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Conserved domains on  [gi|1962007750|ref|NP_001378897|]
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vitrin isoform 9 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 ...
 430-590 6.31e-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: 183.97  E-value: 6.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 509
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 586
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962007750 587 VDEF 590
Cdd:cd01472   161 VADF 164
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 229-392 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: 158.60  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 308
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 309 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 388
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962007750 389 TNGF 392
Cdd:cd01482   161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 1.15e-40

LCCL domain;


:

Pssm-ID: 427521  Cd Length: 96  Bit Score: 142.80  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962007750 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 ...
 430-590 6.31e-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: 183.97  E-value: 6.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 509
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 586
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962007750 587 VDEF 590
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
431-595 2.16e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.38  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 509
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSF 585
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|
gi 1962007750 586 FVDEFDNLHQ 595
Cdd:pfam00092 161 TVSDFEALED 170
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 229-392 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: 158.60  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 308
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 309 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 388
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962007750 389 TNGF 392
Cdd:cd01482   161 VADF 164
LCCL pfam03815
LCCL domain;
44-133 1.15e-40

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 142.80  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962007750 118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
LCCL smart00603
LCCL domain;
42-124 1.24e-38

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.14  E-value: 1.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750   42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 1962007750  120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 431-595 1.26e-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: 140.28  E-value: 1.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 509
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  510 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYD---DVRIPAMAAHLKGVITYAIGVAWAA-QEELEVIATHPARD 582
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 1962007750  583 HSFFVDEFDNLHQ 595
Cdd:smart00327 161 YVFLPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
229-372 3.27e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 138.95  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 307
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1962007750 308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 372
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 229-374 1.22e-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: 131.81  E-value: 1.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 307
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 374
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 429-593 1.75e-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: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 429 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 501
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 502 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAA--QEELEVIA 576
Cdd:COG1240   161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRDNAGRIDPLEAAELaaaAGIRIYTIGVGTEAvdEGLLREIA 238

                         170       180
                  ....*....|....*....|...
gi 1962007750 577 T------HPARDHSFFVDEFDNL 593
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 ...
 430-590 6.31e-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: 183.97  E-value: 6.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 509
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKK---SKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 586
Cdd:cd01472    81 TGKALKYVRENLFTEasgSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 1962007750 587 VDEF 590
Cdd:cd01472   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 430-590 3.68e-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: 170.93  E-value: 3.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 509
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFF 586
Cdd:cd01482    81 TGKALTHVREKNFTPDAgarPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 1962007750 587 VDEF 590
Cdd:cd01482   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
431-595 2.16e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.38  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS- 509
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLFKKS---KPNKRKLMILITDGRSYD-DVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSF 585
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|
gi 1962007750 586 FVDEFDNLHQ 595
Cdd:pfam00092 161 TVSDFEALED 170
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 229-392 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: 158.60  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNV 308
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 309 GRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKaVCR 388
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH-VFN 160


                  ....
gi 1962007750 389 TNGF 392
Cdd:cd01482   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 228-372 1.17e-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: 156.23  E-value: 1.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 307
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1962007750 308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE 372
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEE 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 430-585 2.90e-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: 155.14  E-value: 2.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 508
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 509 STGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPAMAAHLK--GVITYAIGVAWAAQEELEVIATHPARDHS 584
Cdd:cd01450    81 NTGKALQYALEQLFSESnaRENVPKVIIVLTDGRSDDGGDPKEAAAKLKdeGIKVFVVGVGPADEEELREIASCPSERHV 160


                  .
gi 1962007750 585 F 585
Cdd:cd01450   161 F 161
LCCL pfam03815
LCCL domain;
44-133 1.15e-40

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 142.80  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  44 INCDVKAGKI------IDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSY 117
Cdd:pfam03815   1 LSCSTTLLDIcnfcpfTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                          90
                  ....*....|....*.
gi 1962007750 118 SNGVQSLSLPRWRESF 133
Cdd:pfam03815  81 QNGIESLSLSSWSKSF 96
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 430-607 8.98e-39

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 142.14  E-value: 8.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTS 509
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 510 TGAAINFALEQLF------KKSKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDH 583
Cdd:cd01475    83 TGLAIQYAMNNAFseaegaRPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|....
gi 1962007750 584 SFFVDEFDNLHQYVPRIIQNICTE 607
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVV 186
LCCL smart00603
LCCL domain;
42-124 1.24e-38

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 137.14  E-value: 1.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750   42 PQINCDVKAGKIIDPEFI--VKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSN 119
Cdd:smart00603   1 QAVTCDTRGLDLCKPVTDnrVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDAN 80


                   ....*
gi 1962007750  120 GVQSL 124
Cdd:smart00603  81 GIQSE 85
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 431-595 1.26e-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: 140.28  E-value: 1.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGTS 509
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  510 TGAAINFALEQLFKKSK---PNKRKLMILITDGRSYD---DVRIPAMAAHLKGVITYAIGVAWAA-QEELEVIATHPARD 582
Cdd:smart00327  81 LGAALQYALENLFSKSAgsrRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|...
gi 1962007750  583 HSFFVDEFDNLHQ 595
Cdd:smart00327 161 YVFLPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
229-372 3.27e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 138.95  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 307
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1962007750 308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK-VEEASRLARESGINIFFITIEGAAENE 372
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEE 146
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 431-593 1.76e-37

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 137.10  E-value: 1.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTST 510
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 511 GAAINFALEQLFKKSK---PNKRKLMILITDGRSYDDVRIPAM--AAHLKGVITYAIGVAWA-----AQEELEVIATHPA 580
Cdd:cd01469    82 ATAIQYVVTELFSESNgarKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIASKPP 161

                         170
                  ....*....|...
gi 1962007750 581 RDHSFFVDEFDNL 593
Cdd:cd01469   162 EEHFFNVTDFAAL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-372 4.71e-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: 132.42  E-value: 4.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGL-S 306
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1962007750 307 NVGRAISFVTKNFFSKANgNRSGAPNVVVVMVDGWPTD--KVEEASRLARESGINIFFITIEGAAENE 372
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEE 147
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 229-374 1.22e-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: 131.81  E-value: 1.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQR-GGLSN 307
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750  308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDK---VEEASRLARESGINIFFITIeGAAENEKQ 374
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGV-GNDVDEEE 149
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 430-590 3.07e-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: 119.35  E-value: 3.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSG-GT 508
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 509 STGAAINFALEQLFKKSKPNK-----RKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHParDH 583
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRieegvPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                  ....*..
gi 1962007750 584 SFFVDEF 590
Cdd:cd01481   159 VFQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 430-585 3.98e-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: 118.82  E-value: 3.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGY-WSGGT 508
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 509 STGAAINFALEQLFKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGV-AWAAQEELEVIATHPARDHS 584
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElrkLGITVYTIGIgDDANEDELKEIADKTTGGAV 160


                  .
gi 1962007750 585 F 585
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 ...
 229-382 6.39e-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: 6.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLS-N 307
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1962007750 308 VGRAISFVTKNFFSKANGNR--SGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVV-EPNFA 382
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAfDPSFV 159
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 228-430 6.56e-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: 6.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 307
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 308 VGRAISFVTKNFFSKANGNRSGAPN---VVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENE-KQYVVEPnfAN 383
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGSERvprVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEElREIASEP--LA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1962007750 384 KAVcrtngFYslhVQSWFGLHKTLQPLVKRVCDTDRLA------CSKTCLNSA 430
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 ...
 228-375 2.35e-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: 2.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSN 307
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 308 VGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRL--ARESGINIFFITIEGAAENEKQY 375
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHFQRENSR 150
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-375 7.66e-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: 101.10  E-value: 7.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKIT-QRGGLS 306
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1962007750 307 NVGRAISFVTKNFFSKAngnRSGAPNVVVVMVDGWPTD---KVEEASRLARESGINIFFITIeGAAENEKQY 375
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 ...
 430-588 3.41e-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: 97.07  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEF------EISDTDTRIGAVQYTYEQRLEFGFDK-YSSKPDILNAIKRVG 502
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 503 YWSGGTSTGAAINFALEQLFKKSKPNKRKLMILITDGRSY-DDVRIPAMAA----HLkGVITYAIGVAWAAQEELEVIAT 577
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDgSPDGGIEKAVneadHL-GIKIFFVAVGSQNEEPLSRIAC 161

                         170       180
                  ....*....|....*....|.
gi 1962007750 578 ----------HPARDHSFFVD 588
Cdd:cd01480   162 dgksalyrenFAELLWSFFID 182
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 430-586 2.91e-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: 93.62  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGtGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYE--QRLEFGFDKYSSKPDILNAIKRVGYWSGG 507
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 508 TSTGAAINFALEQLFKKS--KPNKRKLMILITDGRSYDDVRIPA-MAAHLKGVITYAIGV---AWAAQEELEVIATHPar 581
Cdd:cd01476    80 TATGAAIEVALQQLDPSEgrREGIPKVVVVLTDGRSHDDPEKQArILRAVPNIETFAVGTgdpGTVDTEELHSITGNE-- 157


                  ....*
gi 1962007750 582 DHSFF 586
Cdd:cd01476   158 DHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 229-365 8.72e-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: 8.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 229 DLSFLIDGSTSIgKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATH--FNLKTHTNSRDLKTAIEKITQRGGLS 306
Cdd:cd01476     2 DLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 307 NVGRAISFVTkNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARES-GINIFFITI 365
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 ...
 226-377 1.79e-13

