*....|.
gi 2513403868  190 LLTDIAAITGG 200
Cdd:smart00327 149 ELKKLASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
36-199 3.18e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.02  E-value: 3.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISE--DKQALQSRIDQLAPgMIG 113
Cdd:pfam00092   1 DIVFLLDGSGSI---GGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNLRY-LGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 114 QQTAIGDALGVAVKLL---DNSLETDAAKMAILLTDGNDTASklDPKVAAQLAAAHHVMVHTIAFGDENSSEedkvdtgl 190
Cdd:pfam00092  77 GTTNTGKALKYALENLfssAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNADDEE-------- 146


                  ....*....
gi 2513403868 191 LTDIAAITG 199
Cdd:pfam00092 147 LRKIASEPG 155
PRK13685 PRK13685
hypothetical protein; Provisional
 3-222 4.83e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 67.80  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   3 PQLLFWTLWILLVSALARP--EYLLPpktlikpmRN---IVLILDVSGSMEksSGQNEQTRLQAVQQTARTFISQ-RKND 76
Cdd:PRK13685   60 PAALLVLSLVLLTVAMAGPthDVRIP--------RNravVMLVIDVSQSMR--ATDVEPNRLAAAQEAAKQFADElTPGI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  77 RIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGmigQQTAIGDALGVAVKlldnSLETDAAKMA----------ILLTD 146
Cdd:PRK13685  130 NLGLIAFAGTATVLVSPTTNREATKNAIDKLQLA---DRTATGEAIFTALQ----AIATVGAVIGggdtpppariVLMSD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 147 GNDT--ASKLDPK---VAAQLAAAHHVMVHTIAFGDENSSEE--DK-----VDTGLLTDIAAITGGHAWQAAThRDALAQ 214
Cdd:PRK13685  203 GKETvpTNPDNPRgayTAARTAKDQGVPISTISFGTPYGSVEinGQrqpvpVDDESLKKIAQLSGGEFYTAAS-LEELRA 281


                  ....*...
gi 2513403868 215 VWQQIDAQ 222
Cdd:PRK13685  282 VYATLQQQ 289
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 35-222 3.98e-12

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 64.64  E-value: 3.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMEKssgqneqtRLQAVQQTARTFISQ--RKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMI 112
Cdd:TIGR03436  54 LTVGLVIDTSGSMRN--------DLDRARAAAIRFLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 113 ------------GQQTAIGDALGVAV-KLLDNSLETDAAKMA-ILLTDGNDTASKLDPKVAAQLAAAHHVMVHTI-AFGD 177
Cdd:TIGR03436 126 tdynssgafvrdGGGTALYDAITLAAlEQLANALAGIPGRKAlIVISDGGDNRSRDTLERAIDAAQRADVAIYSIdARGL 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2513403868 178 ENSSEEDKVDTGL-----LTDIAAITGGHAWQAATH--RDALAQVWQQIDAQ 222
Cdd:TIGR03436 206 RAPDLGAGAKAGLggpeaLERLAEETGGRAFYVNSNdlDGAFAQIAEELRSQ 257
 
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 ...
 35-206 9.91e-47

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: 154.02  E-value: 9.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMeKSSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMIGQ 114
Cdd:cd01467     3 RDIMIALDVSGSM-LAQDFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 115 QTAIGDALGVAVKLLDNSLETDaaKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSE----EDKVDTGL 190
Cdd:cd01467    82 GTAIGDAIGLAIKRLKNSEAKE--RVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGPkpdgSTILDEDS 159

                         170
                  ....*....|....*.
gi 2513403868 191 LTDIAAITGGHAWQAA 206
Cdd:cd01467   160 LVEIADKTGGRIFRAL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 3-220 1.16e-44

