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Conserved domains on  [gi|569007279|ref|XP_006527154|]
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von Willebrand factor A domain-containing protein 2 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 301-458 4.75e-40

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: 143.20  E-value: 4.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007279 381 GTALLHIEDKVMTVQRGARPGVPKAVVMLTGGSGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRDSLiHV 458
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSET-HV 158
VWA pfam00092
von Willebrand factor type A domain;
113-286 8.31e-26

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 8.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFS-GGPTL 191
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  192 TGSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQD-EVSGPAAHARARELLLLGVG-SEILQAELVKITGSPKHVMV 269
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAP-KVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 569007279  270 HTDpqDLFSQIPELQRR 286
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 483-518 9.93e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 53.79  E-value: 9.93e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 569007279 483 VNLCK-PSPCMNEGTCVLKNGSYRCECRGGWEGPHCE 518
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 69-99 4.15e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 4.15e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 569007279   69 CDSQPCQNGGTCIPEGvDRYHCLCPLAFGGE 99
Cdd:pfam00008   1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 301-458 4.75e-40

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: 143.20  E-value: 4.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007279 381 GTALLHIEDKVMTVQRGARPGVPKAVVMLTGGSGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRDSLiHV 458
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSET-HV 158
VWA pfam00092
von Willebrand factor type A domain;
301-450 1.30e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 131.24  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGvGSA 380
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGG-GTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007279  381 --GTALLHIEDKVMTVQRGARPGVPKAVVMLTGG-SGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAG 450
Cdd:pfam00092  80 ntGKALKYALENLFSSAAGARPGAPKVVVLLTDGrSQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIAS 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 301-475 1.56e-33

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: 125.64  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   381 -GTALLHIEDKVMTVQRGARPGVPKAVVMLTGG---SGAEDAAVPAQKLRGNGISVLVMSVG-AVLREAVRRLAGPRDSL 455
Cdd:smart00327  81 lGAALQYALENLFSKSAGSRRGAPKVVILITDGesnDGPKDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                          170       180
                   ....*....|....*....|
gi 569007279   456 ihvaaYTDLPYHQDMLIEWL 475
Cdd:smart00327 161 -----YVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
113-286 8.31e-26

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 8.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFS-GGPTL 191
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  192 TGSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQD-EVSGPAAHARARELLLLGVG-SEILQAELVKITGSPKHVMV 269
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAP-KVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 569007279  270 HTDpqDLFSQIPELQRR 286
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 112-265 2.68e-24

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: 99.22  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPTL 191
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007279 192 TGSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQDEVSGPAAhARAR---ELLLLGVGSeILQAELVKITGSPK 265
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVP-KVLVVITDGKSQDDVEEPAV-ELKQagiEVFAVGVKN-ADEEELKQIASDPK 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 113-284 4.23e-24

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: 99.07  E-value: 4.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSI-PFSGGPTL 191
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   192 TGSALLQVAEHGFgSASRTGQDRPRRVVVLLTESRSQD---EVSGPAAHARAR--ELLLLGVGSEILQAELVKITGSPKH 266
Cdd:smart00327  81 LGAALQYALENLF-SKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*...
gi 569007279   267 VMVHTDpqDLFSQIPELQ 284
Cdd:smart00327 160 VYVFLP--ELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 273-449 6.62e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.95  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 273 PQDLFSQIPELQRRLCSQPRPGCQAQSLDLVFLLDASASVGREN-----FAQMQSFIRKCTLRfdvnpdvTQVGLVVYGS 347
Cdd:COG1240   66 LLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRPR-------DRVGLVAFGG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 348 RVQTAFGLDTHptRAAVLRAMSQAPyLGGvgsaGTALLHIEDKVMTVQRGARPGVPKAVVMLTGG---SGAEDAAVPAQK 424
Cdd:COG1240  139 EAEVLLPLTRD--REALKRALDELP-PGG----GTPLGDALALALELLKRADPARRKVIVLLTDGrdnAGRIDPLEAAEL 211

