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Conserved domains on  [gi|308081588|ref|NP_001183957|]
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vitrin isoform 2 [Mus musculus]

Protein Classification

VWA domain-containing protein( domain architecture ID 10510807)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 444-604 5.82e-55

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: 184.35  E-value: 5.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS 523
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 524 TGAAIQYALEQLFKK---SKPNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSFF 600
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 308081588 601 VDDF 604
Cdd:cd01472  161 VADF 164
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 243-406 9.56e-46

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


The actual alignment was detected with superfamily member cd01482:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 159.37  E-value: 9.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSNV 322
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 323 GRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVVEPGFASKaVCR 402
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 308081588 403 TNGF 406
Cdd:cd01482  161 VADF 164
LCCL pfam03815
LCCL domain;
22-111 3.26e-40

LCCL domain;


:

Pssm-ID: 427521  Cd Length: 96  Bit Score: 141.65  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   22 INCDVKAGKIIN------PEFMVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSY 95
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 308081588   96 SNGVQSLSLPRWRESF 111
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 444-604 5.82e-55

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: 184.35  E-value: 5.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS 523
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 524 TGAAIQYALEQLFKK---SKPNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSFF 600
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 308081588 601 VDDF 604
Cdd:cd01472  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
445-610 6.77e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 176.31  E-value: 6.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS- 523
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  524 TGAAIQYALEQLFKKS---KPNKRKVMIIITDGRSYD-DVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSF 599
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 308081588  600 FVDDFDNLYKI 610
Cdd:pfam00092 161 TVSDFEALEDL 171
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 243-406 9.56e-46

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: 159.37  E-value: 9.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSNV 322
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 323 GRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVVEPGFASKaVCR 402
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 308081588 403 TNGF 406
Cdd:cd01482  161 VADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 445-610 1.37e-41

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: 148.37  E-value: 1.37e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGY-WSGGTS 523
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   524 TGAAIQYALEQLFKKSK---PNKRKVMIIITDGRSYD---DVRIPAMAAYQKGVITYAIGIAWAA-QDELEVMATHPAKD 596
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 308081588   597 HSFFVDDFDNLYKI 610
Cdd:smart00327 161 YVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
243-422 7.07e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 146.65  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQR-GGLSN 321
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDK-VEEVSRVARESGINVFFITVEGAAERDIQhvvepGFASKAV 400
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELR-----KIASEPG 155

                         170       180
                  ....*....|....*....|..
gi 308081588  401 CRtngfYSFNVQSWLSLHKTVQ 422
Cdd:pfam00092 156 EG----HVFTVSDFEALEDLQD 173
LCCL pfam03815
LCCL domain;
22-111 3.26e-40

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 141.65  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   22 INCDVKAGKIIN------PEFMVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSY 95
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 308081588   96 SNGVQSLSLPRWRESF 111
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
LCCL smart00603
LCCL domain;
20-102 4.91e-37

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 132.51  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588    20 PQINCDVKAGKIINPEF--MVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSYSN 97
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTdnRVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 308081588    98 GVQSL 102
Cdd:smart00603  81 GIQSE 85
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 243-386 5.52e-36

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: 132.96  E-value: 5.52e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQR-GGLSN 321
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308081588   322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDK---VEEVSRVARESGINVFFITVEGAAERD 386
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 443-614 2.81e-17

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: 82.29  E-value: 2.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 443 SADIGFVIDGSSSMGTSN-----FRTVLQFVANLSKefeisdtDTRVGAVQY--TYEQRLEFGFDKynskADILSAIRRV 515
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 516 GyWSGGTSTGAAIQYALEQLfKKSKPNKRKVMIIITDGR---SYDDVRIPAMAAYQKGVITYAIGIAWAAQDE--LEVMA 590
Cdd:COG1240  161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIA 238

                        170       180
                 ....*....|....*....|....
gi 308081588 591 THpAKDHSFFVDDFDNLYKIAPRI 614
Cdd:COG1240  239 EA-TGGRYFRADDLSELAAIYREI 261
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 446-592 1.65e-07