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: 151.24  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   3 PQLLFWTLWILLVSALARPEYLLPPKTLIKPMRNIVLILDVSGSMEkssgqnEQTRLQAVQQTARTFISQ-RKNDRIGLV 81
Cdd:COG1240    61 LLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMA------AENRLEAAKGALLDFLDDyRPRDRVGLV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  82 IFASQAWPFAPISEDKQALQSRIDQLAPGmigQQTAIGDALGVAVKLLDNSlETDAAKMAILLTDGNDTASKLDPKVAAQ 161
Cdd:COG1240   135 AFGGEAEVLLPLTRDREALKRALDELPPG---GGTPLGDALALALELLKRA-DPARRKVIVLLTDGRDNAGRIDPLEAAE 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2513403868 162 LAAAHHVMVHTIAFGDENsseedkVDTGLLTDIAAITGGHAWQaATHRDALAQVWQQID 220
Cdd:COG1240   211 LAAAAGIRIYTIGVGTEA------VDEGLLREIAEATGGRYFR-ADDLSELAAIYREID 262
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 35-200 3.79e-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: 108.65  E-value: 3.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMEkssgqneQTRLQAVQQTARTFISQ-RKNDRIGLVIFASQAW---PFAPIsEDKQALQSRIDQLAPG 110
Cdd:COG2304    92 LNLVFVIDVSGSMS-------GDKLELAKEAAKLLVDQlRPGDRVSIVTFAGDARvllPPTPA-TDRAKILAAIDRLQAG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 111 migQQTAIGDALGVAVKLLDNSLETDAAKMAILLTDGNDTASKLDPKV---AAQLAAAHHVMVHTIAFGDEnsseedkVD 187
Cdd:COG2304   164 ---GGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEEllkLAEEAREEGITLTTLGVGSD-------YN 233

                         170
                  ....*....|...
gi 2513403868 188 TGLLTDIAAITGG 200
Cdd:COG2304   234 EDLLERLADAGGG 246
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-202 9.25e-26

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: 99.18  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISE--DKQALQSRIDQLAPGMi 112
Cdd:cd00198     1 ADIVFLLDVSGSM---GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTdtDKADLLEAIDALKKGL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 113 GQQTAIGDALGVAVKLLDNSLETDAAKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSEEdkvdtglLT 192
Cdd:cd00198    77 GGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDE-------LK 149

                         170
                  ....*....|
gi 2513403868 193 DIAAITGGHA 202
Cdd:cd00198   150 EIADKTTGGA 159
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-200 5.22e-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: 92.52  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQA---WPFaPISEDKQALQSRIDQLAPGMi 112
Cdd:smart00327   1 DVVFLLDGSGSM---GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDArvlFPL-NDSRSKDALLEALASLSYKL- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  113 GQQTAIGDALGVAVKLLDNSLET---DAAKMAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDEnsseedkVDTG 189
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAGsrrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND-------VDEE 148

                          170
                   ....*....|.
gi 2513403868  190 LLTDIAAITGG 200
Cdd:smart00327 149 ELKKLASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
36-199 3.18e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.02  E-value: 3.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISE--DKQALQSRIDQLAPgMIG 113
Cdd:pfam00092   1 DIVFLLDGSGSI---GGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNLRY-LGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 114 QQTAIGDALGVAVKLL---DNSLETDAAKMAILLTDGNDTASklDPKVAAQLAAAHHVMVHTIAFGDENSSEedkvdtgl 190
Cdd:pfam00092  77 GTTNTGKALKYALENLfssAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNADDEE-------- 146


                  ....*....
gi 2513403868 191 LTDIAAITG 199
Cdd:pfam00092 147 LRKIASEPG 155
VWA_2 pfam13519
von Willebrand factor type A domain;
37-131 2.86e-16

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 72.32  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMekSSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGmiGQQT 116
Cdd:pfam13519   1 LVFVLDTSGSM--RNGDYGPTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPK--GGGT 76

                          90
                  ....*....|....*
gi 2513403868 117 AIGDALGVAVKLLDN 131
Cdd:pfam13519  77 NLAAALQLARAALKH 91
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 36-201 3.68e-16

