NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157834404|pdb|1ZON|A]
View 

Chain A, LEUKOCYTE ADHESION GLYCOPROTEIN

Protein Classification

vWA domain-containing protein( domain architecture ID 10106978)

vWA (von Willebrand factor type A) domain-containing protein similar to mammalian alpha subunits of integrins

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 6-174 2.01e-82

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


:

Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 241.49  E-value: 2.01e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 83
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       84 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 157
Cdd:cd01469  81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                       170
                ....*....|....*..
1ZON_A      158 ASEFVKILDTFEKLKDL 174
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 6-174 2.01e-82

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 241.49  E-value: 2.01e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 83
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       84 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 157
Cdd:cd01469  81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                       170
                ....*....|....*..
1ZON_A      158 ASEFVKILDTFEKLKDL 174
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
7-177 1.56e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 142.80  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          7 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 81
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A         82 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFAS 155
Cdd:pfam00092  78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
1ZON_A        156 KPASEFVKILDTFEKLKDLFTE 177
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-171 6.97e-34

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: 118.33  E-value: 6.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A           7 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 81
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          82 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKF 153
Cdd:smart00327  78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKL 153

                          170
                   ....*....|....*...
1ZON_A         154 ASKPASEFVKILDTFEKL 171
Cdd:smart00327 154 ASAPGGVYVFLPELLDLL 171
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 6-178 6.63e-08

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: 51.09  E-value: 6.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFD--GSMSLQPDefqkiLDFMKDVMKKLSNtSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDALLKHVKHML 79
Cdd:COG1240  93 RDVVLVVDasGSMAAENR-----LEAAKGALLDFLD-DYRprdrVGLVAFGGEAEVLLPLTR-----DREALKRALDELP 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       80 L--LTNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETL 150
Cdd:COG1240 162 PggGTPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLL 234

                       170       180
                ....*....|....*....|....*...
1ZON_A      151 HKFASKPASEFVKILDTfEKLKDLFTEL 178
Cdd:COG1240 235 REIAEATGGRYFRADDL-SELAAIYREI 261
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 8-140 2.15e-04

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: 40.75  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          8 LVFLFDGSMSLQPDefqkiLDFMKDVMKKLSNTSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDAL---LKHVKHMLL 80
Cdd:TIGR03436  56 VGLVIDTSGSMRND-----LDRARAAAIRFLKTVLRpndrVFVVTFNTRLRLLQDFTS-----DPRLLeaaLNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A         81 L--------------TNTFGAINYVATEVFREELGARPDaTKVLIIITDGEATDSGN-----IDAAK--DIIRYIIGIGK 139
Cdd:TIGR03436 126 TdynssgafvrdgggTALYDAITLAALEQLANALAGIPG-RKALIVISDGGDNRSRDtleraIDAAQraDVAIYSIDARG 204


                  .
1ZON_A        140 H 140
Cdd:TIGR03436 205 L 205
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 6-174 2.01e-82

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 241.49  E-value: 2.01e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 83
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       84 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 157
Cdd:cd01469  81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                       170
                ....*....|....*..
1ZON_A      158 ASEFVKILDTFEKLKDL 174
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
7-177 1.56e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 142.80  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          7 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 81
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A         82 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFAS 155
Cdd:pfam00092  78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
1ZON_A        156 KPASEFVKILDTFEKLKDLFTE 177
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 7-171 6.97e-34

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: 118.33  E-value: 6.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A           7 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 81
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          82 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKF 153
Cdd:smart00327  78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKL 153

                          170
                   ....*....|....*...
1ZON_A         154 ASKPASEFVKILDTFEKL 171
Cdd:smart00327 154 ASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 6-162 7.16e-33

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: 115.08  E-value: 7.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL-- 81
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpDKTRVGLVQYSDDVRVEFSLNDY---KSKDDLLKAVKNLKYLgg 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       82 --TNTFGAINYVATEVFREElGARPDATKVLIIITDGEATDSGNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKF 153
Cdd:cd01450  78 ggTNTGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKdegikvFVVGVGPA-----DEEELREI 151


                ....*....
1ZON_A      154 ASKPASEFV 162
Cdd:cd01450 152 ASCPSERHV 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 6-168 7.38e-28