                        170       180
                 ....*....|....*....|....*..
gi 569007279 425 LRGNGISVLVMSVG--AVLREAVRRLA 449
Cdd:COG1240  212 AAAAGIRIYTIGVGteAVDEGLLREIA 238
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 483-518 9.93e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 53.79  E-value: 9.93e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 569007279 483 VNLCK-PSPCMNEGTCVLKNGSYRCECRGGWEGPHCE 518
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
483-518 1.82e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 1.82e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 569007279   483 VNLCK-PSPCMNEGTCVLKNGSYRCECRGGWE-GPHCE 518
Cdd:smart00179   2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 69-99 4.15e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 4.15e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 569007279   69 CDSQPCQNGGTCIPEGvDRYHCLCPLAFGGE 99
Cdd:pfam00008   1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 486-516 4.64e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.44  E-value: 4.64e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 569007279  486 CKPSPCMNEGTCVLKNGSYRCECRGGWEGPH 516
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 68-102 5.80e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.54  E-value: 5.80e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569007279  68 PCD-SQPCQNGGTCIPeGVDRYHCLCPLAFGGEVNC 102
Cdd:cd00053    1 ECAaSNPCSNGGTCVN-TPGSYRCVCPPGYTGDRSC 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
69-102 5.94e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 5.94e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 569007279    69 CDS-QPCQNGGTCIPeGVDRYHCLCPLAFGGEVNC 102
Cdd:smart00179   5 CASgNPCQNGGTCVN-TVGSYRCECPPGYTDGRNC 38
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 301-458 4.75e-40

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: 143.20  E-value: 4.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007279 381 GTALLHIEDKVMTVQRGARPGVPKAVVMLTGGSGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRDSLiHV 458
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSET-HV 158
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 300-454 5.39e-39

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 140.12  E-value: 5.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGS 379
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007279 380 A-GTALLHIEDKvMTVQRGARPGVPKAVVMLTGG--SGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRDS 454
Cdd:cd01450   81 NtGKALQYALEQ-LFSESNARENVPKVIIVLTDGrsDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA pfam00092
von Willebrand factor type A domain;
301-450 1.30e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 131.24  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGvGSA 380
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGG-GTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007279  381 --GTALLHIEDKVMTVQRGARPGVPKAVVMLTGG-SGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAG 450
Cdd:pfam00092  80 ntGKALKYALENLFSSAAGARPGAPKVVVLLTDGrSQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIAS 152
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 301-464 1.10e-34

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: 128.50  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 381 GTALLHIEDKVMTVQRGARPGVPKAVVMLTGGSGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRDSLiHVAA 460
Cdd:cd01472   82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL-YVFN 160


                 ....
gi 569007279 461 YTDL 464
Cdd:cd01472  161 VADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 301-475 1.56e-33

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: 125.64  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGSA 380
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   381 -GTALLHIEDKVMTVQRGARPGVPKAVVMLTGG---SGAEDAAVPAQKLRGNGISVLVMSVG-AVLREAVRRLAGPRDSL 455
Cdd:smart00327  81 lGAALQYALENLFSKSAGSRRGAPKVVILITDGesnDGPKDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                          170       180
                   ....*....|....*....|
gi 569007279   456 ihvaaYTDLPYHQDMLIEWL 475
Cdd:smart00327 161 -----YVFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 300-513 2.16e-32

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: 124.03  E-value: 2.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGS 379
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 380 AGTALLHIEDKVMTVQRGARPG---VPKAVVMLTGGSGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGP--RDS 454
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEplADH 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007279 455 LIHVAAYTdlpyhqdmLIEWLCReaRLPVNLCK-PSPCmNEGT------CVLKNGSYRCECRGGWE 513
Cdd:cd01475  163 VFYVEDFS--------TIEELTK--KFQGKICVvPDLC-ATLShvcqqvCISTPGSYLCACTEGYA 217
VWA pfam00092
von Willebrand factor type A domain;
113-286 8.31e-26

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 8.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFS-GGPTL 191
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  192 TGSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQD-EVSGPAAHARARELLLLGVG-SEILQAELVKITGSPKHVMV 269
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAP-KVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 569007279  270 HTDpqDLFSQIPELQRR 286
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 301-439 1.51e-24

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: 100.09  E-value: 1.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVG-S 379
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007279 380 AGTALLHIEDKVMTVQRGAR--PGVPKAVVMLTGGSGAEDAAVPAQKLRGNGIsvLVMSVGA 439
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGI--VPFAIGA 141
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 112-265 2.68e-24