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: 73.48  E-value: 3.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKNDRIGLVIFASQAWPFAPISE--DKQALQSRIDQLAPgMIG 113
Cdd:cd01450     2 DIVFLLDGSESV---GPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDykSKDDLLKAVKNLKY-LGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 114 QQTAIGDALGVAVKLL--DNSLETDAAKMAILLTDGNDTaSKLDPKVAAQLAAAHHVMVHTIAFGDENSSEedkvdtglL 191
Cdd:cd01450    78 GGTNTGKALQYALEQLfsESNARENVPKVIIVLTDGRSD-DGGDPKEAAAKLKDEGIKVFVVGVGPADEEE--------L 148

                         170
                  ....*....|
gi 2513403868 192 TDIAAITGGH 201
Cdd:cd01450   149 REIASCPSER 158
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 24-200 4.30e-15

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: 71.69  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  24 LLPPKTLIKPMRNIVLILDVSGSMEKSSGQnEQTRLQAVQQTARTFISQ-RKNDRIGLVIFASQA-------------WP 89
Cdd:cd01456    10 LEPVETEPQLPPNVAIVLDNSGSMREVDGG-GETRLDNAKAALDETANAlPDGTRLGLWTFSGDGdnpldvrvlvpkgCL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  90 FAPI----SEDKQALQSRIDQLAPGMIGqqTAIGDALGVAVKLLDNsletDAAKMAILLTDGNDTASKLDPKVAAQLAA- 164
Cdd:cd01456    89 TAPVngfpSAQRSALDAALNSLQTPTGW--TPLAAALAEAAAYVDP----GRVNVVVLITDGEDTCGPDPCEVARELAKr 162

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2513403868 165 ---AHHVMVHTIAFGDEnsseedkVDTGLLTDIAAITGG 200
Cdd:cd01456   163 rtpAPPIKVNVIDFGGD-------ADRAELEAIAEATGG 194
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 37-200 2.10e-14

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: 68.96  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMekssgQNEqtRLQAVQQTARTFISQ-RKNDRIGLVIFASQA---WPFAPISED-KQALQSRIDQLAPGm 111
Cdd:cd01466     3 LVAVLDVSGSM-----AGD--KLQLVKHALRFVISSlGDADRLSIVTFSTSAkrlSPLRRMTAKgKRSAKRVVDGLQAG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 112 igQQTAIGDALGVAVKLLDNSLETDAAKMAILLTDGNDTASKLDPKVAAQLAAahhvmVHTIAFGDENsseedkvDTGLL 191
Cdd:cd01466    75 --GGTNVVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRADNAPIP-----IHTFGLGASH-------DPALL 140


                  ....*....
gi 2513403868 192 TDIAAITGG 200
Cdd:cd01466   141 AFIAEITGG 149
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 36-202 2.50e-14

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: 68.84  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMekssgqnEQTRLQAVQQTARTFISQ-RKNDRIGLVIFASQA---WPFAPISeDKQALQSRIDQLAPGM 111
Cdd:cd01465     2 NLVFVIDRSGSM-------DGPKLPLVKSALKLLVDQlRPDDRLAIVTYDGAAetvLPATPVR-DKAAILAAIDRLTAGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 112 IgqqTAIGDALGVAVKLLDNSLETDAAKMAILLTDGNDTASKLDPKVAAQLAAA---HHVMVHTIAFGDENSSEedkvdt 188
Cdd:cd01465    74 S---TAGGAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQkreSGITLSTLGFGDNYNED------ 144

                         170
                  ....*....|....
gi 2513403868 189 gLLTDIAAITGGHA 202
Cdd:cd01465   145 -LMEAIADAGNGNT 157
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 10-182 1.10e-13

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 68.94  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  10 LWILLVSALARPEYLLPPKTLIKPMRNIVLILDVSGSMeksSGQNEQTRLQAVQQTARtfiSQRKNDRIGLVIFASQAWP 89
Cdd:COG2425    94 LLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSM---AGSKEAAAKAAALALLR---ALRPNRRFGVILFDTEVVE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  90 FAPISEDKQaLQSRIDQLAPGMIGQQTAIGDALGVAVKLLDNSLETDAAkmAILLTDGNDTASklDPKVAAQLAAAHH-V 168
Cdd:COG2425   168 DLPLTADDG-LEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNAD--IVLITDGEAGVS--PEELLREVRAKESgV 242