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 68.95  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 226 CKIDLSFLIDGSTSIGKRRFRIQKQLLADVAQ------ALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRD-LKTAIEK 298
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTsLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 299 ITQRGGLSNVGRAISFVTKNFFskaNGNRSGAPNVVVVMVDGWPT----DKVEEASRLARESGINIFFITIeGAAENEKQ 374
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAV-GSQNEEPL 156


                  ...
gi 1962007750 375 YVV 377
Cdd:cd01480   157 SRI 159
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 431-564 8.98e-13

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 67.03  E-value: 8.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 431 DIGFVIDGSSSVGTGN-FRTVLQFVTNLTKEFEISDTDTRIGAVQYTY--EQRLEFGFDKYSSKPDILNAIK--RVGYWS 505
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTnaKELIRLSSPNSTNKDLALNAIRalLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1962007750 506 GG-TSTGAAINFALEQLF--KKSKPNKRKLMILITDGRSYDDVRIPAMAAHLK--GVITYAIGV 564
Cdd:cd01471    82 NGsTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRerGVIIAVLGV 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 429-593 1.75e-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: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 429 SADIGFVIDGSSSVGTGN-----FRTVLQFVTNLTKefeisdtDTRIGAVQY--TYEQRLEFGFDKysskPDILNAIKRV 501
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRP-------RDRVGLVAFggEAEVLLPLTRDR----EALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 502 GyWSGGTSTGAAINFALEQLfKKSKPNKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAA--QEELEVIA 576
Cdd:COG1240   161 P-PGGGTPLGDALALALELL-KRADPARRKVIVLLTDGRDNAGRIDPLEAAELaaaAGIRIYTIGVGTEAvdEGLLREIA 238

                         170       180
                  ....*....|....*....|...
gi 1962007750 577 T------HPARDHSFFVDEFDNL 593
Cdd:COG1240   239 EatggryFRADDLSELAAIYREI 261
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 426-607 3.68e-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: 65.22  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 426 CLNSADIGFVIDGSSSVgTGNFRTVLQFVTNLTKEFeiSDTDTRIGAVQYTYEQRLEFGFDKYSSKPDI-LNAIKRVGYw 504
Cdd:cd01474     1 CAGHFDLYFVLDKSGSV-AANWIEIYDFVEQLVDRF--NSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 505 SGGTSTGAAINFALEQLFKKSKPNKR--KLMILITDGRSYDDVRIPAMA----AHLKGVITYAIGVAWAAQEELEVIATH 578
Cdd:cd01474    77 SGQTYIHEGLENANEQIFNRNGGGREtvSVIIALTDGQLLLNGHKYPEHeaklSRKLGAIVYCVGVTDFLKSQLINIADS 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1962007750 579 ParDHSFFVDE-FDNLHQYVPRIIQNICTE 607
Cdd:cd01474   157 K--EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 228-388 3.72e-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: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 228 IDLSFLIDGSTSIG-KRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKThTNSRDLKTAIE------KIT 300
Cdd:cd01471     1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSS-PNSTNKDLALNairallSLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 301 QRGGLSNVGRAISFVTKNFFSKAnGNRSGAPNVVVVMVDGWPTDK---VEEASRLaRESGINIFFITIegaaeneKQYVv 377
Cdd:cd01471    80 YPNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKfrtLKEARKL-RERGVIIAVLGV-------GQGV- 149

                         170
                  ....*....|.
gi 1962007750 378 epnfaNKAVCR 388
Cdd:cd01471   150 -----NHEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
232-336 5.85e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 5.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 232 FLIDGSTSI-----GKRRFRIQKQLLADVAQALdigpAGPLMGVVQYGDNPATHFNLKThtNSRDLKTAIEKITQRGGLS 306
Cdd:pfam13519   3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1962007750 307 NVGRAISFVTKNFFskanGNRSGAPNVVVV 336
Cdd:pfam13519  77 NLAAALQLARAALK----HRRKNQPRRIVL 102
VWA_2 pfam13519
von Willebrand factor type A domain;
434-536 5.20e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 5.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 434 FVIDGSSSVGTGNFR-TVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKysSKPDILNAIKRVGYWSGGTSTGA 512
Cdd:pfam13519   3 FVLDTSGSMRNGDYGpTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGTNLAA 80