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: 99.22  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPTL 191
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007279 192 TGSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQDEVSGPAAhARAR---ELLLLGVGSeILQAELVKITGSPK 265
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVP-KVLVVITDGKSQDDVEEPAV-ELKQagiEVFAVGVKN-ADEEELKQIASDPK 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 113-284 4.23e-24

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: 99.07  E-value: 4.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSI-PFSGGPTL 191
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279   192 TGSALLQVAEHGFgSASRTGQDRPRRVVVLLTESRSQD---EVSGPAAHARAR--ELLLLGVGSEILQAELVKITGSPKH 266
Cdd:smart00327  81 LGAALQYALENLF-SKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*...
gi 569007279   267 VMVHTDpqDLFSQIPELQ 284
Cdd:smart00327 160 VYVFLP--ELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 112-269 6.04e-23

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: 95.44  E-value: 6.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGP-T 190
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 191 LTGSALLQVAEHGFgSASRTGQDRPrRVVVLLTESRSQD--EVSGPAAHARAR--ELLLLGVGSeILQAELVKITGSPKH 266
Cdd:cd01450   81 NTGKALQYALEQLF-SESNARENVP-KVIIVLTDGRSDDggDPKEAAAKLKDEgiKVFVVGVGP-ADEEELREIASCPSE 157


                 ...
gi 569007279 267 VMV 269
Cdd:cd01450  158 RHV 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 300-450 2.52e-21

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 90.92  E-value: 2.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVgRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQT--AFGLDTHPTRAAVLRAMSQAPYLGGV 377
Cdd:cd01476    1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007279 378 GSAGTAllhIED--KVMTVQRGARPGVPKAVVMLTGGSGAEDAAVPAQKLR-GNGISVLVMSVG---AVLREAVRRLAG 450
Cdd:cd01476   80 TATGAA---IEValQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGdpgTVDTEELHSITG 155
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 300-447 1.84e-20

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 88.95  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGS 379
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007279 380 AGTALLHIEDKVMTVQRGARPGVPKAVVMLTGG----SGAEDAAVPAQKLRG---NGISVLvmsvGAVLREAVRR 447
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGeshdDPLLKDVIPQAEREGiirYAIGVG----GHFQRENSRE 151
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 300-454 1.26e-19

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: 86.08  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQAPYLGGVGS 379
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 380 A-GTALLHIEDkvmTVQRGARPGVPKAVVMLTGG---SGAEDAAVPAQKLRGNGISVLVMSVG-AVLREAVRRLAGPRDS 454
Cdd:cd00198   81 NiGAALRLALE---LLKSAKRPNARRVIILLTDGepnDGPELLAEAARELRKLGITVYTIGIGdDANEDELKEIADKTTG 157
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 112-262 5.80e-19

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: 84.15  E-value: 5.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFS-GGPT 190
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007279 191 LTGSALLQVAEHGFGSASrtgqDRPRRVVVLLTESRSQDEVSGPA-----AHARARELLLLGVGSEILQAELVKITG 262
Cdd:cd00198   81 NIGAALRLALELLKSAKR----PNARRVIILLTDGEPNDGPELLAeaareLRKLGITVYTIGIGDDANEDELKEIAD 153
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 111-336 1.32e-18

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: 84.74  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 111 RIDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPT 190
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 191 LTGSALLQVAEHGFGSAS--RTGQDRPRRVVVLLTESRSQDEVSGPAAHARAR--ELLLLGVGSEILqAELVKITGSP-- 264
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEgaRPGSERVPRVGIVVTDGRPQDDVSEVAAKARALgiEMFAVGVGRADE-EELREIASEPla 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007279 265 KHVMVHTDpqdlFSQIPEL----QRRLCSQPRPgCQAQSLDlVFLLDASASVgrenfaqmqSFIRKCTLRFDVNPD 336
Cdd:cd01475  161 DHVFYVED----FSTIEELtkkfQGKICVVPDL-CATLSHV-CQQVCISTPG---------SYLCACTEGYALLED 221
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 113-264 1.18e-16