                         170
                  ....*....|....
gi 2513403868 169 MVHTIAFGDENSSE 182
Cdd:COG2425   243 RLFTVAIGDAGNPG 256
PRK13685 PRK13685
hypothetical protein; Provisional
 3-222 4.83e-13

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 67.80  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868   3 PQLLFWTLWILLVSALARP--EYLLPpktlikpmRN---IVLILDVSGSMEksSGQNEQTRLQAVQQTARTFISQ-RKND 76
Cdd:PRK13685   60 PAALLVLSLVLLTVAMAGPthDVRIP--------RNravVMLVIDVSQSMR--ATDVEPNRLAAAQEAAKQFADElTPGI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  77 RIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGmigQQTAIGDALGVAVKlldnSLETDAAKMA----------ILLTD 146
Cdd:PRK13685  130 NLGLIAFAGTATVLVSPTTNREATKNAIDKLQLA---DRTATGEAIFTALQ----AIATVGAVIGggdtpppariVLMSD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 147 GNDT--ASKLDPK---VAAQLAAAHHVMVHTIAFGDENSSEE--DK-----VDTGLLTDIAAITGGHAWQAAThRDALAQ 214
Cdd:PRK13685  203 GKETvpTNPDNPRgayTAARTAKDQGVPISTISFGTPYGSVEinGQrqpvpVDDESLKKIAQLSGGEFYTAAS-LEELRA 281


                  ....*...
gi 2513403868 215 VWQQIDAQ 222
Cdd:PRK13685  282 VYATLQQQ 289
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 35-222 3.98e-12

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 64.64  E-value: 3.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMEKssgqneqtRLQAVQQTARTFISQ--RKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMI 112
Cdd:TIGR03436  54 LTVGLVIDTSGSMRN--------DLDRARAAAIRFLKTvlRPNDRVFVVTFNTRLRLLQDFTSDPRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 113 ------------GQQTAIGDALGVAV-KLLDNSLETDAAKMA-ILLTDGNDTASKLDPKVAAQLAAAHHVMVHTI-AFGD 177
Cdd:TIGR03436 126 tdynssgafvrdGGGTALYDAITLAAlEQLANALAGIPGRKAlIVISDGGDNRSRDTLERAIDAAQRADVAIYSIdARGL 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2513403868 178 ENSSEEDKVDTGL-----LTDIAAITGGHAWQAATH--RDALAQVWQQIDAQ 222
Cdd:TIGR03436 206 RAPDLGAGAKAGLggpeaLERLAEETGGRAFYVNSNdlDGAFAQIAEELRSQ 257
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
33-178 1.99e-11

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 61.48  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  33 PMRN--IVLILDVSGSMeksSGQneqtRLQAVQQTARTFISQ-------RKNDRIGLVIFASQA-W--PFAPISedkqal 100
Cdd:COG4245     2 PMRRlpVYLLLDTSGSM---SGE----PIEALNEGLQALIDElrqdpyaLETVEVSVITFDGEAkVllPLTDLE------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 101 QSRIDQLAPGmiGqQTAIGDALGVAVKLLDNSLET-------DAAKMAILLTDGNDTASKLDPKVAA--QLAAAHHVMVH 171
Cdd:COG4245    69 DFQPPDLSAS--G-GTPLGAALELLLDLIERRVQKytaegkgDWRPVVFLITDGEPTDSDWEAALQRlkDGEAAKKANIF 145


                  ....*..
gi 2513403868 172 TIAFGDE 178
Cdd:COG4245   146 AIGVGPD 152
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 26-210 2.44e-09

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 57.59  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  26 PPKT--LIKPMRNIV-LILDVSGSMEKssgqneQTRLQAVQQTARTFISQ--RKNDRIGLVIFASQAWPFAPI-----SE 95
Cdd:TIGR00868 293 PPPTfsLLKIRQRIVcLVLDKSGSMTV------EDRLKRMNQAAKLFLLQtvEKGSWVGMVTFDSAAYIKNELiqitsSA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  96 DKQALQSRIDQLAPGmigqQTAIGDALGVAVKLLDNSLETDAAKMAILLTDGND-TASKLDPKVAAQLAaahhvMVHTIA 174
Cdd:TIGR00868 367 ERDALTANLPTAASG----GTSICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDnTISSCFEEVKQSGA-----IIHTIA 437

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2513403868 175 FGDENSSEedkvdtglLTDIAAITGGHAWQAATHRD 210
Cdd:TIGR00868 438 LGPSAAKE--------LEELSDMTGGLRFYASDQAD 465
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 35-202 2.76e-08

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: 52.22  E-value: 2.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMEKssgqneqTRLQAVQQTARTFISQ-RKNDRIGLVIFAS--QAWPFAPISEDKQALQSRIDQLAPGM 111
Cdd:cd01461     3 KEVVFVIDTSGSMSG-------TKIEQTKEALLTALKDlPPGDYFNIIGFSDtvEEFSPSSVSATAENVAAAIEYVNRLQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 112 IGQQTAIGDALGVAVKLLDNSleTDAAKMAILLTDG--NDTASKLDpkvAAQLAAAHHVMVHTIAFGDEnsseedkVDTG 189
Cdd:cd01461    76 ALGGTNMNDALEAALELLNSS--PGSVPQIILLTDGevTNESQILK---NVREALSGRIRLFTFGIGSD-------VNTY 143

                         170
                  ....*....|...
gi 2513403868 190 LLTDIAAITGGHA 202
Cdd:cd01461   144 LLERLAREGRGIA 156
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 36-195 3.06e-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: 48.93  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMEkssGQNEQTRLQAVQQTARTFISQRKnDRIGLVIFASQA-----WPFaPISEDKQALQSRIDQLApg 110
Cdd:cd01476     2 DLLFVLDSSGSVR---GKFEKYKKYIERIVEGLEIGPTA-TRVALITYSGRGrqrvrFNL-PKHNDGEELLEKVDNLR-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 111 MIGQQTAIGDALGVAVKLLDNS--LETDAAKMAILLTDGNdtaSKLDPKVAAQLAAAHHVMvHTIAFGdenSSEEDKVDT 188
Cdd:cd01476    75 FIGGTTATGAAIEVALQQLDPSegRREGIPKVVVVLTDGR---SHDDPEKQARILRAVPNI-ETFAVG---TGDPGTVDT 147


                  ....*..
gi 2513403868 189 GLLTDIA 195
Cdd:cd01476   148 EELHSIT 154
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 36-182 1.20e-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: 44.81  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMEKSSGQNeqtrLQAVQQTARTFISqrKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMIGQQ 115
Cdd:cd01474     6 DLYFVLDKSGSVAANWIEI----YDFVEQLVDRFNS--PGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2513403868 116 TAIGDALGVAVKLLDNS----LETdaAKMAILLTDG-NDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSE 182
Cdd:cd01474    80 TYIHEGLENANEQIFNRngggRET--VSVIIALTDGqLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQ 149
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 37-153 1.50e-05

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 44.62  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMEKSSGQNEQTRLqavqqtARTFISQ----RKNDRIGLVIFASQAWPFAP----ISEDKQALQSRIDQLA 108
Cdd:cd01473     3 LTLILDESASIGYSNWRKDVIPF------TEKIINNlnisKDKVHVGILLFAEKNRDVVPfsdeERYDKNELLKKINDLK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2513403868 109 PGMI-GQQTAIGDALGVAVK---LLDNSlETDAAKMAILLTDGNDTASK 153
Cdd:cd01473    77 NSYRsGGETYIVEALKYGLKnytKHGNR-RKDAPKVTMLFTDGNDTSAS 124
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
35-152 1.14e-04

