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Conserved domains on  [gi|767962761|ref|XP_011538056|]
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von Willebrand factor A domain-containing protein 2 isoform X4 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10891046)

VWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

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 ...
 534-664 8.75e-37

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: 135.49  E-value: 8.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767962761 614 GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGRGAEDAAVPAQKLRNNGIS 664
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVN 132
VWA pfam00092
von Willebrand factor type A domain;
346-519 1.32e-25

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPTL 424
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED-EVAGPARHARARELLLLGVG-SEAVRAELEEITGSPKHVMV 502
Cdd:pfam00092  81 TGKALKYALENLF-SSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 767962761  503 YSDpqDLFNQIPELQGK 519
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 127-208 4.90e-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.


The actual alignment was detected with superfamily member cd01482:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 85.03  E-value: 4.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 127 KGGRTETELALKYLLHRGLPGGRNAS--VPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEPR 204
Cdd:cd01482   75 KGGNTRTGKALTHVREKNFTPDAGARpgVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154


                 ....
gi 767962761 205 GQHV 208
Cdd:cd01482  155 ETHV 158
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 716-751 3.38e-09

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: 52.64  E-value: 3.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767962761 716 VNLCK-PSPCMNEGSCVLQNGSYRCKCRDGWEGPHCE 751
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 302-332 3.77e-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: 43.91  E-value: 3.77e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767962761  302 CDSQPCQNGGTCVPEGlDGYQCLCPLAFGGE 332
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 ...
 534-664 8.75e-37

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: 135.49  E-value: 8.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767962761 614 GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGRGAEDAAVPAQKLRNNGIS 664
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVN 132
VWA pfam00092
von Willebrand factor type A domain;
534-664 7.58e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 122.00  E-value: 7.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGvGSA 613
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGG-GTT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767962761  614 --GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGR-GAEDAAVPAQKLRNNGIS 664
Cdd:pfam00092  80 ntGKALKYALENLFSSAAGARPGAPKVVVLLTDGRsQDGDPEEVARELKSAGVT 133
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 534-664 6.05e-29

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: 113.70  E-value: 6.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767962761   614 -GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGR---GAEDAAVPAQKLRNNGIS 664
Cdd:smart00327  81 lGAALQYALENLFSKSAGSRRGAPKVVILITDGEsndGPKDLLKAAKELKRSGVK 135
VWA pfam00092
von Willebrand factor type A domain;
346-519 1.32e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPTL 424
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED-EVAGPARHARARELLLLGVG-SEAVRAELEEITGSPKHVMV 502
Cdd:pfam00092  81 TGKALKYALENLF-SSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 767962761  503 YSDpqDLFNQIPELQGK 519
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 345-505 1.10e-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: 101.15  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 345 VDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPTL 424
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 425 TGSALRQAAERGFGSATRTGQDRPrRVVVLLTESHSEDEVAGPARhARAR---ELLLLGVGSeAVRAELEEITGSPK--H 499
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVP-KVLVVITDGKSQDDVEEPAV-ELKQagiEVFAVGVKN-ADEEELKQIASDPKelY 157


                 ....*.
gi 767962761 500 VMVYSD 505
Cdd:cd01472  158 VFNVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 346-513 1.22e-21

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: 92.52  E-value: 1.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPTL 424
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED---EVAGPARHARAR--ELLLLGVGSEAVRAELEEITGSPKH 499
Cdd:smart00327  81 LGAALQYALENLF-SKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*.
gi 767962761   500 VMVY--SDPQDLFNQI 513
Cdd:smart00327 160 VYVFlpELLDLLIDLL 175
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 127-208 4.90e-19

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: 85.03  E-value: 4.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 127 KGGRTETELALKYLLHRGLPGGRNAS--VPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEPR 204
Cdd:cd01482   75 KGGNTRTGKALTHVREKNFTPDAGARpgVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154


                 ....
gi 767962761 205 GQHV 208
Cdd:cd01482  155 ETHV 158
VWA pfam00092
von Willebrand factor type A domain;
128-208 6.66e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 76.16  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  128 GGRTETELALKYLLH---RGLPGGRnASVPQILIIVTDGKSQ-GDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEP 203
Cdd:pfam00092  76 GGTTNTGKALKYALEnlfSSAAGAR-PGAPKVVVLLTDGRSQdGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEP 154


                  ....*
gi 767962761  204 RGQHV 208
Cdd:pfam00092 155 GEGHV 159
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 128-216 1.36e-12

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: 66.71  E-value: 1.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   128 GGRTETELALKYLLHRGLPG--GRNASVPQILIIVTDGKSQ---GDVALPSKQLKERGVTVFAVGV-RFPRWEELHALAS 201
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKsaGSRRGAPKVVILITDGESNdgpKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLAS 155

                           90
                   ....*....|....*
gi 767962761   202 EPRGQHVLLAEQVED 216
Cdd:smart00327 156 APGGVYVFLPELLDL 170
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 716-751 3.38e-09

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: 52.64  E-value: 3.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767962761 716 VNLCK-PSPCMNEGSCVLQNGSYRCKCRDGWEGPHCE 751
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 463-663 2.67e-08

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: 55.71  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 463 EVAGPARHARARELLLLGVGSEAVRAELEEITGSPKHVMVYSDPQDLFNQIPELQGKLCSRQRPGCRTQALDLVFMLDTS 542
Cdd:COG1240   23 LLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDAS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 543 ASVGPEN-FAQMQSFVRSCALQFEVNpdvTQVGLVVYGSQVQTAFGLDTkpTRAAMLRAISQAPyLGGvgsaGTALLHIY 621
Cdd:COG1240  103 GSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGG----GTPLGDAL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767962761 622 DKVMTVQRGARPGVPKAVVVLTGGR---GAEDAAVPAQKLRNNGI 663
Cdd:COG1240  173 ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGI 217
EGF_CA smart00179
Calcium-binding EGF-like domain;
716-751 1.66e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.66e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767962761   716 VNLCK-PSPCMNEGSCVLQNGSYRCKCRDGWE-GPHCE 751
Cdd:smart00179   2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 302-332 3.77e-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: 43.91  E-value: 3.77e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767962761  302 CDSQPCQNGGTCVPEGlDGYQCLCPLAFGGE 332
Cdd:pfam00008   1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 301-335 2.73e-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: 41.69  E-value: 2.73e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767962761 301 PCD-SQPCQNGGTCVPeGLDGYQCLCPLAFGGEANC 335
Cdd:cd00053    1 ECAaSNPCSNGGTCVN-TPGSYRCVCPPGYTGDRSC 35
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 719-749 1.39e-04

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: 39.67  E-value: 1.39e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767962761  719 CKPSPCMNEGSCVLQNGSYRCKCRDGWEGPH 749
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
302-335 2.56e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 2.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767962761   302 CDS-QPCQNGGTCVPeGLDGYQCLCPLAFGGEANC 335
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 ...
 534-664 8.75e-37

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: 135.49  E-value: 8.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767962761 614 GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGRGAEDAAVPAQKLRNNGIS 664
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVN 132
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 533-687 2.47e-34

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 128.56  E-value: 2.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGS 612
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767962761 613 A-GTALLHIYDKvMTVQRGARPGVPKAVVVLTGGR--GAEDAAVPAQKLRNNGISVLVVGVGPVLSEGLRRLAGPRDS 687
Cdd:cd01450   81 NtGKALQYALEQ-LFSESNARENVPKVIIVLTDGRsdDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 534-697 3.60e-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: 128.11  E-value: 3.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 614 GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGRGAEDAAVPAQKLRNNGISVLVVGVGPVLSEGLRRLAGPRDSLiHVAA 693
Cdd:cd01472   82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL-YVFN 160


                 ....
gi 767962761 694 YADL 697
Cdd:cd01472  161 VADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 532-746 6.71e-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: 123.65  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 532 ALDLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVG 611
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 612 SAGTALLHIYDKVMTVQRGARPG---VPKAVVVLTGGRGAEDAAVPAQKLRNNGISVLVVGVGPVLSEGLRRLAGP--RD 686
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEplAD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962761 687 SLIHVAAYADLRYHQDVLIEWLCGEakqpvnlckPSPCmNEGS------CVLQNGSYRCKCRDGWE 746
Cdd:cd01475  162 HVFYVEDFSTIEELTKKFQGKICVV---------PDLC-ATLShvcqqvCISTPGSYLCACTEGYA 217
VWA pfam00092
von Willebrand factor type A domain;
534-664 7.58e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 122.00  E-value: 7.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGvGSA 613
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGG-GTT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767962761  614 --GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGR-GAEDAAVPAQKLRNNGIS 664
Cdd:pfam00092  80 ntGKALKYALENLFSSAAGARPGAPKVVVLLTDGRsQDGDPEEVARELKSAGVT 133
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 534-664 6.05e-29

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: 113.70  E-value: 6.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGSA 613
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767962761   614 -GTALLHIYDKVMTVQRGARPGVPKAVVVLTGGR---GAEDAAVPAQKLRNNGIS 664
Cdd:smart00327  81 lGAALQYALENLFSKSAGSRRGAPKVVILITDGEsndGPKDLLKAAKELKRSGVK 135
VWA pfam00092
von Willebrand factor type A domain;
346-519 1.32e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.89  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPTL 424
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED-EVAGPARHARARELLLLGVG-SEAVRAELEEITGSPKHVMV 502
Cdd:pfam00092  81 TGKALKYALENLF-SSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPGEGHV 159