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 53.47  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  446 IGFVIDGSSSMgtsnfRTVLQFVANLSKEF--EISDTDTRVGAVQYTYEQRLEFGFDkyNSKADILSAIRRVGYWS---- 519
Cdd:TIGR03436  56 VGLVIDTSGSM-----RNDLDRARAAAIRFlkTVLRPNDRVFVVTFNTRLRLLQDFT--SDPRLLEAALNRLKPPLrtdy 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  520 ----------GGTSTGAAIQYALEQLFKKSKPNK--RKVMIIITDG---RSYDDVRIPAMAAYQKGVITYAIGIAWAAQD 584
Cdd:TIGR03436 129 nssgafvrdgGGTALYDAITLAALEQLANALAGIpgRKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDARGLRAP 208


                  ....*...
gi 308081588  585 ELEVMATH 592
Cdd:TIGR03436 209 DLGAGAKA 216
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 444-604 5.82e-55

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: 184.35  E-value: 5.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS 523
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 524 TGAAIQYALEQLFKK---SKPNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSFF 600
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 308081588 601 VDDF 604
Cdd:cd01472  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
445-610 6.77e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 176.31  E-value: 6.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS- 523
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  524 TGAAIQYALEQLFKKS---KPNKRKVMIIITDGRSYD-DVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSF 599
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 308081588  600 FVDDFDNLYKI 610
Cdd:pfam00092 161 TVSDFEALEDL 171
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 444-604 8.46e-52

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: 175.55  E-value: 8.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS 523
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 524 TGAAIQYALEQLFKKSK---PNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSFF 600
Cdd:cd01482   81 TGKALTHVREKNFTPDAgarPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 308081588 601 VDDF 604
Cdd:cd01482  161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 243-406 9.56e-46

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: 159.37  E-value: 9.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSNV 322
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 323 GRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVVEPGFASKaVCR 402
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 308081588 403 TNGF 406
Cdd:cd01482  161 VADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 444-599 2.73e-45

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: 158.22  E-value: 2.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSG-GT 522
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 523 STGAAIQYALEQLFKKS--KPNKRKVMIIITDGRSYDDVRIPAMAAY--QKGVITYAIGIAWAAQDELEVMATHPAKDHS 598
Cdd:cd01450   81 NTGKALQYALEQLFSESnaRENVPKVIIVLTDGRSDDGGDPKEAAAKlkDEGIKVFVVGVGPADEEELREIASCPSERHV 160


                 .
gi 308081588 599 F 599
Cdd:cd01450  161 F 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 242-384 3.46e-45

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: 157.77  E-value: 3.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSN 321
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308081588 322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAE 384
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADE 143
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 444-621 1.63e-43

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: 155.62  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTS 523
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 524 TGAAIQYALEQLF------KKSKPNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDH 597
Cdd:cd01475   83 TGLAIQYAMNNAFseaegaRPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180
                 ....*....|....*....|....
gi 308081588 598 SFFVDDFDNLYKIAPRIIQNICTE 621
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKICVV 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 445-610 1.37e-41

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: 148.37  E-value: 1.37e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGY-WSGGTS 523
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   524 TGAAIQYALEQLFKKSK---PNKRKVMIIITDGRSYD---DVRIPAMAAYQKGVITYAIGIAWAA-QDELEVMATHPAKD 596
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 308081588   597 HSFFVDDFDNLYKI 610
Cdd:smart00327 161 YVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
243-422 7.07e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 146.65  E-value: 7.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQR-GGLSN 321
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDK-VEEVSRVARESGINVFFITVEGAAERDIQhvvepGFASKAV 400
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELR-----KIASEPG 155

                         170       180
                  ....*....|....*....|..
gi 308081588  401 CRtngfYSFNVQSWLSLHKTVQ 422
Cdd:pfam00092 156 EG----HVFTVSDFEALEDLQD 173
LCCL pfam03815
LCCL domain;
22-111 3.26e-40

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 141.65  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   22 INCDVKAGKIIN------PEFMVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSY 95
Cdd:pfam03815   1 LSCSTTLLDICNfcpftgTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 308081588   96 SNGVQSLSLPRWRESF 111
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 445-610 2.32e-37