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 42.50  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMekSSGQNEQTRLQAVQQTART--FISQRKNDRIGLVIFASQAWPFAPISEDKQALQSRIDQLAPGMI 112
Cdd:COG1721   148 LTVVLLLDTSASM--RFGSGGPSKLDLAVEAAASlaYLALRQGDRVGLLTFGDRVRRYLPPRRGRRHLLRLLEALARLEP 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2513403868 113 GQQTAIGDALGVAVKLLD-NSLetdaakmAILLTDGNDTAS 152
Cdd:COG1721   226 AGETDLAAALRRLARRLPrRSL-------VVLISDFLDPEE 259
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 37-186 1.38e-04

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: 41.18  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMeksSGQNEQtrLQAVQQTARTFISQRKNDRIGLVIFASQAwpFAPISEDKQALQSRIDQLAPGMIGQQT 116
Cdd:cd01462     3 VILLVDQSGSM---YGAPEE--VAKAVALALLRIALAENRDTYLILFDSEF--QTKIVDKTDDLEEPVEFLSGVQLGGGT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 117 AIGDALGVAVKLLDNSLETDAAkmAILLTDGNDTASKLDPKVAAQLAAAHHVMVHTIAFGDENSSEEDKV 186
Cdd:cd01462    76 DINKALRYALELIERRDPRKAD--IVLITDGYEGGVSDELLREVELKRSRVARFVALALGDHGNPGYDRI 143
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 37-150 1.54e-04

VWA subfamily: 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 no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.56  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMEKSSgqneqtrLQAVQQTARTFISQRKND-------RIGLVIFASQAWPFAPISEdkqalqsrIDQLAP 109
Cdd:cd01464     6 IYLLLDTSGSMAGEP-------IEALNQGLQMLQSELRQDpyalesvEISVITFDSAARVIVPLTP--------LESFQP 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2513403868 110 GMIGQQ--TAIGDALGVAVKLLDNSLE-TDAAKMA------ILLTDGNDT 150
Cdd:cd01464    71 PRLTASggTSMGAALELALDCIDRRVQrYRADQKGdwrpwvFLLTDGEPT 120
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 35-182 3.59e-04

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: 40.29  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMekssGQNEQtrlqavqQTARTFISQRKND--------RIGLVIFASQA---WPFAPISeDKQALQSR 103
Cdd:cd01472     1 ADIVFLVDGSESI----GLSNF-------NLVKDFVKRVVERldigpdgvRVGVVQYSDDPrteFYLNTYR-SKDDVLEA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 104 IDQLAPgmIGQQTAIGDALGVAVKLL---DNSLETDAAKMAILLTDGNDTASKLDPkvAAQLAAAhHVMVHTIAFGDENS 180
Cdd:cd01472    69 VKNLRY--IGGGTNTGKALKYVRENLfteASGSREGVPKVLVVITDGKSQDDVEEP--AVELKQA-GIEVFAVGVKNADE 143


                  ..
gi 2513403868 181 SE 182
Cdd:cd01472   144 EE 145
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 37-201 1.50e-03

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: 38.41  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  37 IVLILDVSGSMEKSSgqneqtRLQAVQQTARTFISQ--RKNDRIGLVIFA-SQAWPFAPISEDKQALQSRIDQLAPgmiG 113
Cdd:cd01451     3 VIFVVDASGSMAARH------RMAAAKGAVLSLLRDayQRRDKVALIAFRgTEAEVLLPPTRSVELAKRRLARLPT---G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 114 QQTAIGDALGVAVKLLDNSLETDAAK-MAILLTDGNDTASkLDPKVAAQLAAAHHVMVHTIAF--GDensSEEDKVDTGL 190
Cdd:cd01451    74 GGTPLAAGLLAAYELAAEQARDPGQRpLIVVITDGRANVG-PDPTADRALAAARKLRARGISAlvID---TEGRPVRRGL 149

