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Conserved domains on  [gi|2668716271|ref|WP_330584186|]
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VWA domain-containing protein [Coprococcus comes]

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 ...
 7-100 9.85e-17

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 cd01454:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 174  Bit Score: 71.59  E-value: 9.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   7 YRLMDMCDRNGNRDGAALRFVAEHLCTRPELQKLLILISDGQPADYGYS--GTEAEADLRGIKKEYEKRDVILFAAAIG- 83
Cdd:cd01454    73 KRLAALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYegNVFATEDALRAVIEARKLGIEVFGITIDr 152

                          90       100
                  ....*....|....*....|..
gi 2668716271  84 ----DDKENIRRIY-KDGFLDI 100
Cdd:cd01454   153 dattVDKEYLKNIFgEEGYALI 174
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 7-100 9.85e-17

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 71.59  E-value: 9.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   7 YRLMDMCDRNGNRDGAALRFVAEHLCTRPELQKLLILISDGQPADYGYS--GTEAEADLRGIKKEYEKRDVILFAAAIG- 83
Cdd:cd01454    73 KRLAALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYegNVFATEDALRAVIEARKLGIEVFGITIDr 152

                          90       100
                  ....*....|....*....|..
gi 2668716271  84 ----DDKENIRRIY-KDGFLDI 100
Cdd:cd01454   153 dattVDKEYLKNIFgEEGYALI 174
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
1-116 2.90e-13

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 64.35  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   1 MDNEDCYRLMDMCDRNGNRDGAALRFVAEHLCTRPELQKLLILISDGQPADY-GYSGTEAEADLRGIKKEYEKRDVILFA 79
Cdd:COG4548   318 YDDAVRARIAGLEPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIdVYEGRYGIEDTRQAVREARRAGIHPFC 397

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2668716271  80 AAIG-DDKENIRRIY-KDGFLDITKLEELPKNMAQLVKQ 116
Cdd:COG4548   398 ITIDpEADDYLPRIFgRGGYTVIDDVERLPERLPQLYRR 436
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
 18-106 1.16e-08

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 50.80  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271  18 NRDGAALRFVAEHLCTRPELQKLLILISDGQPADYGYSGTEA----EADLRGIKKEYEKR-DVILFAAAIGDDKEniRRI 92
Cdd:pfam11775 116 NIDGEALAQAAKLFAGRMEDKKILLMISDGAPCDDSTLSVAAgdgfEEHLRHIIEEIETLsDIDLIAIGIGHDAP--RRY 193

                          90
                  ....*....|....
gi 2668716271  93 YKDGFLdITKLEEL 106
Cdd:pfam11775 194 YKNAAL-INDAEEL 206
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 21-114 3.03e-06

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: 43.60  E-value: 3.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   21 GAALRFVAEHLCT-----RPELQKLLILISDGQPadygysgTEAEADLRGIKKEYEKRDVILFAAAIGD--DKENIRRIY 93
Cdd:smart00327  82 GAALQYALENLFSksagsRRGAPKVVILITDGES-------NDGPKDLLKAAKELKRSGVKVFVVGVGNdvDEEELKKLA 154

                           90       100
                   ....*....|....*....|.
gi 2668716271   94 KDGFLDITKLEELPKNMAQLV 114
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 7-100 9.85e-17

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 71.59  E-value: 9.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   7 YRLMDMCDRNGNRDGAALRFVAEHLCTRPELQKLLILISDGQPADYGYS--GTEAEADLRGIKKEYEKRDVILFAAAIG- 83
Cdd:cd01454    73 KRLAALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYegNVFATEDALRAVIEARKLGIEVFGITIDr 152

                          90       100
                  ....*....|....*....|..
gi 2668716271  84 ----DDKENIRRIY-KDGFLDI 100
Cdd:cd01454   153 dattVDKEYLKNIFgEEGYALI 174
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
1-116 2.90e-13

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 64.35  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   1 MDNEDCYRLMDMCDRNGNRDGAALRFVAEHLCTRPELQKLLILISDGQPADY-GYSGTEAEADLRGIKKEYEKRDVILFA 79
Cdd:COG4548   318 YDDAVRARIAGLEPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIdVYEGRYGIEDTRQAVREARRAGIHPFC 397

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2668716271  80 AAIG-DDKENIRRIY-KDGFLDITKLEELPKNMAQLVKQ 116
Cdd:COG4548   398 ITIDpEADDYLPRIFgRGGYTVIDDVERLPERLPQLYRR 436
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
 18-106 1.16e-08