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: 137.10  E-value: 2.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTST 524
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 525 GAAIQYALEQLFKKSK---PNKRKVMIIITDGRSYDDVRIPAM--AAYQKGVITYAIGIAWA-----AQDELEVMATHPA 594
Cdd:cd01469   82 ATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIASKPP 161

                        170
                 ....*....|....*.
gi 308081588 595 KDHSFFVDDFDNLYKI 610
Cdd:cd01469  162 EEHFFNVTDFAALKDI 177
LCCL smart00603
LCCL domain;
20-102 4.91e-37

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 132.51  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588    20 PQINCDVKAGKIINPEF--MVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSYSN 97
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTdnRVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 308081588    98 GVQSL 102
Cdd:smart00603  81 GIQSE 85
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 242-379 3.22e-36

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: 133.19  E-value: 3.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGL-S 320
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308081588 321 NVGRAISFVTKTFFSKANgNRGGAPNVAVVMVDGWPTD--KVEEVSRVARESGINVFFITV 379
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGV 140
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 243-386 5.52e-36

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: 132.96  E-value: 5.52e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588   243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQR-GGLSN 321
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308081588   322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDK---VEEVSRVARESGINVFFITVEGAAERD 386
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDVDEE 148
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 444-599 8.52e-34

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: 126.53  E-value: 8.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGY-WSGGT 522
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 523 STGAAIQYALEQLFKKSKPNKRKVMIIITDGRSYDDVRIPAMAAYQ---KGVITYAIGI-AWAAQDELEVMATHPAKDHS 598
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElrkLGITVYTIGIgDDANEDELKEIADKTTGGAV 160


                 .
gi 308081588 599 F 599
Cdd:cd00198  161 F 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 444-604 7.89e-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: 7.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSG-GT 522
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 523 STGAAIQYALEQLFKKSKPNK-----RKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPakDH 597
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRieegvPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                 ....*..
gi 308081588 598 SFFVDDF 604
Cdd:cd01481  159 VFQVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 243-396 2.74e-29

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: 113.96  E-value: 2.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 243 DLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLS-N 321
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308081588 322 VGRAISFVTKTFFSKANGNR--GGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVV-EPGFA 396
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAfDPSFV 159
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 242-444 1.90e-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: 113.63  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSN 321
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 322 VGRAISFVTKTFFSKANGNRGGAPN---VAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVV-EPgfAS 397
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSERvprVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIAsEP--LA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308081588 398 KAVcrtngFYSFNVQSWLSLHKTVQplvKRVCDTDRLA------CSKTCLNSA 444
Cdd:cd01475  161 DHV-----FYVEDFSTIEELTKKFQ---GKICVVPDLCatlshvCQQVCISTP 205
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 242-385 4.55e-26

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: 105.13  E-value: 4.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSN 321
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308081588 322 VGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTD--KVEEVSRVARESGINVFFITVEGAAER 385
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQR 146
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 242-400 5.03e-25

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: 101.49  E-value: 5.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKIT-QRGGLS 320
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 321 NVGRAISFVTKTFFSKANGNRggaPNVAVVMVDGWPTD---KVEEVSRVARESGINVFFITV-EGAAERDIQHVVEPGFA 396
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNA---RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTTG 157


                 ....
gi 308081588 397 SKAV 400
Cdd:cd00198  158 GAVF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 444-556 4.25e-24

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: 99.77  E-value: 4.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTVLQFVANLSKEF------EISDTDTRVGAVQYTYEQRLEFGFDK-YNSKADILSAIRRVG 516
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 308081588 517 YWSGGTSTGAAIQYALEQLFKKSKPNKRKVMIIITDGRSY 556
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSD 122
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 444-578 2.22e-22

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: 94.00  E-value: 2.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGtSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYE--QRLEFGFDKYNSKADILSAIRRVGYWSGG 521
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 522 TSTGAAIQYALEQLFKKS--KPNKRKVMIIITDGRSYDDVRIPA-MAAYQKGVITYAIGI 578
Cdd:cd01476   80 TATGAAIEVALQQLDPSEgrREGIPKVVVVLTDGRSHDDPEKQArILRAVPNIETFAVGT 139
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 443-614 2.81e-17