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: 77.71  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPTLT 192
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007279 193 GSALLQVAEHGFGSASRTGQDRPrRVVVLLTESRSQDEVSGPAAHARAR--ELLLLGVGSEIlQAELVKITGSP 264
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVP-KVVILITDGKSQDDVELPARVLRNLgvNVFAVGVKDAD-ESELKMIASKP 153
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 113-270 1.94e-16

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: 77.05  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 113 DVLFLLDSSaGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASY---GRNLMVaVPVGEYQHVPDLIRSLDSIPFSGGP 189
Cdd:cd01476    2 DLLFVLDSS-GSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYsgrGRQRVR-FNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 190 TLTGSALLQVAEHGFGSASRtgQDRPRRVVVLLTESRSQDEVSGPAAHARAR---ELLLLGVG--SEILQAELVKITGSP 264
Cdd:cd01476   80 TATGAAIEVALQQLDPSEGR--REGIPKVVVVLTDGRSHDDPEKQARILRAVpniETFAVGTGdpGTVDTEELHSITGNE 157


                 ....*.
gi 569007279 265 KHVMVH 270
Cdd:cd01476  158 DHIFTD 163
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 113-272 7.79e-15

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: 72.36  E-value: 7.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 113 DVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPTL- 191
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 192 TGSALLQVAEHGFGSA--SRTGQDRPrRVVVLLTESRSQDEVSGPAAHARARELLLLGVGS-EILQAELVKITGSPKHVM 268
Cdd:cd01481   82 TGSALDYVVKNLFTKSagSRIEEGVP-QFLVLITGGKSQDDVERPAVALKRAGIVPFAIGArNADLAELQQIAFDPSFVF 160


                 ....
gi 569007279 269 VHTD 272
Cdd:cd01481  161 QVSD 164
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 300-454 2.51e-13

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 68.57  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGREN-FAQMQSFIRKCTLRFDVNPDVTQVGLVVYGSRVQTAFGLDTHP-----TRAAVLRAMSQAPY 373
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstnkdLALNAIRALLSLYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 374 LGGVGSAGTALLHIEdKVMTVQRGARPGVPKAVVMLTGG--SGAEDAAVPAQKLRGNGISVLVMSVGA-VLREAVRRLAG 450
Cdd:cd01471   81 PNGSTNTTSALLVVE-KHLFDTRGNRENAPQLVIIMTDGipDSKFRTLKEARKLRERGVIIAVLGVGQgVNHEENRSLVG 159


                 ....
gi 569007279 451 PRDS 454
Cdd:cd01471  160 CDPD 163
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 273-449 6.62e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.95  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 273 PQDLFSQIPELQRRLCSQPRPGCQAQSLDLVFLLDASASVGREN-----FAQMQSFIRKCTLRfdvnpdvTQVGLVVYGS 347
Cdd:COG1240   66 LLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrleaaKGALLDFLDDYRPR-------DRVGLVAFGG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 348 RVQTAFGLDTHptRAAVLRAMSQAPyLGGvgsaGTALLHIEDKVMTVQRGARPGVPKAVVMLTGG---SGAEDAAVPAQK 424
Cdd:COG1240  139 EAEVLLPLTRD--REALKRALDELP-PGG----GTPLGDALALALELLKRADPARRKVIVLLTDGrdnAGRIDPLEAAEL 211

                        170       180
                 ....*....|....*....|....*..
gi 569007279 425 LRGNGISVLVMSVG--AVLREAVRRLA 449
Cdd:COG1240  212 AAAAGIRIYTIGVGteAVDEGLLREIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 110-228 7.96e-10

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: 58.55  E-value: 7.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 110 CRIDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSR------ARVGIASYGRNLMV-AVPVGEYQHVPDLIRSLDS 182
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYSDQQEVeAGFLRDIRNYTSLKEAVDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569007279 183 IPFSGGPTLTGSALLQVAEHgFGSASRTGQdrpRRVVVLLTESRSQ 228
Cdd:cd01480   81 LEYIGGGTFTDCALKYATEQ-LLEGSHQKE---NKFLLVITDGHSD 122
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 483-518 9.93e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 53.79  E-value: 9.93e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 569007279 483 VNLCK-PSPCMNEGTCVLKNGSYRCECRGGWEGPHCE 518
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 112-229 1.13e-09

