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Conserved domains on  [gi|1962009176|ref|NP_001378896|]
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vitrin isoform 8 precursor [Homo sapiens]

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 ...
 445-604 6.55e-53

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: 178.58  E-value: 6.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 524
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAH-LKVITYAIGVAWAAQEELEVIATHPARDHSFF 600
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKqAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962009176 601 VDEF 604
Cdd:cd01472   161 VADF 164
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 244-407 1.50e-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.


The actual alignment was detected with superfamily member cd01482:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 158.99  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 323
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 324 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 403
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962009176 404 TNGF 407
Cdd:cd01482   161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 9.02e-41

LCCL domain;


:

Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.19  E-value: 9.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962009176 118 SNGVQSLSLPRWRESF 133
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 ...
 445-604 6.55e-53

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: 178.58  E-value: 6.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 524
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAH-LKVITYAIGVAWAAQEELEVIATHPARDHSFF 600
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKqAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962009176 601 VDEF 604
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
446-609 1.62e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 164.76  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 524
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAA-HLKVITYAIGVAWAAQEELEVIATHPARDHSF 599
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELkSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|
gi 1962009176 600 FVDEFDNLHQ 609
Cdd:pfam00092 161 TVSDFEALED 170
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 244-407 1.50e-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: 158.99  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 323
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 324 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 403
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962009176 404 TNGF 407
Cdd:cd01482   161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 9.02e-41

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.19  E-value: 9.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962009176 118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
LCCL smart00603
LCCL domain;
42-124 9.50e-39

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.52  E-value: 9.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176   42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 1962009176  120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
244-387 2.74e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 139.33  E-value: 2.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 322
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1962009176 323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 387
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 446-609 6.27e-38

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: 138.36  E-value: 6.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 524
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  525 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAMAA----HLKVITYAIGVAWAA-QEELEVIATHPARD 596
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDGPKDLLKAAkelkRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 1962009176  597 HSFFVDEFDNLHQ 609
Cdd:smart00327 161 YVFLPELLDLLID 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 244-389 1.06e-35

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 132.19  E-value: 1.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 322
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 389
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 444-607 5.30e-12

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: 66.50  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 444 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 516
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 517 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGR----SYDDVRIPAMAAHLKVITYAIGVAWAA--QEELEVIA 590
Cdd:COG1240   161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRdnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREIA 238

                         170       180
                  ....*....|....*....|...
gi 1962009176 591 T------HPARDHSFFVDEFDNL 607
Cdd:COG1240   239 EatggryFRADDLSELAAIYREI 261
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 445-604 6.55e-53

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: 178.58  E-value: 6.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 524
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAH-LKVITYAIGVAWAAQEELEVIATHPARDHSFF 600
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKqAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962009176 601 VDEF 604
Cdd:cd01472   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 445-604 5.03e-48

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: 165.54  E-value: 5.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 524
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAM-AAHLKVITYAIGVAWAAQEELEVIATHPARDHSFF 600
Cdd:cd01482    81 TGKALTHVREKNFTPDAgarPGVPKVVILITDGKSQDDVELPARvLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 1962009176 601 VDEF 604
Cdd:cd01482   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
446-609 1.62e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 164.76  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 524
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAA-HLKVITYAIGVAWAAQEELEVIATHPARDHSF 599
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELkSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|
gi 1962009176 600 FVDEFDNLHQ 609
Cdd:pfam00092 161 TVSDFEALED 170
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 244-407 1.50e-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: 158.99  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 323
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 324 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 403
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962009176 404 TNGF 407
Cdd:cd01482   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 243-387 1.08e-44

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: 156.62  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 322
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1962009176 323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE 387
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEE 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 445-599 2.39e-43

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: 2.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 523
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 524 STGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPAMAAHLK---VITYAIGVAWAAQEELEVIATHPARDHS 598
Cdd:cd01450    81 NTGKALQYALEQLFSESnaRENVPKVIIVLTDGRSDDGGDPKEAAAKLKdegIKVFVVGVGPADEEELREIASCPSERHV 160


                  .
gi 1962009176 599 F 599
Cdd:cd01450   161 F 161
LCCL pfam03815
LCCL domain;
44-133 9.02e-41

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.19  E-value: 9.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962009176 118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
LCCL smart00603
LCCL domain;
42-124 9.50e-39

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.52  E-value: 9.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176   42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 1962009176  120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
244-387 2.74e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 139.33  E-value: 2.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 322
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1962009176 323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 387
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 446-609 6.27e-38

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: 138.36  E-value: 6.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 524
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  525 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAMAA----HLKVITYAIGVAWAA-QEELEVIATHPARD 596
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDGPKDLLKAAkelkRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 1962009176  597 HSFFVDEFDNLHQ 609
Cdd:smart00327 161 YVFLPELLDLLID 173
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 445-621 2.34e-37

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: 138.67  E-value: 2.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 524
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 525 TGAAINFALEQLF------KKSKPNKRKLMILITDGRSYDDVR-IPAMAAHLKVITYAIGVAWAAQEELEVIATHPARDH 597
Cdd:cd01475    83 TGLAIQYAMNNAFseaegaRPGSERVPRVGIVVTDGRPQDDVSeVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|....
gi 1962009176 598 SFFVDEFDNLHQYVPRIIQNICTE 621
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVV 186
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 446-607 4.10e-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: 136.33  E-value: 4.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTST 525
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 526 GAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPA---MAAHLKVITYAIGVAWA-----AQEELEVIATHPA 594
Cdd:cd01469    82 ATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDPLLKDvipQAEREGIIRYAIGVGGHfqrenSREELKTIASKPP 161

                         170
                  ....*....|...
gi 1962009176 595 RDHSFFVDEFDNL 607
Cdd:cd01469   162 EEHFFNVTDFAAL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 243-387 4.34e-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: 132.80  E-value: 4.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGL-S 321
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1962009176 322 NVGRAISFVTKNFFSKANgNRSGAPNVVVVMVDGWPTD--KVEEASRLARESGINIFFITIEGAAENE 387
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEE 147
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 244-389 1.06e-35

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 132.19  E-value: 1.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 322
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176  323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 389
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 445-599 9.13e-31

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: 118.05  E-value: 9.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGT 523
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 524 STGAAINFALEQLFKKSKPNKRKLMILITDGRSYDDVRIPAMAAH----LKVITYAIGV-AWAAQEELEVIATHPARDHS 598
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARelrkLGITVYTIGIgDDANEDELKEIADKTTGGAV 160


                  .
gi 1962009176 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 ...
 445-604 1.31e-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: 114.73  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 523
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 524 STGAAINFALEQLFKKSKPNK-----RKLMILITDGRSYDDVRIPAMAahLK---VITYAIGVAWAAQEELEVIATHPar 595
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRieegvPQFLVLITGGKSQDDVERPAVA--LKragIVPFAIGARNADLAELQQIAFDP-- 156


                  ....*....
gi 1962009176 596 DHSFFVDEF 604
Cdd:cd01481   157 SFVFQVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 244-397 6.05e-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: 112.80  E-value: 6.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLS-N 322
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1962009176 323 VGRAISFVTKNFFSKANGNR--SGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVV-EPNFA 397
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAfDPSFV 159
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 243-445 6.04e-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: 112.09  E-value: 6.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 322
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 323 VGRAISFVTKNFFSKANGNRSGAPN---VVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE-KQYVVEPnfAN 398
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGSERvprVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEElREIASEP--LA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1962009176 399 KAVcrtngFYslhVQSWFGLHKTLQPLVKRVCDTDRLA------CSKTCLNSA 445
Cdd:cd01475   161 DHV-----FY---VEDFSTIEELTKKFQGKICVVPDLCatlshvCQQVCISTP 205
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 243-390 1.95e-25

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: 103.20  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 322
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 323 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRL--ARESGINIFFITIEGAAENEKQY 390
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHFQRENSR 150
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 243-390 6.54e-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: 6.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKIT-QRGGLS 321
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1962009176 322 NVGRAISFVTKNFFSKAngnRSGAPNVVVVMVDGWPTD---KVEEASRLARESGINIFFITIeGAAENEKQY 390
Cdd:cd00198    81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGI-GDDANEDEL 148
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 445-602 1.78e-23

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: 97.84  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEF------EISDTDTRIGAVQYTYEQRLEFGFDK-YSSKPDILNAIKRVG 517
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 518 YWSGGTSTGAAINFALEQLFKKSKPNKRKLMILITDGRSY-DDVRIPAMAA----HLKVITYAIGVAWAAQEELEVIAT- 591
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDgSPDGGIEKAVneadHLGIKIFFVAVGSQNEEPLSRIACd 162

                         170       180
                  ....*....|....*....|
gi 1962009176 592 ---------HPARDHSFFVD 602
Cdd:cd01480   163 gksalyrenFAELLWSFFID 182
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 445-600 3.21e-21

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: 90.92  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGtGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYE--QRLEFGFDKYSSKPDILNAIKRVGYWSGG 522
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 523 TSTGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPA--MAAHLKVITYAIGV---AWAAQEELEVIATHPar 595
Cdd:cd01476    80 TATGAAIEVALQQLDPSEgrREGIPKVVVVLTDGRSHDDPEKQAriLRAVPNIETFAVGTgdpGTVDTEELHSITGNE-- 157


                  ....*
gi 1962009176 596 DHSFF 600
Cdd:cd01476   158 DHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 244-380 8.06e-18

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: 80.91  E-value: 8.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 244 DLSFLIDGSTSIgKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATH--FNLKTHTNSRDLKTAIEKITQRGGLS 321
Cdd:cd01476     2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 322 NVGRAISFVTkNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARES-GINIFFITI 380
Cdd:cd01476    81 ATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGT 139
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 241-392 1.67e-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: 69.34  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 241 CKIDLSFLIDGSTSIGKRRFRIQKQLLADVAQ------ALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRD-LKTAIEK 313
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTsLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 314 ITQRGGLSNVGRAISFVTKNFFskaNGNRSGAPNVVVVMVDGWPT----DKVEEASRLARESGINIFFITIeGAAENEKQ 389
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAV-GSQNEEPL 156


                  ...
gi 1962009176 390 YVV 392
Cdd:cd01480   157 SRI 159
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 243-403 3.83e-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: 65.48  E-value: 3.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 243 IDLSFLIDGSTSIG-KRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKThTNSRDLKTAIE------KIT 315
Cdd:cd01471     1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSS-PNSTNKDLALNairallSLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 316 QRGGLSNVGRAISFVTKNFFSKAnGNRSGAPNVVVVMVDGWPTDK---VEEASRLaRESGINIFFITIegaaeneKQYVv 392
Cdd:cd01471    80 YPNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKfrtLKEARKL-RERGVIIAVLGV-------GQGV- 149

                         170
                  ....*....|.
gi 1962009176 393 epnfaNKAVCR 403
Cdd:cd01471   150 -----NHEENR 155
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 444-607 5.30e-12

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: 66.50  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 444 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 516
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 517 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGR----SYDDVRIPAMAAHLKVITYAIGVAWAA--QEELEVIA 590
Cdd:COG1240   161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRdnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREIA 238

                         170       180
                  ....*....|....*....|...
gi 1962009176 591 T------HPARDHSFFVDEFDNL 607
Cdd:COG1240   239 EatggryFRADDLSELAAIYREI 261
VWA_2 pfam13519
von Willebrand factor type A domain;
247-351 5.39e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 5.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 247 FLIDGSTSI-----GKRRFRIQKQLLADVAQALdigpAGPLMGVVQYGDNPATHFNLKThtNSRDLKTAIEKITQRGGLS 321
Cdd:pfam13519   3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1962009176 322 NVGRAISFVTKNFFskanGNRSGAPNVVVV 351
Cdd:pfam13519  77 NLAAALQLARAALK----HRRKNQPRRIVL 102
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 441-621 6.91e-12

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: 64.45  E-value: 6.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 441 CLNSADIGFVIDGSSSVgTGNFRTVLQFVTNLTKEFeiSDTDTRIGAVQYTYEQRLEFGFDKYSSKPDI-LNAIKRVGYw 519
Cdd:cd01474     1 CAGHFDLYFVLDKSGSV-AANWIEIYDFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 520 SGGTSTGAAINFALEQLFKKSKPNKR--KLMILITDGRSYDDVRIPAM-----AAHLKVITYAIGVAWAAQEELEVIATH 592
Cdd:cd01474    77 SGQTYIHEGLENANEQIFNRNGGGREtvSVIIALTDGQLLLNGHKYPEheaklSRKLGAIVYCVGVTDFLKSQLINIADS 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1962009176 593 ParDHSFFVDE-FDNLHQYVPRIIQNICTE 621
Cdd:cd01474   157 K--EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 446-578 6.98e-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: 64.71  E-value: 6.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 446 DIGFVIDGSSSVGTGN-FRTVLQFVTNLTKEFEISDTDTRIGAVQYTY--EQRLEFGFDKYSSKPDILNAIK--RVGYWS 520
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTnaKELIRLSSPNSTNKDLALNAIRalLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1962009176 521 GG-TSTGAAINFALEQLF--KKSKPNKRKLMILITDGRSYDDVRIPAMAAHLK---VITYAIGV 578
Cdd:cd01471    82 NGsTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRergVIIAVLGV 145
VWA_2 pfam13519
von Willebrand factor type A domain;
449-551 5.07e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 449 FVIDGSSSVGTGNFR-TVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKysSKPDILNAIKRVGYWSGGTSTGA 527
Cdd:pfam13519   3 FVLDTSGSMRNGDYGpTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGTNLAA 80

                          90       100
                  ....*....|....*....|....
gi 1962009176 528 AINFAlEQLFKKSKPNKRKLMILI 551
Cdd:pfam13519  81 ALQLA-RAALKHRRKNQPRRIVLI 103
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 445-603 1.62e-06

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: 48.86  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTV--LQFVTNLTKEFEISDTDTRIGAVQytyeqrleFGFDKYSSKP---------DILNAI 513
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVV--------FAGAAFTQAPltldreslkELLEDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 514 KrVGYWSGGTSTGAAINFALEQlFKKSKPnKRKLMILITDGRSYDDVRIPAMAAHL----KVITYAIGVAWAAQEELEVI 589
Cdd:cd01467    75 K-IGLAGQGTAIGDAIGLAIKR-LKNSEA-KERVIVLLTDGENNAGEIDPATAAELaknkGVRIYTIGVGKSGSGPKPDG 151