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: 82.29  E-value: 2.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 443 SADIGFVIDGSSSMGTSN-----FRTVLQFVANLSKefeisdtDTRVGAVQY--TYEQRLEFGFDKynskADILSAIRRV 515
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 516 GyWSGGTSTGAAIQYALEQLfKKSKPNKRKVMIIITDGR---SYDDVRIPAMAAYQKGVITYAIGIAWAAQDE--LEVMA 590
Cdd:COG1240  161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIA 238

                        170       180
                 ....*....|....*....|....
gi 308081588 591 THpAKDHSFFVDDFDNLYKIAPRI 614
Cdd:COG1240  239 EA-TGGRYFRADDLSELAAIYREI 261
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 243-379 7.84e-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: 78.21  E-value: 7.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 243 DLSFLIDGSTSIgKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGdNPATQ---FNLKTHMNSQDLKTAIEKITQRGGL 319
Cdd:cd01476    2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYS-GRGRQrvrFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308081588 320 SNVGRAISFVTKtFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARES-GINVFFITV 379
Cdd:cd01476   80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGT 139
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 240-379 4.95e-14

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: 70.88  E-value: 4.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 240 CKIDLSFLIDGSTSIGKRRFRIQKQFLADVVQ------ALDIGPAGPLVGVVQYGDNPaTQFNLKTHM--NSQDLKTAIE 311
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQ-EVEAGFLRDirNYTSLKEAVD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308081588 312 KITQRGGLSNVGRAISFVTKTFFskaNGNRGGAPNVAVVMVDGWPT----DKVEEVSRVARESGINVFFITV 379
Cdd:cd01480   80 NLEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAV 148
VWA_2 pfam13519
von Willebrand factor type A domain;
448-549 1.14e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 67.32  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  448 FVIDGSSSM-----GTSNFRTVLQFVANLSKEFEISdtdtRVGAVQYTYEQRLEFGFDKynSKADILSAIRRVGYWSGGT 522
Cdd:pfam13519   3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                          90       100
                  ....*....|....*....|....*..
gi 308081588  523 STGAAIQYALEQLFKKSKPNKRKVMII 549
Cdd:pfam13519  77 NLAAALQLARAALKHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 445-578 4.14e-13

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: 68.18  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 445 DIGFVIDGSSSMGTSN-FRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSK-----ADILSAIRRVGYW 518
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308081588 519 SGGTSTGAAIQYALEQLF--KKSKPNKRKVMIIITDGRSYDDVRIPAMAAY--QKGVITYAIGI 578
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGIPDSKFRTLKEARKlrERGVIIAVLGV 145
VWA_2 pfam13519
von Willebrand factor type A domain;
246-350 6.85e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 65.01  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  246 FLIDGSTSI-----GKRRFRIQKQFLADVVQALdigpAGPLVGVVQYGDNPATQFNLKThmNSQDLKTAIEKITQRGGLS 320
Cdd:pfam13519   3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 308081588  321 NVGRAISFVTKTFFskanGNRGGAPNVAVV 350
Cdd:pfam13519  77 NLAAALQLARAALK----HRRKNQPRRIVL 102
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 242-379 1.17e-12

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: 66.64  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 242 IDLSFLIDGSTSIG-KRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHmNSQDLKTA------IEKIT 314
Cdd:cd01471    1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSP-NSTNKDLAlnairaLLSLY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308081588 315 QRGGLSNVGRAISFVTKTFFSKAnGNRGGAPNVAVVMVDGWPTDKVE--EVSRVARESGINVFFITV 379
Cdd:cd01471   80 YPNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 440-621 7.48e-11

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: 61.37  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 440 CLNSADIGFVIDGSSSMgTSNFRTVLQFVANLSKEFeiSDTDTRVGAVQYTYEQRLEFGFDKYNSKADI-LSAIRRVGYw 518
Cdd:cd01474    1 CAGHFDLYFVLDKSGSV-AANWIEIYDFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 519 SGGTSTGAAIQYALEQLFKKSKPNKR--KVMIIITDGRSYDDVRIPAMAAYQK----GVITYAIGIAWAAQDELEVMATh 592
Cdd:cd01474   77 SGQTYIHEGLENANEQIFNRNGGGREtvSVIIALTDGQLLLNGHKYPEHEAKLsrklGAIVYCVGVTDFLKSQLINIAD- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 308081588 593 pAKDHSFFVDD-FDNLYKIAPRIIQNICTE 621
Cdd:cd01474  156 -SKEYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 445-619 3.78e-10