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: 102.31  E-value: 7.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL-- 81
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTYRSKDD---VLEAVKNLRYIgg 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       82 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKD----IIRYIIGIGKHfqtkeSQETLHKFASK 156
Cdd:cd01472  78 gTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELkqagIEVFAVGVKNA-----DEEELKQIASD 152

                       170
                ....*....|..
1ZON_A      157 PASEFVKILDTF 168
Cdd:cd01472 153 PKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 4-182 2.82e-27

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: 102.46  E-value: 2.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        4 GNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLL 81
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLdvGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       82 TNTFGAINYVATEVFREELGARPDAT---KVLIIITDGEATDSGNIDAAK----DIIRYIIGIGkhfqtKESQETLHKFA 154
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKaralGIEMFAVGVG-----RADEEELREIA 155

                       170       180
                ....*....|....*....|....*...
1ZON_A      155 SKPASEFVKILDTFEKLKDLFTELQKKI 182
Cdd:cd01475 156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 7-168 8.59e-27

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: 99.67  E-value: 8.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        7 DLVFLFDGSMSLQPDEFQKILDFMKDVMK--KLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL--- 81
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEafEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKED---VLAAIKNLPYKggn 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       82 TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDsgNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKFAS 155
Cdd:cd01482  79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD--DVELPARVLRnlgvnvFAVGVKDA-----DESELKMIAS 151

                       170
                ....*....|...
1ZON_A      156 KPASEFVKILDTF 168
Cdd:cd01482 152 KPSETHVFNVADF 164
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 6-162 9.56e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 70.67  E-value: 9.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTS--YQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLL-LT 82
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGgGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       83 NTFGAINYVATEVFREelgARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKFAS 155
Cdd:cd00198  81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPEllaeaARELRKlgITVYTIGIGDDANEDE----LKEIAD 153


                ....*..
1ZON_A      156 KPASEFV 162
Cdd:cd00198 154 KTTGGAV 160
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 7-121 2.10e-15

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 70.05  E-value: 2.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        7 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKLS--NTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLLT-- 82
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTKAD---VLGAVRRLRLRGgs 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1ZON_A       83 --NTFGAINYVATEVFREELGARPD--ATKVLIIITDGEATDS 121
Cdd:cd01481  79 qlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQDD 121
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 7-161 9.82e-12

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: 60.11  E-value: 9.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        7 DLVFLFDGSMSLQpDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKT--EFDFSDYVKRKDPDALLKHVKHMLLLT 82
Cdd:cd01476   2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIgpTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       83 NTFGAINYvATEVFREELGARPDATKVLIIITDGEATDsgNIDAAKDIIR-----YIIGIGKHFQTKESQETLHKFASKP 157
Cdd:cd01476  81 ATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRavpniETFAVGTGDPGTVDTEELHSITGNE 157


                ....
1ZON_A      158 ASEF 161
Cdd:cd01476 158 DHIF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 6-138 6.10e-08

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 50.08  E-value: 6.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFDGSMSL-QPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvKRKDPDALLKHVKHMLLL- 81
Cdd:cd01471   1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLSLy 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1ZON_A       82 -----TNTFGAINYVATEVFrEELGARPDATKVLIIITDGEA-TDSGNIDAAKDI-----IRYIIGIG 138
Cdd:cd01471  80 ypngsTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPdSKFRTLKEARKLrergvIIAVLGVG 146
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 6-178 6.63e-08

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: 51.09  E-value: 6.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        6 VDLVFLFD--GSMSLQPDefqkiLDFMKDVMKKLSNtSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDALLKHVKHML 79
Cdd:COG1240  93 RDVVLVVDasGSMAAENR-----LEAAKGALLDFLD-DYRprdrVGLVAFGGEAEVLLPLTR-----DREALKRALDELP 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       80 L--LTNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETL 150
Cdd:COG1240 162 PggGTPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLL 234

                       170       180
                ....*....|....*....|....*...
1ZON_A      151 HKFASKPASEFVKILDTfEKLKDLFTEL 178
Cdd:COG1240 235 REIAEATGGRYFRADDL-SELAAIYREI 261
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 4-129 1.25e-07