                          90       100
                  ....*....|....*....|....
gi 1962007750 513 AINFAlEQLFKKSKPNKRKLMILI 536
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 ...
 430-589 9.96e-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: 9.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTV--LQFVTNLTKEFEISDTDTRIGAVQytyeqrleFGFDKYSSKP---------DILNAI 498
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDRRENDRIGLVV--------FAGAAFTQAPltldreslkELLEDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 499 KrVGYWSGGTSTGAAINFALEQlFKKSKPnKRKLMILITDGRSYDDVRIPAMAAHL---KGVITYAIGVAWAAQEELEVI 575
Cdd:cd01467    75 K-IGLAGQGTAIGDAIGLAIKR-LKNSEA-KERVIVLLTDGENNAGEIDPATAAELaknKGVRIYTIGVGKSGSGPKPDG 151

                         170
                  ....*....|....
gi 1962007750 576 ATHPARDHSFFVDE 589
Cdd:cd01467   152 STILDEDSLVEIAD 165
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 505-590 2.69e-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: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 505 SGGTSTGAAINFALEQLFK---KSKPNK----RKLMILITDGRSYDDV-----RIPAMAAHLKGVITYAIGVAwAAQEEL 572
Cdd:cd01464    76 SGGTSMGAALELALDCIDRrvqRYRADQkgdwRPWVFLLTDGEPTDDLtaaieRIKEARDSKGRIVACAVGPK-ADLDTL 154

                          90
                  ....*....|....*....
gi 1962007750 573 EVIATH-PARDHSFFVDEF 590
Cdd:cd01464   155 KQITEGvPLLDDALSGLNF 173
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 508-564 2.93e-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: 2.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1962007750 508 TSTGAAINFALEQLFKKskPNKRKLMILITDGR----SYDDVRIPAMAAHLK--------GVITYAIGV 564
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 ...
 431-537 4.83e-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: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 431 DIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTD------TRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYW 504
Cdd:cd01477    21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1962007750 505 SGGTS-----TG--AAINfALEQLFKKSKPNKRKLMILIT 537
Cdd:cd01477   101 VSSTNasyldTGlqAAEQ-MLAAGKRTSRENYKKVVIVFA 139
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 430-607 7.61e-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: 45.09  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 430 ADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEfeISDTDtRIGAVQY--TYEQRLEFGfdKYSSKPDILNAIKRVgYWSGG 507
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQ--LRPGD-RVSIVTFagDARVLLPPT--PATDRAKILAAIDRL-QAGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 508 TSTGAAINFALEQLFKKSKPNKRKLMILITDGR----SYDDVRIPAMAAHL--KGVITYAIGVAWAAQEE-LEVIATHpA 580
Cdd:COG2304   166 TALGAGLELAYELARKHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAreEGITLTTLGVGSDYNEDlLERLADA-G 244

                         170       180
                  ....*....|....*....|....*..
gi 1962007750 581 RDHSFFVDEFDNLHQYVPRIIQNICTE 607
Cdd:COG2304   245 GGNYYYIDDPEEAEKVFVREFSRIGYE 271
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
505-571 2.59e-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: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 505 SGGTSTGAAINFALEQL---FKKSKPNK----RKLMILITDGRSYDDV------RIPAMAAHLKGVItYAIGVAWAAQEE 571
Cdd:COG4245    78 SGGTPLGAALELLLDLIerrVQKYTAEGkgdwRPVVFLITDGEPTDSDweaalqRLKDGEAAKKANI-FAIGVGPDADTE 156
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
505-581 4.79e-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: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 505 SGGTST--GAAINFALEQLfkKSKPNKRKLMILITDGRSYD-----------DVRIPAMAAHLKGVITYAIGVAWAAQEE 571
Cdd:COG4548   330 EPGYYTrmGAAIRHATALL--AAQPARRRLLLVLTDGKPNDidvyegrygieDTRQAVREARRAGIHPFCITIDPEADDY 407

                          90
                  ....*....|....*...
gi 1962007750 572 LE--------VIATHPAR 581
Cdd:COG4548   408 LPrifgrggyTVIDDVER 425
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 434-576 1.11e-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: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 434 FVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDtdtRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYwSGGTSTGAA 513
Cdd:cd01465     5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGGAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 514 INFALEQLFKKSKPNKRKLMILITDGRSY----DDVRIPAMAAHL--KGVITYAIGVAWAAQEEL-EVIA 576
Cdd:cd01465    81 IQLGYQEAQKHFVPGGVNRILLATDGDFNvgetDPDELARLVAQKreSGITLSTLGFGDNYNEDLmEAIA 150
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 478-564 3.46e-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: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962007750 478 EQRLEFGFDKysSKPDILNAIKRVGYwSGGTSTGAAINFALEQLfkKSKPNKRKLMILITDGRSYDDVR--IPAMAAHLK 555
Cdd:COG2425   166 VEDLPLTADD--GLEDAIEFLSGLFA-GGGTDIAPALRAALELL--EEPDYRNADIVLITDGEAGVSPEelLREVRAKES 240


                  ....*....
gi 1962007750 556 GVITYAIGV 564
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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