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Conserved domains on  [gi|4758022|ref|NP_004077|]
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cochlin isoform b precursor [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 9.04e-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: 247.20  E-value: 9.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 4758022  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 ...
 366-527 3.52e-58

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: 190.90  E-value: 3.52e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFF 523
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                ....
gi 4758022  524 TREF 527
Cdd:cd01472 161 VADF 164
LCCL smart00603
LCCL domain;
30-112 6.74e-43

LCCL domain;


:

Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.92  E-value: 6.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022      30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 4758022     108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
 
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 9.04e-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: 247.20  E-value: 9.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 4758022  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 ...
 366-527 3.52e-58

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: 190.90  E-value: 3.52e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFF 523
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                ....
gi 4758022  524 TREF 527
Cdd:cd01472 161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
367-536 3.77e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 167.45  E-value: 3.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA- 445
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    446 TGDAISFTVRNVFGPIRESP--NKNFLVIVTDGQSYD-DVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAF 522
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 4758022    523 FTREFTGLEPIVSD 536
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
LCCL smart00603
LCCL domain;
30-112 6.74e-43

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.92  E-value: 6.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022      30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 4758022     108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
165-309 1.81e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 149.73  E-value: 1.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 243
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758022    244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 367-527 1.90e-37

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: 136.43  E-value: 1.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGTA 445
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     446 TGDAISFTVRNVFGPIRES--PNKNFLVIVTDGQSYD---DVQGPAAAAHDAGITIFSVGV-AWAPLDDLKDMASKPKES 519
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGV 160


                   ....*...
gi 4758022     520 HAFFTREF 527
Cdd:smart00327 161 YVFLPELL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 165-308 1.12e-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: 128.73  E-value: 1.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 243
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758022     244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 308
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
32-121 1.47e-34

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 125.47  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     32 ITCFTRGLDIRK------EKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVD 105
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 4758022    106 ANGIQSQMLSRWSASF 121
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 365-513 1.40e-09

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: 59.18  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  365 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdySTKENVLAVIRNIRyMSG 442
Cdd:COG1240  92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758022  443 GTATGDAIsFTVRNVFGPIRESPNKnFLVIVTDGQSYDDVQGP---AAAAHDAGITIFSVGVAWAPLDD--LKDMA 513
Cdd:COG1240 165 GTPLGDAL-ALALELLKRADPARRK-VIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA 238
PRK09193 PRK09193
indolepyruvate ferredoxin oxidoreductase; Validated
 455-549 8.51e-03

indolepyruvate ferredoxin oxidoreductase; Validated


Pssm-ID: 236404 [Multi-domain]  Cd Length: 1165  Bit Score: 39.04  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    455 RNVFGpireSPNKNFLvIVTDGQSYDDVQGP-------AAAAHDAGITIFSVGVAWaPLDdlkdmaskPKEshaffTREF 527
Cdd:PRK09193  275 RVVID----SPNARLG-IVAAGKAYLDVRQAlrdlgldEETAARLGIRLYKVGMVW-PLE--------PQG-----VRAF 335

                          90       100
                  ....*....|....*....|....*
gi 4758022    528 -TGLEPIVsdVI--RgicRDFLESQ 549
Cdd:PRK09193  336 aEGLDEIL--VVeeK---RQIIEYQ 355
 
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 9.04e-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: 247.20  E-value: 9.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKaVC 323
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VF 159


                ....*
gi 4758022  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 1.03e-61

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: 1.03e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDkAVC 323
Cdd:cd01472  81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL-YVF 159


                ....*
gi 4758022  324 RNNGF 328
Cdd:cd01472 160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 366-527 3.52e-58

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: 190.90  E-value: 3.52e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNVFGPI--RESPNKNFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFF 523
Cdd:cd01472  81 TGKALKYVRENLFTEAsgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                ....
gi 4758022  524 TREF 527
Cdd:cd01472 161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
367-536 3.77e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 167.45  E-value: 3.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA- 445
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    446 TGDAISFTVRNVFGPIRESP--NKNFLVIVTDGQSYD-DVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAF 522
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARpgAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 4758022    523 FTREFTGLEPIVSD 536
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 368-527 7.08e-45

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: 155.91  E-value: 7.08e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  368 IAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTATG 447
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRTG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  448 DAISFTVRNVFGP---IRESPNKnFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFFT 524
Cdd:cd01482  83 KALTHVREKNFTPdagARPGVPK-VVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                ...
gi 4758022  525 REF 527
Cdd:cd01482 162 ADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 366-522 8.29e-44

