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Conserved domains on  [gi|13938219|gb|AAH07230|]
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COCH protein [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 10652016)

vWA (von Willebrand factor type A) domain-containing protein similar to Homo sapiens type VI collagen alpha 3 chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 164-328 1.80e-80

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: 247.59  E-value: 1.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 13938219 324 RNNGF 328
Cdd:cd01482 160 NVADF 164
LCCL smart00603
LCCL domain;
30-112 5.40e-43

LCCL domain;


:

Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.15  E-value: 5.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219     30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 13938219    108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 366-485 3.59e-41

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: 145.06  E-value: 3.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13938219 446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGP 485
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEP 122
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 164-328 1.80e-80

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: 247.59  E-value: 1.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 13938219 324 RNNGF 328
Cdd:cd01482 160 NVADF 164
LCCL smart00603
LCCL domain;
30-112 5.40e-43

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.15  E-value: 5.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219     30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 13938219    108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
165-309 8.03e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 149.73  E-value: 8.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 243
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13938219   244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 366-485 3.59e-41

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: 145.06  E-value: 3.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13938219 446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGP 485
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEP 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 165-308 4.24e-35

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: 129.11  E-value: 4.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 243
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13938219    244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 308
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
32-121 1.53e-34

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 124.70  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    32 ITCFTRGLDIRK------EKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVD 105
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 13938219   106 ANGIQSQMLSRWSASF 121
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
VWA pfam00092
von Willebrand factor type A domain;
367-485 1.26e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA- 445
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 13938219   446 TGDAISFTVRNVFGPIRESP--NKNFLVIVTDGQSYD-DVQGP 485
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARpgAPKVVVLLTDGRSQDgDPEEV 123
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 367-481 7.74e-29

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: 112.16  E-value: 7.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGTA 445
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 13938219    446 TGDAISFTVRNVFGPIRES--PNKNFLVIVTDGQSYDD 481
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDG 118
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 365-485 9.88e-04

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: 41.08  E-value: 9.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 365 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdySTKENVLAVIRNIRyMSG 442
Cdd:COG1240  92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13938219 443 GTATGDAIsFTVRNVFGPIRESPNKnFLVIVTDGQSYDDVQGP 485
Cdd:COG1240 165 GTPLGDAL-ALALELLKRADPARRK-VIVLLTDGRDNAGRIDP 205
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 164-328 1.80e-80

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: 247.59  E-value: 1.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 13938219 324 RNNGF 328
Cdd:cd01482 160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 164-328 2.47e-62

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: 200.53  E-value: 2.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDkAVC 323
Cdd:cd01472  81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL-YVF 159


                ....*
gi 13938219 324 RNNGF 328
Cdd:cd01472 160 NVADF 164
LCCL smart00603
LCCL domain;
30-112 5.40e-43

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.15  E-value: 5.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219     30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 13938219    108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
165-309 8.03e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 149.73  E-value: 8.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 243
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13938219   244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 366-485 3.59e-41

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: 145.06  E-value: 3.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13938219 446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGP 485
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEP 122
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 164-309 6.51e-40

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: 141.66  E-value: 6.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-S 242
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938219 243 NTGKALKHTAQKFFTvDAGVRKGIPKVVVVFIDGWPSD--DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01450  81 NTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEEL 148
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 165-308 4.24e-35

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: 129.11  E-value: 4.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 243
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13938219    244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 308
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
32-121 1.53e-34

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 124.70  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    32 ITCFTRGLDIRK------EKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVD 105
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 13938219   106 ANGIQSQMLSRWSASF 121
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
VWA pfam00092
von Willebrand factor type A domain;
367-485 1.26e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA- 445
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 13938219   446 TGDAISFTVRNVFGPIRESP--NKNFLVIVTDGQSYD-DVQGP 485
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARpgAPKVVVLLTDGRSQDgDPEEV 123
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 368-485 3.87e-33

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: 123.55  E-value: 3.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 368 IAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTATG 447
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRTG 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13938219 448 DAISFTVRNVFGP---IRESPNKnFLVIVTDGQSYDDVQGP 485
Cdd:cd01482  83 KALTHVREKNFTPdagARPGVPK-VVILITDGKSQDDVELP 122
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 366-481 1.23e-32

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: 122.01  E-value: 1.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSG-GT 444
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13938219 445 ATGDAISFTVRNVFGPIRESPN-KNFLVIVTDGQSYDD 481
Cdd:cd01450  81 NTGKALQYALEQLFSESNARENvPKVIIVLTDGRSDDG 118
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 164-309 2.97e-30