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: 59.64  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 445 DIGFVIDGSSSMGTSNFRT-VLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNS--KADILSAIRRV--GYWS 519
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERydKNELLKKINDLknSYRS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 520 GG-TSTGAAIQYALEQLFKksKPNKR----KVMIIITDGR--SYDDVRIPAMAA-YQ-KGVITYAIGIAWAAQDELEVMA 590
Cdd:cd01473   82 GGeTYIVEALKYGLKNYTK--HGNRRkdapKVTMLFTDGNdtSASKKELQDISLlYKeENVKLLVVGVGAASENKLKLLA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 308081588 591 THPAKD----HSFFVdDFDNLYKIAPRIIQNIC 619
Cdd:cd01473  160 GCDINNdncpNVIKT-EWNNLNGISKFLTDKIC 191
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 444-621 8.38e-09

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 57.03  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTV----LQFVANLSKE--FEISDTDTRVGAVqytyeqrLEFGfdKYNSKADILSAIRRVgY 517
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAkeaaKLLVDQLRPGdrVSIVTFAGDARVL-------LPPT--PATDRAKILAAIDRL-Q 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 518 WSGGTSTGAAIQYALEQLFKKSKPNKRKVMIIITDGR----SYDDVRIPAMA--AYQKGVITYAIGIAWAAQDE-LEVMA 590
Cdd:COG2304  162 AGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDanvgITDPEELLKLAeeAREEGITLTTLGVGSDYNEDlLERLA 241

                        170       180       190
                 ....*....|....*....|....*....|.
gi 308081588 591 THpAKDHSFFVDDFDNLYKIAPRIIQNICTE 621
Cdd:COG2304  242 DA-GGGNYYYIDDPEEAEKVFVREFSRIGYE 271
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 445-578 1.15e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 56.61  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 445 DIGFVIDGSSSMGTSNFRT----VLQFVANLSK--EFEISDTDTRVgavqytyEQRLEFGFDKYNSKA-DILSAIRRvgy 517
Cdd:COG2425  120 PVVLCVDTSGSMAGSKEAAakaaALALLRALRPnrRFGVILFDTEV-------VEDLPLTADDGLEDAiEFLSGLFA--- 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308081588 518 wSGGTSTGAAIQYALEQLfkKSKPNKRKVMIIITDGRSYDDVR--IPAMAAYQKGVITYAIGI 578
Cdd:COG2425  190 -GGGTDIAPALRAALELL--EEPDYRNADIVLITDGEAGVSPEelLREVRAKESGVRLFTVAI 249
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 446-592 1.65e-07

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 53.47  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  446 IGFVIDGSSSMgtsnfRTVLQFVANLSKEF--EISDTDTRVGAVQYTYEQRLEFGFDkyNSKADILSAIRRVGYWS---- 519
Cdd:TIGR03436  56 VGLVIDTSGSM-----RNDLDRARAAAIRFlkTVLRPNDRVFVVTFNTRLRLLQDFT--SDPRLLEAALNRLKPPLrtdy 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588  520 ----------GGTSTGAAIQYALEQLFKKSKPNK--RKVMIIITDG---RSYDDVRIPAMAAYQKGVITYAIGIAWAAQD 584
Cdd:TIGR03436 129 nssgafvrdgGGTALYDAITLAALEQLANALAGIpgRKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDARGLRAP 208


                  ....*...
gi 308081588  585 ELEVMATH 592
Cdd:TIGR03436 209 DLGAGAKA 216
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 444-603 6.12e-07