                         170
                  ....*....|....*..
gi 767962761  503 YSDpqDLFNQIPELQGK 519
Cdd:pfam00092 160 FTV--SDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 345-505 1.10e-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: 101.15  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 345 VDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPTL 424
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 425 TGSALRQAAERGFGSATRTGQDRPrRVVVLLTESHSEDEVAGPARhARAR---ELLLLGVGSeAVRAELEEITGSPK--H 499
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVP-KVLVVITDGKSQDDVEEPAV-ELKQagiEVFAVGVKN-ADEEELKQIASDPKelY 157


                 ....*.
gi 767962761 500 VMVYSD 505
Cdd:cd01472  158 VFNVAD 163
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 534-663 5.14e-23

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: 96.24  E-value: 5.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 534 DLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVG-S 612
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767962761 613 AGTALLHIYDKVMTVQRGAR--PGVPKAVVVLTGGRGAEDAAVPAQKLRNNGI 663
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGI 134
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 345-503 5.66e-22

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: 93.12  E-value: 5.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 345 VDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGP-T 423
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 424 LTGSALRQAAERGFgSATRTGQDRPrRVVVLLTESHSED--EVAGPARHARAR--ELLLLGVGSeAVRAELEEITGSPKH 499
Cdd:cd01450   81 NTGKALQYALEQLF-SESNARENVP-KVIIVLTDGRSDDggDPKEAAAKLKDEgiKVFVVGVGP-ADEEELREIASCPSE 157


                 ....
gi 767962761 500 VMVY 503
Cdd:cd01450  158 RHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 346-513 1.22e-21

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: 92.52  E-value: 1.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPTL 424
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED---EVAGPARHARAR--ELLLLGVGSEAVRAELEEITGSPKH 499
Cdd:smart00327  81 LGAALQYALENLF-SKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*.
gi 767962761   500 VMVY--SDPQDLFNQI 513
Cdd:smart00327 160 VYVFlpELLDLLIDLL 175
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 533-645 2.85e-21

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: 91.65  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGS 612
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767962761 613 AGTALLHIYDKVMTVQRGARPGVPKAVVVLTGG 645
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDG 113
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 346-500 2.16e-19

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: 85.91  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 346 DLLFLLDSSaGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYS--RELLVAVPVGEYQDVPDLVWSLDGIPFRGGPT 423
Cdd:cd01476    2 DLLFVLDSS-GSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 424 LTGSALRQAAERGFGSATRtgQDRPRRVVVLLTESHSEDEVAGPARHARAR---ELLLLGVG--SEAVRAELEEITGSPK 498
Cdd:cd01476   81 ATGAAIEVALQQLDPSEGR--REGIPKVVVVLTDGRSHDDPEKQARILRAVpniETFAVGTGdpGTVDTEELHSITGNED 158


                 ..
gi 767962761 499 HV 500
Cdd:cd01476  159 HI 160
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 345-495 4.58e-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: 84.92  E-value: 4.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 345 VDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFR-GGPT 423
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767962761 424 LTGSALRQAAERGFGSATrtgqDRPRRVVVLLT---ESHSEDEVAGPARHARAR--ELLLLGVGSEAVRAELEEITG 495
Cdd:cd00198   81 NIGAALRLALELLKSAKR----PNARRVIILLTdgePNDGPELLAEAARELRKLgiTVYTIGIGDDANEDELKEIAD 153
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 127-208 4.90e-19

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: 85.03  E-value: 4.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 127 KGGRTETELALKYLLHRGLPGGRNAS--VPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEPR 204
Cdd:cd01482   75 KGGNTRTGKALTHVREKNFTPDAGARpgVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154


                 ....
gi 767962761 205 GQHV 208
Cdd:cd01482  155 ETHV 158
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 533-659 2.37e-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: 82.83  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPEnFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQT--AFGLDTKPTRAAMLRAISQAPYLGGV 610
Cdd:cd01476    1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767962761 611 GSAGTALLHIYDkVMTVQRGARPGVPKAVVVLTGGRGAEDAAVPAQKLR 659
Cdd:cd01476   80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILR 127
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 131-247 7.87e-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: 83.20  E-value: 7.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 131 TETELALKYLLHRGLP---GGR--NASVPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEPRG 205
Cdd:cd01475   81 TMTGLAIQYAMNNAFSeaeGARpgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767962761 206 QHVLLAEQvedatnglFSTLSS------SAICSSATPdCRVEAHPCEH 247
Cdd:cd01475  161 DHVFYVED--------FSTIEEltkkfqGKICVVPDL-CATLSHVCQQ 199
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 533-664 1.15e-17