                         170
                  ....*....|.
gi 2513403868 191 LTDIAAITGGH 201
Cdd:cd01451   150 AKDLARALGGQ 160
VWA_3 pfam13768
von Willebrand factor type A domain;
36-200 2.11e-03

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 37.76  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMeksSGQNEqtrlqAVQQTARTFISQ-RKNDRIGLVIF---ASQAWP-FAPISE-DKQALQSRIDQLAP 109
Cdd:pfam13768   2 DVVIVVDVSSSM---SGEPK-----LQKDALSVALRQlPTGDKFAVLGFgtlPRPLFPgWRVVSPrSLQEAFQFIKTLQP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868 110 GMiGQQTAIGdALGVAVKLLDNSLEtdaAKMAILLTDGNDTaSKLDPKVAAQLAAAHHVMVHTIAFGDEnsseedkVDTG 189
Cdd:pfam13768  74 PL-GGSDLLG-ALKEAVRAPASPGY---IRHVLLLTDGSPM-QGETRVSDLISRAPGKIRFFAYGLGAS-------ISAP 140

                         170
                  ....*....|.
gi 2513403868 190 LLTDIAAITGG 200
Cdd:pfam13768 141 MLQLLAEASNG 151
vWA_ku cd01458
Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to ...
 34-149 2.84e-03

Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks (DSB) in a preferred orientation. DSB's are repaired by either homologues recombination or non-homologues end joining and facilitate repair by the non-homologous end-joining pathway (NHEJ). The Ku heterodimer is required for accurate process that tends to preserve the sequence at the junction. Ku78 is found in all three kingdoms of life. However, only the eukaryotic proteins have a vWA domain fused to them at their N-termini. The vWA domain is not involved in DNA binding but may very likey mediate Ku78's interactions with other proteins. Members of this subgroup lack the conserved MIDAS motif.


Pssm-ID: 238735  Cd Length: 218  Bit Score: 38.11  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  34 MRNIVLILDVSGSMEKSSGQNEQTRLQAVQQTARTFISQ----RKNDRIGLVIF------ASQAW-----------PFAP 92
Cdd:cd01458     1 KESVVFLVDVSPSMFESKDGEYESPFEEALKCIRQLMKSkiisSPKDLVGVVFYgteeskNPVGYeniyvlldldtPGAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  93 ISEDKQAL--QSRIDQLAPGMIGQQTAIGDALGVAVKLL-DNSLETDAAKMaILLTDGND 149
Cdd:cd01458    81 RVEDLKELiePGGLSFAGQVGDSGQVSLSDALWVCLDLFsKGKKKKSHKRI-FLFTNNDD 139
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 36-180 3.55e-03

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: 37.36  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  36 NIVLILDVSGSMeksSGQNEQTRLQAVQQTARTFISQRKND------RIGLVIFASQAWPFAPISEDKQ---ALQSRIDQ 106
Cdd:cd01480     4 DITFVLDSSESV---GLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAGFLRDIRnytSLKEAVDN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2513403868 107 LApgMIGQQTAIGDALGVAVKLLDNSLETDAAKMAILLTDGNDTASKLD-PKVAAQLAAAHHVMVHTIAFGDENS 180
Cdd:cd01480    81 LE--YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSPDGgIEKAVNEADHLGIKIFFVAVGSQNE 153
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 35-153 5.57e-03

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 36.99  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513403868  35 RNIVLILDVSGSMeksSGQneqtRLQAVQQTARTFISQ-RKNDRIGLVIFASQAWPFAPISED---------KQALQSRI 104
Cdd:cd01463    14 KDIVILLDVSGSM---TGQ----RLHLAKQTVSSILDTlSDNDFFNIITFSNEVNPVVPCFNDtlvqattsnKKVLKEAL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2513403868 105 DQLAPGMIGQQTAigdALGVAVKLLDNSLETDAA-------KMAILLTDGNDTASK 153
Cdd:cd01463    87 DMLEAKGIANYTK---ALEFAFSLLLKNLQSNHSgsrsqcnQAIMLITDGVPENYK 139
 
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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