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: 152.83  E-value: 8.29e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSG-GT 444
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  445 ATGDAISFTVRNVFGPIRESPN-KNFLVIVTDGQSYD--DVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHA 521
Cdd:cd01450  81 NTGKALQYALEQLFSESNARENvPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERHV 160


                .
gi 4758022  522 F 522
Cdd:cd01450 161 F 161
LCCL smart00603
LCCL domain;
30-112 6.74e-43

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 147.92  E-value: 6.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022      30 IAITCFTRGLDIRKEKAD--VLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDAN 107
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 4758022     108 GIQSQ 112
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
165-309 1.81e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 149.73  E-value: 1.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-SN 243
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGtTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758022    244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEEL 147
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 164-309 1.15e-39

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: 1.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN-S 242
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758022  243 NTGKALKHTAQKFFTvDAGVRKGIPKVVVVFIDGWPSD--DIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01450  81 NTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEEL 148
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 366-544 2.06e-39

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: 143.29  E-value: 2.06e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNVFG------PIRESPNKnFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKES 519
Cdd:cd01475  83 TGLAIQYAMNNAFSeaegarPGSERVPR-VGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                       170       180
                ....*....|....*....|....*
gi 4758022  520 HAFFTREFTGLEPIVSDVIRGICRD 544
Cdd:cd01475 162 HVFYVEDFSTIEELTKKFQGKICVV 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 367-527 1.90e-37

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: 136.43  E-value: 1.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGTA 445
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     446 TGDAISFTVRNVFGPIRES--PNKNFLVIVTDGQSYD---DVQGPAAAAHDAGITIFSVGV-AWAPLDDLKDMASKPKES 519
Cdd:smart00327  81 LGAALQYALENLFSKSAGSrrGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGV 160


                   ....*...
gi 4758022     520 HAFFTREF 527
Cdd:smart00327 161 YVFLPELL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 165-308 1.12e-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: 128.73  E-value: 1.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEV-GFRGGNSN 243
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758022     244 TGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSD---DIEEAGIVAREFGVNVFIVSVAKPIPEE 308
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
LCCL pfam03815
LCCL domain;
32-121 1.47e-34

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 125.47  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022     32 ITCFTRGLDIRK------EKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVD 105
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 4758022    106 ANGIQSQMLSRWSASF 121
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 366-533 4.71e-32

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: 121.69  E-value: 4.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTA 445
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNVFGPIRES-PN-KNFLVIVTDGQSYDDVQGPAA--AAHDAGITIFSVGVAWA-----PLDDLKDMASKP 516
Cdd:cd01469  81 TATAIQYVVTELFSESNGArKDaTKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIASKP 160

                       170
                ....*....|....*..
gi 4758022  517 KESHAFFTREFTGLEPI 533
Cdd:cd01469 161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 164-309 6.32e-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: 115.11  E-value: 6.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNS- 242
Cdd:cd01481   1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758022  243 NTGKALKHTAQKFFTVDAGVR--KGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01481  81 NTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAEL 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 366-522 3.46e-29

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: 113.04  E-value: 3.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRY-MSGGT 444
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  445 ATGDAISfTVRNVFGPIRESPNKNFLVIVTDGQSYDDVQGPAAAAHDA---GITIFSVGV-AWAPLDDLKDMASKPKESH 520
Cdd:cd00198  81 NIGAALR-LALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELrklGITVYTIGIgDDANEDELKEIADKTTGGA 159


                ..
gi 4758022  521 AF 522
Cdd:cd00198 160 VF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 367-527 1.51e-27

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: 108.57  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  367 NIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMsGGTA- 445
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLR-GGSQl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 -TGDAISFTVRNVF-----GPIRESPNKnFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPkeS 519
Cdd:cd01481  81 nTGSALDYVVKNLFtksagSRIEEGVPQ-FLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--S 157


                ....*...
gi 4758022  520 HAFFTREF 527
Cdd:cd01481 158 FVFQVSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 164-309 1.56e-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: 110.55  E-value: 1.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSN 243
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758022  244 TGKALKHTAQKFFTVDAGVRKG---IPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd01475  83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEEL 151
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 164-312 3.35e-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: 3.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRrFNLQKNFVGKVALMLGIGTEGPHVGLVQAS--EHPKIEFYLKNFTSAKDVLFAIKEVGFRGGN 241
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758022  242 SNTGKALKHTAQkFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVARE-FGVNVFIVSVAKPIP---EELGMV 312
Cdd:cd01476  80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDPGTvdtEELHSI 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 164-309 2.35e-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: 91.09  E-value: 2.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  164 ADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFR-GGNS 242
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  243 NTGKALKHTAQKFFtvdAGVRKGIPKVVVVFIDGWPSDD---IEEAGIVAREFGVNVFIVSVAKPIPEEL 309
Cdd:cd00198  81 NIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDE 147
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 165-281 1.16e-20