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: 49.31  E-value: 1.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        4 GNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLS--------NTSYQFAAVQFSTSYKTEFDFSDYVkrKDPDALLKHV 75
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkdpAGSWRVGVVQYSDQQEVEAGFLRDI--RNYTSLKEAV 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       76 KHMLLL---TNTFGAINYVaTEVFREelGARPDATKVLIIITDGE---ATDSGNIDAAKD 129
Cdd:cd01480  79 DNLEYIgggTFTDCALKYA-TEQLLE--GSHQKENKFLLVITDGHsdgSPDGGIEKAVNE 135
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 4-181 4.90e-07

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: 47.89  E-value: 4.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        4 GNVDLVFLFDGSMSLQpDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYvkRKDPDALLKHVKHMLL--L 81
Cdd:cd01474   3 GHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDD--SSAIIKGLEVLKKVTPsgQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       82 TNTFGAINYVATEVFREELGARPDAtKVLIIITDGEATDSGNIDAAKD--------IIRYIIGIgkhfqTKESQETLHKF 153
Cdd:cd01474  80 TYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHEaklsrklgAIVYCVGV-----TDFLKSQLINI 153

                       170       180
                ....*....|....*....|....*...
1ZON_A      154 ASKPASEFvKILDTFEKLKDLFTELQKK 181
Cdd:cd01474 154 ADSKEYVF-PVTSGFQALSGIIESVVKK 180
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 8-140 2.15e-04

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: 40.75  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A          8 LVFLFDGSMSLQPDefqkiLDFMKDVMKKLSNTSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDAL---LKHVKHMLL 80
Cdd:TIGR03436  56 VGLVIDTSGSMRND-----LDRARAAAIRFLKTVLRpndrVFVVTFNTRLRLLQDFTS-----DPRLLeaaLNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A         81 L--------------TNTFGAINYVATEVFREELGARPDaTKVLIIITDGEATDSGN-----IDAAK--DIIRYIIGIGK 139
Cdd:TIGR03436 126 TdynssgafvrdgggTALYDAITLAALEQLANALAGIPG-RKALIVISDGGDNRSRDtleraIDAAQraDVAIYSIDARG 204


                  .
1ZON_A        140 H 140
Cdd:TIGR03436 205 L 205
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
5-175 5.18e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.14  E-value: 5.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        5 NVDLVFLFD--GSMSLQP-----DEFQKILD-FMKDvmkKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDallkhvk 76
Cdd:COG4245   5 RLPVYLLLDtsGSMSGEPiealnEGLQALIDeLRQD---PYALETVEVSVITFDGEAKVLLPLTDLEDFQPPD------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A       77 hmlL----LTNTFGAINYVATEVFREELGARPDAT----KVLIIITDGEATDSG---------NIDAAKDIIRYIIGIGk 139
Cdd:COG4245  75 ---LsasgGTPLGAALELLLDLIERRVQKYTAEGKgdwrPVVFLITDGEPTDSDweaalqrlkDGEAAKKANIFAIGVG- 150

                       170       180       190
                ....*....|....*....|....*....|....*...
1ZON_A      140 hfqTKESQETLHKFASKpasefVKILDT--FEKLKDLF 175
Cdd:COG4245 151 ---PDADTEVLKQLTDP-----VRALDAldGLDFREFF 180
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 7-138 9.97e-04

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 38.89  E-value: 9.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZON_A        7 DLVFLFD--GSMSLQPDEFQK--ILDFMKDVMKKLsntsyQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMlllT 82
Cdd:COG2425 120 PVVLCVDtsGSMAGSKEAAAKaaALALLRALRPNR-----RFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGg-gT 193

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1ZON_A       83 NTFGAINYVAtevfrEELGARPDATKVLIIITDGEATDSGN-----IDAAKDIIR-YIIGIG 138
Cdd:COG2425 194 DIAPALRAAL-----ELLEEPDYRNADIVLITDGEAGVSPEellreVRAKESGVRlFTVAIG 250
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 87-135 2.40e-03

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: 36.92  E-value: 2.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
1ZON_A       87 AINYVAtevfrEELGARPDATKVLIIITDGE----ATDSGNIDAAKDIIRYII 135
Cdd:cd01454  89 AIRHAA-----ERLLARPEKRKILLVISDGEpndlDYYEGNVFATEDALRAVI 136
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH