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Conserved domains on  [gi|295789104|ref|NP_001171440|]
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vitrin isoform 2 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 ...
 494-654 5.57e-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: 185.12  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 573
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 574 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 650
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 295789104 651 VDEF 654
Cdd:cd01472  161 VADF 164
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 293-456 1.09e-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: 159.76  E-value: 1.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 372
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 373 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 452
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 295789104 453 TNGF 456
Cdd:cd01482  161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 9.73e-41

LCCL domain;


:

Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.58  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 295789104  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 ...
 494-654 5.57e-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: 185.12  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 573
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 574 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 650
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 295789104 651 VDEF 654
Cdd:cd01472  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
495-663 1.36e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 170.92  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 573
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  574 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSF 649
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 295789104  650 FVDEFDNLHQYVPR 663
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 293-456 1.09e-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: 159.76  E-value: 1.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 372
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 373 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 452
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 295789104 453 TNGF 456
Cdd:cd01482  161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 9.73e-41

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.58  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 295789104  118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 495-659 4.86e-39

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: 141.82  E-value: 4.86e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 573
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   574 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYD---DVRIPAMAAHLKGVITYAIGVAWAA-QEELEVIATHPARD 646
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 295789104   647 HSFFVDEFDNLHQ 659
Cdd:smart00327 161 YVFLPELLDLLID 173
LCCL smart00603
LCCL domain;
42-124 1.18e-38

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.52  E-value: 1.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104    42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 295789104   120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
VWA pfam00092
von Willebrand factor type A domain;
293-436 1.97e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 140.10  E-value: 1.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 371
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789104  372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 436
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 293-438 5.01e-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: 133.35  E-value: 5.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 438
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 493-657 2.00e-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: 68.04  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 493 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 565
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 566 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAA--QEELEVIA 640
Cdd:COG1240  161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRDNAGRIDPLEAAELaaaAGIRIYTIGVGTEAvdEGLLREIA 238

                        170       180
                 ....*....|....*....|...
gi 295789104 641 T------HPARDHSFFVDEFDNL 657
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 ...
 494-654 5.57e-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: 185.12  E-value: 5.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 573
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 574 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 650
Cdd:cd01472   81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 295789104 651 VDEF 654
Cdd:cd01472  161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 494-654 2.92e-50

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: 172.47  E-value: 2.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 573
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 574 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 650
Cdd:cd01482   81 TGKALTHVREKNFTPDAgarPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 295789104 651 VDEF 654
Cdd:cd01482  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
495-663 1.36e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 170.92  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 573
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  574 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSF 649
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 295789104  650 FVDEFDNLHQYVPR 663
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 293-456 1.09e-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: 159.76  E-value: 1.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 372
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 373 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 452
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                 ....
gi 295789104 453 TNGF 456
Cdd:cd01482  161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 292-436 9.43e-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: 157.39  E-value: 9.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 371
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789104 372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE 436
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEE 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 494-649 1.20e-44

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 157.07  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 572
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 573 STGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPAMAAHLK--GVITYAIGVAWAAQEELEVIATHPARDHS 648
Cdd:cd01450   81 NTGKALQYALEQLFSESnaRENVPKVIIVLTDGRSDDGGDPKEAAAKLKdeGIKVFVVGVGPADEEELREIASCPSERHV 160


                 .
gi 295789104 649 F 649
Cdd:cd01450  161 F 161
LCCL pfam03815
LCCL domain;
44-133 9.73e-41

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 143.58  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 295789104  118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 495-659 4.86e-39

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: 141.82  E-value: 4.86e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 573
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   574 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYD---DVRIPAMAAHLKGVITYAIGVAWAA-QEELEVIATHPARD 646
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 295789104   647 HSFFVDEFDNLHQ 659
Cdd:smart00327 161 YVFLPELLDLLID 173
LCCL smart00603
LCCL domain;
42-124 1.18e-38

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.52  E-value: 1.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104    42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 295789104   120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 494-671 1.67e-38

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: 142.14  E-value: 1.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 573
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 574 TGAAINFALEQLF------KKSKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDH 647
Cdd:cd01475   83 TGLAIQYAMNNAFseaegaRPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180
                 ....*....|....*....|....
gi 295789104 648 SFFVDEFDNLHQYVPRIIQNICTE 671
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKICVV 186
VWA pfam00092
von Willebrand factor type A domain;
293-436 1.97e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 140.10  E-value: 1.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 371
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789104  372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 436
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 495-657 1.33e-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: 137.87  E-value: 1.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTST 574
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 575 GAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAM--AAHLKGVITYAIGVAWA-----AQEELEVIATHPA 644
Cdd:cd01469   82 ATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIASKPP 161

                        170
                 ....*....|...
gi 295789104 645 RDHSFFVDEFDNL 657
Cdd:cd01469  162 EEHFFNVTDFAAL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 292-436 1.89e-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: 134.34  E-value: 1.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGL-S 370
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789104 371 NVGRAISFVTKNFFSKANgNRSGAPNVVVVMVDGWPTD--KVEEASRLARESGINIFFITIEGAAENE 436
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEE 147
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 293-438 5.01e-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: 133.35  E-value: 5.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 371
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104   372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 438
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 494-649 1.97e-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: 119.98  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGT 572
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 573 STGAAINFALEQLFKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGV-AWAAQEELEVIATHPARDHS 648
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElrkLGITVYTIGIgDDANEDELKEIADKTTGGAV 160


                 .
gi 295789104 649 F 649
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 ...
 494-654 2.80e-31

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: 119.74  E-value: 2.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 572
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 573 STGAAINFALEQLFKKSKPNK-----RKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHParDH 647
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRieegvPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                 ....*..
gi 295789104 648 SFFVDEF 654
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 ...
 293-446 6.13e-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: 113.19  E-value: 6.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 293 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLS-N 371
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789104 372 VGRAISFVTKNFFSKANGNR--SGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVV-EPNFA 446
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAfDPSFV 159
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 292-494 8.61e-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: 111.71  E-value: 8.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 371
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 372 VGRAISFVTKNFFSKANGNRSGAPN---VVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE-KQYVVEPnfAN 447
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSERvprVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEElREIASEP--LA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 295789104 448 KAVcrtngFYslhVQSWFGLHKTLQPLVKRVCDTDRLA------CSKTCLNSA 494
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 ...
 292-439 1.59e-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: 103.59  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 371
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 372 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRL--ARESGINIFFITIEGAAENEKQY 439
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHFQRENSR 150
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 292-439 3.63e-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: 102.26  E-value: 3.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKIT-QRGGLS 370
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789104 371 NVGRAISFVTKNFFSKAngnRSGAPNVVVVMVDGWPTD---KVEEASRLARESGINIFFITIeGAAENEKQY 439
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 ...
 494-652 2.93e-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: 97.46  E-value: 2.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEF------EISDTDTRIGAVQYTYEQRLEFGFDK-YSSKPDILNAIKRVG 566
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 567 YWSGGTSTGAAINFALEQLFKKSKPNKRKLMILITDGRSY-DDVRIPAMAA----HLkGVITYAIGVAWAAQEELEVIAT 641
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDgSPDGGIEKAVneadHL-GIKIFFVAVGSQNEEPLSRIAC 161

                        170       180
                 ....*....|....*....|.
gi 295789104 642 ----------HPARDHSFFVD 652
Cdd:cd01480  162 dgksalyrenFAELLWSFFID 182
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 494-650 3.12e-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: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGtGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYE--QRLEFGFDKYSSKPDILNAIKRVGYWSGG 571
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 572 TSTGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPA-MAAHLKGVITYAIGV---AWAAQEELEVIATHPar 645
Cdd:cd01476   80 TATGAAIEVALQQLDPSEgrREGIPKVVVVLTDGRSHDDPEKQArILRAVPNIETFAVGTgdpGTVDTEELHSITGNE-- 157


                 ....*
gi 295789104 646 DHSFF 650
Cdd:cd01476  158 DHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 293-429 9.44e-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: 9.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 293 DLSFLIDGSTSIgKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATH--FNLKTHTNSRDLKTAIEKITQRGGLS 370
Cdd:cd01476    2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 371 NVGRAISFVTkNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARES-GINIFFITI 429
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 ...
 290-441 1.62e-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: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 290 CKIDLSFLIDGSTSIGKRRFRIQKQLLADVAQ------ALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRD-LKTAIEK 362
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTsLKEAVDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 363 ITQRGGLSNVGRAISFVTKNFFskaNGNRSGAPNVVVVMVDGWPT----DKVEEASRLARESGINIFFITIeGAAENEKQ 438
Cdd:cd01480   81 LEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAV-GSQNEEPL 156