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: 115.50  E-value: 2.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNS- 242
Cdd:cd01481   1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938219 243 NTGKALKHTAQKFFTVDAGVR--KGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01481  81 NTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAEL 149
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 367-481 7.74e-29

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: 112.16  E-value: 7.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219    367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGTA 445
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 13938219    446 TGDAISFTVRNVFGPIRES--PNKNFLVIVTDGQSYDD 481
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDG 118
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 164-309 9.20e-28

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: 110.55  E-value: 9.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13938219 244 TGKALKHTAQKFFTVDAGVRKG---IPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01475  83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEEL 151
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 366-481 4.22e-24

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: 98.97  E-value: 4.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13938219 446 TGDAISFTVRNVFGPIRES-PN-KNFLVIVTDGQSYDD 481
Cdd:cd01469  81 TATAIQYVVTELFSESNGArKDaTKVLVVITDGESHDD 118
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 164-312 2.45e-23

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: 96.31  E-value: 2.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRrFNLQKNFVGKVALMLGIGTEGPHVGLVQAS--EHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN 241
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13938219 242 SNTGKALKHTAQkFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVARE-FGVNVFIVSVAKPIP---EELGMV 312
Cdd:cd01476  80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDPGTvdtEELHSI 153
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 366-483 4.09e-23

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: 97.46  E-value: 4.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13938219 446 TGDAISFTVRNVFG------PIRESPNKnFLVIVTDGQSYDDVQ 483
Cdd:cd01475  83 TGLAIQYAMNNAFSeaegarPGSERVPR-VGIVVTDGRPQDDVS 125
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 366-485 5.39e-23

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: 95.33  E-value: 5.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGT 444
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13938219 445 ATGDAISfTVRNVFGPIRESPNKNFLVIVTDGQSYDDVQGP 485
Cdd:cd00198  81 NIGAALR-LALELLKSAKRPNARRVIILLTDGEPNDGPELL 120
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 164-309 1.29e-21

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: 91.47  E-value: 1.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFR-GGNS 242
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 243 NTGKALKHTAQKFFtvdAGVRKGIPKVVVVFIDGWPSDD---IEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd00198  81 NIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDE 147
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 367-485 1.43e-21

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: 91.23  E-value: 1.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMsGGTA- 445
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLR-GGSQl 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13938219 446 -TGDAISFTVRNVF-----GPIRESPNKnFLVIVTDGQSYDDVQGP 485
Cdd:cd01481  81 nTGSALDYVVKNLFtksagSRIEEGVPQ-FLVLITGGKSQDDVERP 125
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 165-281 9.13e-21

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: 89.34  E-value: 9.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNT 244
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13938219 245 GKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDD 281
Cdd:cd01469  82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDD 118
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 366-479 4.22e-18

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: 82.05  E-value: 4.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTF------EISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAV-IRNIR 438
Cdd:cd01480   3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13938219 439 YMSGGTATGDAISFTVRNvfgpIRESP---NKNFLVIVTDGQSY 479
Cdd:cd01480  83 YIGGGTFTDCALKYATEQ----LLEGShqkENKFLLVITDGHSD 122
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 367-485 5.71e-15

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: 72.43  E-value: 5.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 367 NIAFLIDGSSSVGDSnFRLMLEFVSNIAKTFEISDIGAKIAAVQFT--YDQRTEFSFTDYSTKENVLAVIRNIRYMSGGT 444
Cdd:cd01476   2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13938219 445 ATGDAISFTVRNVFG--PIRESPNKNfLVIVTDGQSYDDVQGP 485
Cdd:cd01476  81 ATGAAIEVALQQLDPseGRREGIPKV-VVVLTDGRSHDDPEKQ 122
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 162-309 3.20e-13

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: 68.18  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 162 CKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGP------HVGLVQASEHPKIEF----YLKNFTSAKDvlfA 231
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAgflrDIRNYTSLKE---A 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 232 IKEVGFRGGNSNTGKALKHTAQKFFTvdaGVRKGIPKVVVVFIDGWP--SDD--IEEAGIVAREFGVNVFIVSVAKPIPE 307
Cdd:cd01480  78 VDNLEYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSdgSPDggIEKAVNEADHLGIKIFFVAVGSQNEE 154


                ..
gi 13938219 308 EL 309
Cdd:cd01480 155 PL 156
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 165-301 1.65e-10