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 50.80  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271  18 NRDGAALRFVAEHLCTRPELQKLLILISDGQPADYGYSGTEA----EADLRGIKKEYEKR-DVILFAAAIGDDKEniRRI 92
Cdd:pfam11775 116 NIDGEALAQAAKLFAGRMEDKKILLMISDGAPCDDSTLSVAAgdgfEEHLRHIIEEIETLsDIDLIAIGIGHDAP--RRY 193

                          90
                  ....*....|....
gi 2668716271  93 YKDGFLdITKLEEL 106
Cdd:pfam11775 194 YKNAAL-INDAEEL 206
VWA pfam00092
von Willebrand factor type A domain;
21-92 1.97e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 44.19  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2668716271  21 GAALRFVAEHLCT-----RPELQKLLILISDGQPADYgysgteaeaDLRGIKKEYEKRDVILFAAAIG-DDKENIRRI 92
Cdd:pfam00092  82 GKALKYALENLFSsaagaRPGAPKVVVLLTDGRSQDG---------DPEEVARELKSAGVTVFAVGVGnADDEELRKI 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 21-114 3.03e-06

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: 43.60  E-value: 3.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271   21 GAALRFVAEHLCT-----RPELQKLLILISDGQPadygysgTEAEADLRGIKKEYEKRDVILFAAAIGD--DKENIRRIY 93
Cdd:smart00327  82 GAALQYALENLFSksagsRRGAPKVVILITDGES-------NDGPKDLLKAAKELKRSGVKVFVVGVGNdvDEEELKKLA 154

                           90       100
                   ....*....|....*....|.
gi 2668716271   94 KDGFLDITKLEELPKNMAQLV 114
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
21-92 3.55e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.06  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271  21 GAALRFVAEHLCTR---------PELQKLLILISDGQPADYGYsgteaEADLRGIKKEYEKRDVILFAAAIGD--DKENI 89
Cdd:COG4245    84 GAALELLLDLIERRvqkytaegkGDWRPVVFLITDGEPTDSDW-----EAALQRLKDGEAAKKANIFAIGVGPdaDTEVL 158


                  ...
gi 2668716271  90 RRI 92
Cdd:COG4245   159 KQL 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 15-92 3.59e-05

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 40.73  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271  15 RNGN-RDGAALRFVAEHLCT-----RPELQKLLILISDGQPADygysgteaeaDLRGIKKEYEKRDVILFAAAIGD-DKE 87
Cdd:cd01482    75 KGGNtRTGKALTHVREKNFTpdagaRPGVPKVVILITDGKSQD----------DVELPARVLRNLGVNVFAVGVKDaDES 144


                  ....*
gi 2668716271  88 NIRRI 92
Cdd:cd01482   145 ELKMI 149
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 21-92 4.26e-05

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: 40.35  E-value: 4.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668716271  21 GAALRFVAEHL----CTRPELQKLLILISDGQPADYGysgteaeaDLRGIKKEYEKRDVILFAAAIGD-DKENIRRI 92
Cdd:cd01450    83 GKALQYALEQLfsesNARENVPKVIIVLTDGRSDDGG--------DPKEAAAKLKDEGIKVFVVGVGPaDEEELREI 151
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-88 4.61e-04

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: 37.55  E-value: 4.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2668716271  17 GNRDGAALRFVAEHL--CTRPELQKLLILISDGQPADYGYSGTEAEADLRgikkeyeKRDVILFAAAIGDDKEN 88
Cdd:cd00198    79 GTNIGAALRLALELLksAKRPNARRVIILLTDGEPNDGPELLAEAARELR-------KLGITVYTIGIGDDANE 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 21-113 1.99e-03

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: 36.07  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668716271  21 GAALRFVAEHLC-TRPELQKLLILISDGQPadygysgTEAEADLRGIKKEYEKRDVILFAAAIGD---DKENIRRIYKDG 96
Cdd:COG1240   169 GDALALALELLKrADPARRKVIVLLTDGRD-------NAGRIDPLEAAELAAAAGIRIYTIGVGTeavDEGLLREIAEAT 241

                          90       100
                  ....*....|....*....|
gi 2668716271  97 ---FLDITKLEELPKNMAQL 113
Cdd:COG1240   242 ggrYFRADDLSELAAIYREI 261
 
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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