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: 57.75  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGTTLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEYQHVPDLIRSLDSIPFSGGPTL 191
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569007279 192 TGSALLQVAEHGFgSASRTGQDRPRRVVVLLTESRSQD 229
Cdd:cd01469   81 TATAIQYVVTELF-SESNGARKDATKVLVVITDGESHD 117
EGF_CA smart00179
Calcium-binding EGF-like domain;
483-518 1.82e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 1.82e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 569007279   483 VNLCK-PSPCMNEGTCVLKNGSYRCECRGGWE-GPHCE 518
Cdd:smart00179   2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
VWA_2 pfam13519
von Willebrand factor type A domain;
302-409 5.64e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.06  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  302 LVFLLDASASVGRE-----NFAQMQSFIRKCtlrFDVNPDVtQVGLVVYGSRVQTAFGLDTHptRAAVLRAMSQAPYLGG 376
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLAL---LKSLPGD-RVGLVTFGDGPEVLIPLTKD--RAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 569007279  377 VGSAGTALlhieDKVMTVQRGARPGVPKAVVML 409
Cdd:pfam13519  75 GTNLAAAL----QLARAALKHRRKNQPRRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 300-449 5.85e-07

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: 50.08  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRKCTLRF------DVNPDVTQVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQA-P 372
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDNlE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 373 YLGGVGSAGTALLHIEDKvmtVQRGARPGVPKAVVMLTGG-------SGAEDAAVPAQKLrgnGISVLVMSVGAVLREAV 445
Cdd:cd01480   83 YIGGGTFTDCALKYATEQ---LLEGSHQKENKFLLVITDGhsdgspdGGIEKAVNEADHL---GIKIFFVAVGSQNEEPL 156


                 ....
gi 569007279 446 RRLA 449
Cdd:cd01480  157 SRIA 160
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 488-518 7.81e-07

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 45.55  E-value: 7.81e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 569007279 488 PSPCMNEGTCVLKNGSYRCECRGGWEGP-HCE 518
Cdd:cd00053    5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
VWA_2 pfam13519
von Willebrand factor type A domain;
114-222 1.23e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.90  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279  114 VLFLLDSSA---GTTLGGFR--RAKAFVKRFVQAvLREDsraRVGIASYGRNLMVAVPVGeyQHVPDLIRSLDSIPFSGG 188
Cdd:pfam13519   1 LVFVLDTSGsmrNGDYGPTRleAAKDAVLALLKS-LPGD---RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569007279  189 PTLTGSALLQVAehgfgSASRTGQDRPRRVVVLL 222
Cdd:pfam13519  75 GTNLAAALQLAR-----AALKHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 112-256 2.25e-06

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: 48.15  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 112 IDVLFLLDSSAGT-TLGGFRRAKAFVKRFVQAVLREDSRARVGIASYGRNLMVAVPVGEY-----QHVPDLIRSLDSIPF 185
Cdd:cd01471    1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007279 186 SGGPTLTGSALLQVAEHGFgsASRTGQDRPRRVVVLLTESRSQDEVSGPAAHARARE----LLLLGVGSEILQAE 256
Cdd:cd01471   81 PNGSTNTTSALLVVEKHLF--DTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRErgviIAVLGVGQGVNHEE 153
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 69-99 4.15e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 4.15e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 569007279   69 CDSQPCQNGGTCIPEGvDRYHCLCPLAFGGE 99
Cdd:pfam00008   1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 486-516 4.64e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.44  E-value: 4.64e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 569007279  486 CKPSPCMNEGTCVLKNGSYRCECRGGWEGPH 516
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 68-102 5.80e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.54  E-value: 5.80e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569007279  68 PCD-SQPCQNGGTCIPeGVDRYHCLCPLAFGGEVNC 102
Cdd:cd00053    1 ECAaSNPCSNGGTCVN-TPGSYRCVCPPGYTGDRSC 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 69-102 1.89e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 1.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 569007279  69 CDSQ-PCQNGGTCIPeGVDRYHCLCPLAFGGEvNC 102
Cdd:cd00054    5 CASGnPCQNGGTCVN-TVGSYRCSCPPGYTGR-NC 37
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 491-517 3.50e-04