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: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  165 DIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNT 244
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4758022  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 ...
 366-520 1.24e-20

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: 89.75  E-value: 1.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTF------EISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAV-IRNIR 438
Cdd:cd01480   3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  439 YMSGGTATGDAISFTVRNvfgpIRESP---NKNFLVIVTDGQSY-DDVQGPAAAAHDA---GITIFSVGVAWAPLDDLKD 511
Cdd:cd01480  83 YIGGGTFTDCALKYATEQ----LLEGShqkENKFLLVITDGHSDgSPDGGIEKAVNEAdhlGIKIFFVAVGSQNEEPLSR 158


                ....*....
gi 4758022  512 MASKPKESH 520
Cdd:cd01480 159 IACDGKSAL 167
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 367-501 4.94e-17

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: 78.59  E-value: 4.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  367 NIAFLIDGSSSVGDSnFRLMLEFVSNIAKTFEISDIGAKIAAVQFT--YDQRTEFSFTDYSTKENVLAVIRNIRYMSGGT 444
Cdd:cd01476   2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  445 ATGDAISFTVRNVFG--PIRESPNKNfLVIVTDGQSYDDVQGPAAAAH-DAGITIFSVGV 501
Cdd:cd01476  81 ATGAAIEVALQQLDPseGRREGIPKV-VVVLTDGRSHDDPEKQARILRaVPNIETFAVGT 139
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 162-309 4.28e-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: 67.80  E-value: 4.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  162 CKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGP------HVGLVQASEHPKIEF----YLKNFTSAKDvlfA 231
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAgflrDIRNYTSLKE---A 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  232 IKEVGFRGGNSNTGKALKHTAQKFFTvdaGVRKGIPKVVVVFIDGWP--SDD--IEEAGIVAREFGVNVFIVSVAKPIPE 307
Cdd:cd01480  78 VDNLEYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSdgSPDggIEKAVNEADHLGIKIFFVAVGSQNEE 154


                ..
gi 4758022  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 ...
 366-500 8.78e-11

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: 61.25  E-value: 8.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSN-FRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSF-----TDYSTKENVLAVIRNIRY 439
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLsspnsTNKDLALNAIRALLSLYY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758022  440 MSGGTATGDAISFTVRNVFGPIRESPNKNFLVIV-TDGQSYDDVQGPAAAA--HDAG--ITIFSVG 500
Cdd:cd01471  81 PNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIImTDGIPDSKFRTLKEARklRERGviIAVLGVG 146
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 165-301 1.90e-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: 1.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  165 DIAFLIDGSFNIG-QRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLK--NFTSAKDVLFAI---KEVGFR 238
Cdd:cd01471   2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspNSTNKDLALNAIralLSLYYP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758022  239 GGNSNTGKALKHTAQKFFTVdAGVRKGIPKVVVVFIDGWPSDD---IEEAGiVAREFGVNVFIVSV 301
Cdd:cd01471  82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrtLKEAR-KLRERGVIIAVLGV 145
VWA_2 pfam13519
von Willebrand factor type A domain;
166-273 9.02e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.15  E-value: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    166 IAFLIDGSF-----NIGQRRFNLQKNFVgkVALMLGIGTEgpHVGLVQASEHPKIEFYLKnfTSAKDVLFAIKEVGFRGG 240
Cdd:pfam13519   1 LVFVLDTSGsmrngDYGPTRLEAAKDAV--LALLKSLPGD--RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 4758022    241 NSNTGKALKhTAQKFFtvdAGVRKGIPKVVVVF 273
Cdd:pfam13519  75 GTNLAAALQ-LARAAL---KHRRKNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 365-513 1.40e-09

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: 59.18  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  365 SVNIAFLIDGSSSVGDSNfRLmlEFVSNIAKTFeISDI--GAKIAAVQFTYDQRTEFSFTdySTKENVLAVIRNIRyMSG 442
Cdd:COG1240  92 GRDVVLVVDASGSMAAEN-RL--EAAKGALLDF-LDDYrpRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGG 164