                         170
                  ....*....|....
gi 1962009176 590 ATHPARDHSFFVDE 603
Cdd:cd01467   152 STILDEDSLVEIAD 165
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 520-604 1.68e-05

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: 45.79  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 520 SGGTSTGAAINFALEQLFK---KSKPNK----RKLMILITDGRSYDDVRI------PAMAAHLKVITYAIGVAwAAQEEL 586
Cdd:cd01464    76 SGGTSMGAALELALDCIDRrvqRYRADQkgdwRPWVFLLTDGEPTDDLTAaierikEARDSKGRIVACAVGPK-ADLDTL 154

                          90
                  ....*....|....*....
gi 1962009176 587 EVIATH-PARDHSFFVDEF 604
Cdd:cd01464   155 KQITEGvPLLDDALSGLNF 173
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 446-591 3.97e-05

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: 44.72  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 446 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTD------TRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYW 519
Cdd:cd01477    21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 520 SGGTS-----TG--AAINfALEQLFKKSKPNKRKLMILITDGRSYDDVRIP-AMAAHLK-----VITYAIG--VAWAAQE 584
Cdd:cd01477   101 VSSTNasyldTGlqAAEQ-MLAAGKRTSRENYKKVVIVFASDYNDEGSNDPrPIAARLKstgiaIITVAFTqdESSNLLD 179


                  ....*..
gi 1962009176 585 ELEVIAT 591
Cdd:cd01477   180 KLGKIAS 186
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 523-614 8.57e-05

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: 43.47  E-value: 8.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 523 TSTGAAINFALEQLFKKskPNKRKLMILITDGR----SYDDVRIPAMAAHLKVITYAIGVAwaaqeeLEVIATHpaRDHs 598
Cdd:cd01454    84 TRDGAAIRHAAERLLAR--PEKRKILLVISDGEpndlDYYEGNVFATEDALRAVIEARKLG------IEVFGIT--IDR- 152

                          90
                  ....*....|....*.
gi 1962009176 599 ffvDEFDNLHQYVPRI 614
Cdd:cd01454   153 ---DATTVDKEYLKNI 165
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
520-585 2.04e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.60  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1962009176 520 SGGTSTGAAINFALEQL---FKKSKPNK----RKLMILITDGRSYDDV------RIPAMAAHLKVITYAIGVAWAAQEE 585
Cdd:COG4245    78 SGGTPLGAALELLLDLIerrVQKYTAEGkgdwRPVVFLITDGEPTDSDweaalqRLKDGEAAKKANIFAIGVGPDADTE 156
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 445-621 7.64e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 42.01  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 445 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEfeISDTDtRIGAVQY--TYEQRLEFGfdKYSSKPDILNAIKRVgYWSGG 522
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQ--LRPGD-RVSIVTFagDARVLLPPT--PATDRAKILAAIDRL-QAGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 523 TSTGAAINFALEQLFKKSKPNKRKLMILITDGR------SYDDV-RIPAMAAHLKVITYAIGVAWAAQEE-LEVIATHpA 594
Cdd:COG2304   166 TALGAGLELAYELARKHFIPGRVNRVILLTDGDanvgitDPEELlKLAEEAREEGITLTTLGVGSDYNEDlLERLADA-G 244

                         170       180
                  ....*....|....*....|....*..
gi 1962009176 595 RDHSFFVDEFDNLHQYVPRIIQNICTE 621
Cdd:COG2304   245 GGNYYYIDDPEEAEKVFVREFSRIGYE 271
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 493-590 2.87e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 40.05  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962009176 493 EQRLEFGFDKysSKPDILNAIKRVGYwSGGTSTGAAINFALEQLfkKSKPNKRKLMILITDGRSYDDV-----RIPAMAA 567
Cdd:COG2425   166 VEDLPLTADD--GLEDAIEFLSGLFA-GGGTDIAPALRAALELL--EEPDYRNADIVLITDGEAGVSPeellrEVRAKES 240

                          90       100
                  ....*....|....*....|...
gi 1962009176 568 HLKVITYAIGVAwAAQEELEVIA 590
Cdd:COG2425   241 GVRLFTVAIGDA-GNPGLLEALA 262
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
520-561 6.53e-03

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 39.32  E-value: 6.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1962009176 520 SGGTST--GAAINFALEQLfkKSKPNKRKLMILITDGRSYD-DVR 561
Cdd:COG4548   330 EPGYYTrmGAAIRHATALL--AAQPARRRLLLVLTDGKPNDiDVY 372
 
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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