                 ...
gi 295789104 439 YVV 441
Cdd:cd01480  157 SRI 159
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 495-628 1.01e-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: 67.03  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 495 DIGFVIDGSSSVGTGN-FRTVLQFVTNLTKEFEISDTDTRIGAVQYTY--EQRLEFGFDKYSSKPDILNAIK--RVGYWS 569
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTnaKELIRLSSPNSTNKDLALNAIRalLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295789104 570 GG-TSTGAAINFALEQLF--KKSKPNKRKLMILITDGRSYDDVRIPAMAAHLK--GVITYAIGV 628
Cdd:cd01471   82 NGsTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRerGVIIAVLGV 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 493-657 2.00e-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: 68.04  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 493 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 565
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 566 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAA--QEELEVIA 640
Cdd:COG1240  161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRDNAGRIDPLEAAELaaaAGIRIYTIGVGTEAvdEGLLREIA 238

                        170       180
                 ....*....|....*....|...
gi 295789104 641 T------HPARDHSFFVDEFDNL 657
Cdd:COG1240  239 EatggryFRADDLSELAAIYREI 261
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 490-671 2.32e-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: 65.99  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 490 CLNSADIGFVIDGSSSVgTGNFRTVLQFVTNLTKEFeiSDTDTRIGAVQYTYEQRLEFGFDKYSSKPDI-LNAIKRVGYw 568
Cdd:cd01474    1 CAGHFDLYFVLDKSGSV-AANWIEIYDFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 569 SGGTSTGAAINFALEQLFKKSKPNKR--KLMILITDGRSYDDVRIPAMA----AHLKGVITYAIGVAWAAQEELEVIATH 642
Cdd:cd01474   77 SGQTYIHEGLENANEQIFNRNGGGREtvSVIIALTDGQLLLNGHKYPEHeaklSRKLGAIVYCVGVTDFLKSQLINIADS 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 295789104 643 ParDHSFFVDE-FDNLHQYVPRIIQNICTE 671
Cdd:cd01474  157 K--EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 292-452 4.20e-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: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 292 IDLSFLIDGSTSIG-KRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKThTNSRDLKTAIE------KIT 364
Cdd:cd01471    1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSS-PNSTNKDLALNairallSLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 365 QRGGLSNVGRAISFVTKNFFSKAnGNRSGAPNVVVVMVDGWPTDK---VEEASRLaRESGINIFFITIegaaeneKQYVv 441
Cdd:cd01471   80 YPNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKfrtLKEARKL-RERGVIIAVLGV-------GQGV- 149

                        170
                 ....*....|.
gi 295789104 442 epnfaNKAVCR 452
Cdd:cd01471  150 -----NHEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
296-400 6.27e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  296 FLIDGSTSI-----GKRRFRIQKQLLADVAQALdigpAGPLMGVVQYGDNPATHFNLKThtNSRDLKTAIEKITQRGGLS 370
Cdd:pfam13519   3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 295789104  371 NVGRAISFVTKNFFskanGNRSGAPNVVVV 400
Cdd:pfam13519  77 NLAAALQLARAALK----HRRKNQPRRIVL 102
VWA_2 pfam13519
von Willebrand factor type A domain;
498-600 5.68e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104  498 FVIDGSSSVGTGNFR-TVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKysSKPDILNAIKRVGYWSGGTSTGA 576
Cdd:pfam13519   3 FVLDTSGSMRNGDYGpTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGTNLAA 80

                          90       100
                  ....*....|....*....|....
gi 295789104  577 AINFAlEQLFKKSKPNKRKLMILI 600
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 ...
 494-653 9.73e-08

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: 52.33  E-value: 9.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTV--LQFVTNLTKEFEISDTDTRIGAVQytyeqrleFGFDKYSSKP---------DILNAI 562
Cdd:cd01467    3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVV--------FAGAAFTQAPltldreslkELLEDI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 563 KrVGYWSGGTSTGAAINFALEQlFKKSKPnKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAAQEELEVI 639
Cdd:cd01467   75 K-IGLAGQGTAIGDAIGLAIKR-LKNSEA-KERVIVLLTDGENNAGEIDPATAAELaknKGVRIYTIGVGKSGSGPKPDG 151

                        170
                 ....*....|....
gi 295789104 640 ATHPARDHSFFVDE 653
Cdd:cd01467  152 STILDEDSLVEIAD 165
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 569-654 3.03e-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: 45.02  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 569 SGGTSTGAAINFALEQLFK---KSKPNK----RKLMILITDGRSYDDV-----RIPAMAAHLKGVITYAIGVAwAAQEEL 636
Cdd:cd01464   76 SGGTSMGAALELALDCIDRrvqRYRADQkgdwRPWVFLLTDGEPTDDLtaaieRIKEARDSKGRIVACAVGPK-ADLDTL 154

                         90
                 ....*....|....*....
gi 295789104 637 EVIATH-PARDHSFFVDEF 654
Cdd:cd01464  155 KQITEGvPLLDDALSGLNF 173
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 572-628 3.30e-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: 45.01  E-value: 3.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295789104 572 TSTGAAINFALEQLFKKskPNKRKLMILITDGR----SYDDVRIPAMAAHLK--------GVITYAIGV 628
Cdd:cd01454   84 TRDGAAIRHAAERLLAR--PEKRKILLVISDGEpndlDYYEGNVFATEDALRaviearklGIEVFGITI 150
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 495-601 4.96e-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: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 495 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTD------TRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYW 568
Cdd:cd01477   21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 295789104 569 SGGTS-----TG--AAINfALEQLFKKSKPNKRKLMILIT 601
Cdd:cd01477  101 VSSTNasyldTGlqAAEQ-MLAAGKRTSRENYKKVVIVFA 139
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 494-671 9.54e-05

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 44.71  E-value: 9.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 494 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEfeISDTDtRIGAVQY--TYEQRLEFGfdKYSSKPDILNAIKRVgYWSGG 571
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQ--LRPGD-RVSIVTFagDARVLLPPT--PATDRAKILAAIDRL-QAGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 572 TSTGAAINFALEQLFKKSKPNKRKLMILITDGR----SYDDVRIPAMAAHL--KGVITYAIGVAWAAQEE-LEVIATHpA 644
Cdd:COG2304  166 TALGAGLELAYELARKHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAreEGITLTTLGVGSDYNEDlLERLADA-G 244

                        170       180
                 ....*....|....*....|....*..
gi 295789104 645 RDHSFFVDEFDNLHQYVPRIIQNICTE 671
Cdd:COG2304  245 GGNYYYIDDPEEAEKVFVREFSRIGYE 271
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
569-635 3.24e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.22  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 569 SGGTSTGAAINFALEQL---FKKSKPNK----RKLMILITDGRSYDDV------RIPAMAAHLKGVItYAIGVAWAAQEE 635
Cdd:COG4245   78 SGGTPLGAALELLLDLIerrVQKYTAEGkgdwRPVVFLITDGEPTDSDweaalqRLKDGEAAKKANI-FAIGVGPDADTE 156
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
569-645 5.46e-04

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 42.78  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 569 SGGTST--GAAINFALEQLfkKSKPNKRKLMILITDGRSYD-----------DVRIPAMAAHLKGVITYAIGVAWAAQEE 635
Cdd:COG4548  330 EPGYYTrmGAAIRHATALL--AAQPARRRLLLVLTDGKPNDidvyegrygieDTRQAVREARRAGIHPFCITIDPEADDY 407

                         90
                 ....*....|....*...
gi 295789104 636 LE--------VIATHPAR 645
Cdd:COG4548  408 LPrifgrggyTVIDDVER 425
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 498-640 1.24e-03

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: 40.33  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 498 FVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDtdtRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYwSGGTSTGAA 577
Cdd:cd01465    5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGGAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 578 INFALEQLFKKSKPNKRKLMILITDGRSY----DDVRIPAMAAHL--KGVITYAIGVAWAAQEEL-EVIA 640
Cdd:cd01465   81 IQLGYQEAQKHFVPGGVNRILLATDGDFNvgetDPDELARLVAQKreSGITLSTLGFGDNYNEDLmEAIA 150
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 542-628 3.91e-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: 39.66  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789104 542 EQRLEFGFDKysSKPDILNAIKRVGYwSGGTSTGAAINFALEQLfkKSKPNKRKLMILITDGRSYDDVR--IPAMAAHLK 619
Cdd:COG2425  166 VEDLPLTADD--GLEDAIEFLSGLFA-GGGTDIAPALRAALELL--EEPDYRNADIVLITDGEAGVSPEelLREVRAKES 240


                 ....*....
gi 295789104 620 GVITYAIGV 628
Cdd:COG2425  241 GVRLFTVAI 249
 
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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