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758022  443 GTATGDAIsFTVRNVFGPIRESPNKnFLVIVTDGQSYDDVQGP---AAAAHDAGITIFSVGVAWAPLDD--LKDMA 513
Cdd:COG1240 165 GTPLGDAL-ALALELLKRADPARRK-VIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA 238
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 362-542 7.02e-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: 49.82  E-value: 7.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  362 CYNSVNIAFLIDGSSSVGDSNFRLMlEFVSNIAKTFeiSDIGAKIAAVQFTYDQRTEFSFTDYSTKENV-LAVIRNIrYM 440
Cdd:cd01474   1 CAGHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKV-TP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  441 SGGTATGDAISFTVRNVFGPIRESPNKNFLVI-VTDGQ----SYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASK 515
Cdd:cd01474  77 SGQTYIHEGLENANEQIFNRNGGGRETVSVIIaLTDGQlllnGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                       170       180
                ....*....|....*....|....*...
gi 4758022  516 PKesHAFFTRE-FTGLEPIVSDVIRGIC 542
Cdd:cd01474 157 KE--YVFPVTSgFQALSGIIESVVKKAC 182
VWA_2 pfam13519
von Willebrand factor type A domain;
368-472 1.01e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.29  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    368 IAFLIDGSSSVGD-----SNFRLMLEFVSNIAKTFEISdigaKIAAVQFTYDQRTEFSFTDysTKENVLAVIRNIRYMSG 442
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 4758022    443 GTATGDAISFtVRNVFGPIRESPNKNFLVI 472
Cdd:pfam13519  75 GTNLAAALQL-ARAALKHRRKNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 366-522 4.11e-05

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 44.19  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIgakIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRyMSGGTA 445
Cdd:cd01465   1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDR---LAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  446 TGDAISFTVRNV---FGPIRespnKNFLVIVTDGQSY------DDVQGPAAAAHDAGITIFSVGVAWAPLDDL-KDMASK 515
Cdd:cd01465  77 GGAGIQLGYQEAqkhFVPGG----VNRILLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFGDNYNEDLmEAIADA 152


                ....*..
gi 4758022  516 PKESHAF 522
Cdd:cd01465 153 GNGNTAY 159
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 165-351 1.79e-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: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  165 DIAFLIDGSFNIGQRRFNLQ-KNFVGKVALMLGIGTEGPHVGLVQASEHPK--IEFYLKNFTSAKDVLFAIKEVG---FR 238
Cdd:cd01473   2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKnsyRS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  239 GGNSNTGKALKHTAQKFFTvDAGVRKGIPKVVVVFIDG---WPSD-DIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQD 314
Cdd:cd01473  82 GGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtSASKkELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4758022  315 vtfvdkavCR-NNGFFSYHMPNWFGTTKYV-KPLVQKLC 351
Cdd:cd01473 161 --------CDiNNDNCPNVIKTEWNNLNGIsKFLTDKIC 191
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 366-501 1.84e-03

VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 39.62  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022  366 VNIAFLIDGSSSVGDSNFRLM--LEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFT-DYstkENVLAVIRNIR-YMS 441
Cdd:cd01467   3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTlDR---ESLKELLEDIKiGLA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758022  442 G-GTATGDAISFTVrNVFGPirESPNKNFLVIVTDGQSYDDVQGPAAAAHDA---GITIFSVGV 501
Cdd:cd01467  80 GqGTAIGDAIGLAI-KRLKN--SEAKERVIVLLTDGENNAGEIDPATAAELAknkGVRIYTIGV 140
PRK09193 PRK09193
indolepyruvate ferredoxin oxidoreductase; Validated
 455-549 8.51e-03

indolepyruvate ferredoxin oxidoreductase; Validated


Pssm-ID: 236404 [Multi-domain]  Cd Length: 1165  Bit Score: 39.04  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758022    455 RNVFGpireSPNKNFLvIVTDGQSYDDVQGP-------AAAAHDAGITIFSVGVAWaPLDdlkdmaskPKEshaffTREF 527
Cdd:PRK09193  275 RVVID----SPNARLG-IVAAGKAYLDVRQAlrdlgldEETAARLGIRLYKVGMVW-PLE--------PQG-----VRAF 335

                          90       100
                  ....*....|....*....|....*
gi 4758022    528 -TGLEPIVsdVI--RgicRDFLESQ 549
Cdd:PRK09193  336 aEGLDEIL--VVeeK---RQIIEYQ 355
 
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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