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: 50.02  E-value: 6.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 444 ADIGFVIDGSSSMGTSNFRTV--LQFVANLSKEFEISDTDTRVGAV---QYTYEQrLEFGFDkYNSKADILSAIRrVGYW 518
Cdd:cd01467    3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVvfaGAAFTQ-APLTLD-RESLKELLEDIK-IGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 519 SGGTSTGAAIQYALEQlFKKSKPnKRKVMIIITDGRSYDDVRIPAMA---AYQKGVITYAIGIAWAAQDELEVMATHPAK 595
Cdd:cd01467   80 GQGTAIGDAIGLAIKR-LKNSEA-KERVIVLLTDGENNAGEIDPATAaelAKNKGVRIYTIGVGKSGSGPKPDGSTILDE 157


                 ....*...
gi 308081588 596 DHSFFVDD 603
Cdd:cd01467  158 DSLVEIAD 165
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 445-551 6.60e-06

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: 47.03  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 445 DIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTD------TRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYW 518
Cdd:cd01477   21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 308081588 519 SGGTS-----TG--AAIQyALEQLFKKSKPNKRKVMIIIT 551
Cdd:cd01477  101 VSSTNasyldTGlqAAEQ-MLAAGKRTSRENYKKVVIVFA 139
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 448-602 8.96e-06

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: 46.50  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 448 FVIDGSSSMGTSNFRTVLQFVANLSKEFEISDtdtRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYwSGGTSTGAA 527
Cdd:cd01465    5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 528 IQYALEQLFKKSKPNKRKVMIIITDGRSY----DDVRIPAMAAYQ--KGVITYAIGIAWAAQDELEVMATHPAKDHSFFV 601
Cdd:cd01465   81 IQLGYQEAQKHFVPGGVNRILLATDGDFNvgetDPDELARLVAQKreSGITLSTLGFGDNYNEDLMEAIADAGNGNTAYI 160


                 .
gi 308081588 602 D 602
Cdd:cd01465  161 D 161
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
448-585 9.35e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.84  E-value: 9.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 448 FVIDGSSSMGTSNFRTV---LQ-FVANLSKEFEISDTDtRVGAVqytyeqrlefGFDkynSKADILSAIRRVG--YW--- 518
Cdd:COG4245   10 LLLDTSGSMSGEPIEALnegLQaLIDELRQDPYALETV-EVSVI----------TFD---GEAKVLLPLTDLEdfQPpdl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 519 --SGGTSTGAAIQYALEQL---FKKSKPNK----RKVMIIITDGRSYDDV------RIPAMAAYQKGVItYAIGIAWAAQ 583
Cdd:COG4245   76 saSGGTPLGAALELLLDLIerrVQKYTAEGkgdwRPVVFLITDGEPTDSDweaalqRLKDGEAAKKANI-FAIGVGPDAD 154


                 ..
gi 308081588 584 DE 585
Cdd:COG4245  155 TE 156
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 448-604 2.92e-04

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.94  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 448 FVIDGSSSMGTSNFRTV----LQFVANLSKEfEISDTDTRVGAVQYTYEQRLEFGF-DKYNSKADILSAirrvgywSGGT 522
Cdd:cd01464    8 LLLDTSGSMAGEPIEALnqglQMLQSELRQD-PYALESVEISVITFDSAARVIVPLtPLESFQPPRLTA-------SGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 523 STGAAIQYALEQLFK---KSKPNK----RKVMIIITDGRSYDDV-----RIPAMAAYQKGVITYAIGIAwAAQDELEVMA 590
Cdd:cd01464   80 SMGAALELALDCIDRrvqRYRADQkgdwRPWVFLLTDGEPTDDLtaaieRIKEARDSKGRIVACAVGPK-ADLDTLKQIT 158

                        170
                 ....*....|....*
gi 308081588 591 TH-PAKDHSFFVDDF 604
Cdd:cd01464  159 EGvPLLDDALSGLNF 173
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 509-578 2.04e-03

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


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 39.62  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308081588 509 LSAIRRVGYwsggTSTGAAIQYALEQLFKKskPNKRKVMIIITDGR----SYDDVRIPAMA--------AYQKGVITYAI 576
Cdd:cd01454   75 LAALSPGGN----TRDGAAIRHAAERLLAR--PEKRKILLVISDGEpndlDYYEGNVFATEdalravieARKLGIEVFGI 148


                 ..
gi 308081588 577 GI 578
Cdd:cd01454  149 TI 150
 
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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