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 38.10  E-value: 3.50e-04
                          10        20
                  ....*....|....*....|....*..
gi 569007279  491 CMNEGTCVLKNGsyRCECRGGWEGPHC 517
Cdd:pfam07974   2 CSGRGTCVNQCG--KCVCDSGYQGATC 26
EGF_CA smart00179
Calcium-binding EGF-like domain;
69-102 5.94e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 5.94e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 569007279    69 CDS-QPCQNGGTCIPeGVDRYHCLCPLAFGGEVNC 102
Cdd:smart00179   5 CASgNPCQNGGTCVN-TVGSYRCECPPGYTDGRNC 38
EGF smart00181
Epidermal growth factor-like domain;
488-518 6.65e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.50  E-value: 6.65e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 569007279   488 PSPCMNeGTCVLKNGSYRCECRGGWEG-PHCE 518
Cdd:smart00181   5 GGPCSN-GTCINTPGSYTCSCPPGYTGdKRCE 35
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 300-449 8.12e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 41.63  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQ----MQSFIRKctLRfdvnPDVTqVGLVVYGSRVQTAFGLDTHPTRAAVLRAMSQApYLG 375
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELakeaAKLLVDQ--LR----PGDR-VSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 376 GvgsaGTALLH-IEDKVMTVQRGARPGVPKAVVMLTGG---SGAEDAAVP---AQKLRGNGISVLVMSVGAVLREAV-RR 447
Cdd:COG2304  164 G----GTALGAgLELAYELARKHFIPGRVNRVILLTDGdanVGITDPEELlklAEEAREEGITLTTLGVGSDYNEDLlER 239


                 ..
gi 569007279 448 LA 449
Cdd:COG2304  240 LA 241
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 301-453 8.68e-04

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: 40.57  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 301 DLVFLLDASASVGrENFAQMQSFIRKCTLRFdVNPDvTQVGLVVYGSRVQTAFGL--DTHPTRAAVLRAMSQAPylGGVG 378
Cdd:cd01474    6 DLYFVLDKSGSVA-ANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLtdDSSAIIKGLEVLKKVTP--SGQT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007279 379 SAGTALLHIEDKVMTVQRGARPgVPKAVVMLTGG----SGAEDAAVPAQKLRGNGISVLVMSVGAVLREAVRRLAGPRD 453
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGqlllNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKE 158
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 300-432 2.96e-03

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: 38.94  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQM--------QSFIRKCTlRFDvNPDVTQVGLVVYGSRVQTAFGLDtHPTRAAVLRAMSQA 371
Cdd:cd01477   20 LDIVFVVDNSKGMTQGGLWQVratisslfGSSSQIGT-DYD-DPRSTRVGLVTYNSNATVVADLN-DLQSFDDLYSQIQG 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007279 372 PYLgGVGSA-----GTALLHIEDKVMTVQRGARPGVPKAVVMLT---GGSGAEDAAVPAQKLRGNGISV 432
Cdd:cd01477   97 SLT-DVSSTnasylDTGLQAAEQMLAAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAI 164
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 300-463 3.57e-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: 38.41  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 300 LDLVFLLDASASVGRENFAQMQSFIRkcTLRFDVNPDvTQVGLVVYGSRVQTAfgLDTHPT--RAAVLRAMSQAPYLGGV 377
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALK--LLVDQLRPD-DRLAIVTYDGAAETV--LPATPVrdKAAILAAIDRLTAGGST 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007279 378 -GSAGTALlhiedKVMTVQRGARPGVPKAVVMLTGG------SGAEDAAVPAQKLRGNGISVLVMSVGAVLREAV-RRLA 449
Cdd:cd01465   76 aGGAGIQL-----GYQEAQKHFVPGGVNRILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLmEAIA 150

                        170
                 ....*....|....
gi 569007279 450 GPRDsliHVAAYTD 463
Cdd:cd01465  151 DAGN---GNTAYID 161
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 491-512 4.22e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 35.00  E-value: 4.22e-03
                          10        20
                  ....*....|....*....|..
gi 569007279  491 CMNEGTCVLKNGSYRCECRGGW 512
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 74-93 6.43e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 34.23  E-value: 6.43e-03
                          10        20
                  ....*....|....*....|
gi 569007279   74 CQNGGTCIpEGVDRYHCLCP 93
Cdd:pfam12661   1 CQNGGTCV-DGVNGYKCQCP 19
 
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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