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 60.09  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 165 DIAFLIDGSFNIG-QRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLK--NFTSAKDVLFAI---KEVGFR 238
Cdd:cd01471   2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspNSTNKDLALNAIralLSLYYP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13938219 239 GGNSNTGKALKHTAQKFFTVdAGVRKGIPKVVVVFIDGWPSDD---IEEAGiVAREFGVNVFIVSV 301
Cdd:cd01471  82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrtLKEAR-KLRERGVIIAVLGV 145
VWA_2 pfam13519
von Willebrand factor type A domain;
166-273 5.98e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.15  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   166 IAFLIDGSF-----NIGQRRFNLQKNFVgkVALMLGIGTEgpHVGLVQASEHPKIEFYLKnfTSAKDVLFAIKEVGFRGG 240
Cdd:pfam13519   1 LVFVLDTSGsmrngDYGPTRLEAAKDAV--LALLKSLPGD--RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 13938219   241 NSNTGKALKhTAQKFFtvdAGVRKGIPKVVVVF 273
Cdd:pfam13519  75 GTNLAAALQ-LARAAL---KHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 366-483 3.70e-09

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: 56.24  E-value: 3.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 366 VNIAFLIDGSSSVGDSN-FRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSF-----TDYSTKENVLAVIRNIRY 439
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLsspnsTNKDLALNAIRALLSLYY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 13938219 440 MSGGTATGDAISFTVRNVFGPIRESPNKNFLVIV-TDGQSYDDVQ 483
Cdd:cd01471  81 PNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIImTDGIPDSKFR 125
VWA_2 pfam13519
von Willebrand factor type A domain;
368-472 7.09e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219   368 IAFLIDGSSSVGD-----SNFRLMLEFVSNIAKTFEISdigaKIAAVQFTYDQRTEFSFTDysTKENVLAVIRNIRYMSG 442
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 13938219   443 GTATGDAISFtVRNVFGPIRESPNKNFLVI 472
Cdd:pfam13519  75 GTNLAAALQL-ARAALKHRRKNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 365-485 9.88e-04

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: 41.08  E-value: 9.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 365 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdySTKENVLAVIRNIRyMSG 442
Cdd:COG1240  92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13938219 443 GTATGDAIsFTVRNVFGPIRESPNKnFLVIVTDGQSYDDVQGP 485
Cdd:COG1240 165 GTPLGDAL-ALALELLKRADPARRK-VIVLLTDGRDNAGRIDP 205
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 165-351 1.91e-03

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: 39.61  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 165 DIAFLIDGSFNIGQRRFNLQ-KNFVGKVALMLGIGTEGPHVGLVQASEHPK--IEFYLKNFTSAKDVLFAIKEVG---FR 238
Cdd:cd01473   2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKnsyRS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 239 GGNSNTGKALKHTAQKFFTvDAGVRKGIPKVVVVFIDG---WPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQD 314
Cdd:cd01473  82 GGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtSASKkELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13938219 315 vtfvdkavCR-NNGFFSYHMPNWFGTTKYV-KPLVQKLC 351
Cdd:cd01473 161 --------CDiNNDNCPNVIKTEWNNLNGIsKFLTDKIC 191
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 362-482 2.14e-03

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: 39.42  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 362 CYNSVNIAFLIDGSSSVGDSNFRLMlEFVSNIAKTFeiSDIGAKIAAVQFTYDQRTEFSFTDYSTKENV-LAVIRNIrYM 440
Cdd:cd01474   1 CAGHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKV-TP 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13938219 441 SGGTATGDAISFTVRNVFGPIRESPNKNFLVI-VTDGQSYDDV 482
Cdd:cd01474  77 SGQTYIHEGLENANEQIFNRNGGGRETVSVIIaLTDGQLLLNG 119
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 165-302 8.21e-03

VWA F09G8.8 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 37.40  E-value: 8.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13938219 165 DIAFLIDGSFNIGQRRFNLQKNFVGKV---ALMLGIGTEGPH---VGLVQASEHPKIEFYLKNFTSAKDV---LFAIKEV 235
Cdd:cd01477  21 DIVFVVDNSKGMTQGGLWQVRATISSLfgsSSQIGTDYDDPRstrVGLVTYNSNATVVADLNDLQSFDDLysqIQGSLTD 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13938219 236 GFRGGNSNTGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREF-GVNVFIVSVA 302
Cdd:cd01477 101 VSSTNASYLDTGLQAAEQMLAAGKRTSRENYKKVVIVFASDYNDEGSNDPRPIAARLkSTGIAIITVA 168
 
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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