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: 80.69  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPENFAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGGVGS 612
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767962761 613 A-GTALLHIYDkvmTVQRGARPGVPKAVVVLTGGR---GAEDAAVPAQKLRNNGIS 664
Cdd:cd00198   81 NiGAALRLALE---LLKSAKRPNARRVIILLTDGEpndGPELLAEAARELRKLGIT 133
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 346-504 1.58e-17

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: 80.41  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPTLT 425
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 426 GSALRQAAERGFGSATRTGQDRPrRVVVLLTESHSEDEVAGPARHARAR--ELLLLGVgSEAVRAELEEITGSPKHVMVY 503
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVP-KVVILITDGKSQDDVELPARVLRNLgvNVFAVGV-KDADESELKMIASKPSETHVF 159


                 .
gi 767962761 504 S 504
Cdd:cd01482  160 N 160
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 344-521 1.72e-17

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: 82.05  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 344 RVDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPT 423
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 424 LTGSALRQAAERGFGSA--TRTGQDRPRRVVVLLTESHSEDEVAGPARHARAR--ELLLLGVGSeAVRAELEEITGSP-- 497
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAegARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALgiEMFAVGVGR-ADEEELREIASEPla 160

                        170       180
                 ....*....|....*....|....*
gi 767962761 498 KHVMvYSDPQDLFNQIPE-LQGKLC 521
Cdd:cd01475  161 DHVF-YVEDFSTIEELTKkFQGKIC 184
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 123-208 3.23e-16

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: 76.88  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 123 RLKKKGGRTETELALKYLL--HRGLPGGRNASVPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELHALA 200
Cdd:cd01472   71 NLRYIGGGTNTGKALKYVRenLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150


                 ....*...
gi 767962761 201 SEPRGQHV 208
Cdd:cd01472  151 SDPKELYV 158
VWA pfam00092
von Willebrand factor type A domain;
128-208 6.66e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 76.16  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  128 GGRTETELALKYLLH---RGLPGGRnASVPQILIIVTDGKSQ-GDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEP 203
Cdd:pfam00092  76 GGTTNTGKALKYALEnlfSSAAGAR-PGAPKVVVLLTDGRSQdGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEP 154


                  ....*
gi 767962761  204 RGQHV 208
Cdd:pfam00092 155 GEGHV 159
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 346-505 2.77e-14

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: 71.20  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 346 DLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPTL- 424
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 425 TGSALRQAAERGFgsaTRTGQDRPRRVV----VLLTESHSEDEVAGPARHARARELLLLGVGS-EAVRAELEEITGSPKH 499
Cdd:cd01481   82 TGSALDYVVKNLF---TKSAGSRIEEGVpqflVLITGGKSQDDVERPAVALKRAGIVPFAIGArNADLAELQQIAFDPSF 158


                 ....*.
gi 767962761 500 VMVYSD 505
Cdd:cd01481  159 VFQVSD 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 128-216 1.36e-12

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: 66.71  E-value: 1.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761   128 GGRTETELALKYLLHRGLPG--GRNASVPQILIIVTDGKSQ---GDVALPSKQLKERGVTVFAVGV-RFPRWEELHALAS 201
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKsaGSRRGAPKVVILITDGESNdgpKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLAS 155

                           90
                   ....*....|....*
gi 767962761   202 EPRGQHVLLAEQVED 216
Cdd:smart00327 156 APGGVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 128-209 2.12e-12

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: 65.78  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 128 GGRTETELALKYLLHRGL-PGGRNASVPQILIIVTDGKSQ--GDVALPSKQLKERGVTVFAVGVRFPRWEELHALASEPR 204
Cdd:cd01450   77 GGGTNTGKALQYALEQLFsESNARENVPKVIIVLTDGRSDdgGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 767962761 205 GQHVL 209
Cdd:cd01450  157 ERHVF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 343-466 1.44e-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: 60.86  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 343 CRVDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSR------ARVGVATYSRE-LLVAVPVGEYQDVPDLVWSLDG 415
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYSDQqEVEAGFLRDIRNYTSLKEAVDN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767962761 416 IPFRGGPTLTGSALRQAAERgFGSATRTGQdrpRRVVVLLTESHSEDEVAG 466
Cdd:cd01480   81 LEYIGGGTFTDCALKYATEQ-LLEGSHQKE---NKFLLVITDGHSDGSPDG 127
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 124-216 3.50e-10

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: 59.68  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 124 LKKKGGRTETELALKYLLHRGLP---GGRNaSVPQILIIVTDGKSQGDVALPS--KQLKERGVTVFAVGV--RFPR---W 193
Cdd:cd01469   72 ISQLLGLTNTATAIQYVVTELFSesnGARK-DATKVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVggHFQRensR 150

                         90       100
                 ....*....|....*....|...
gi 767962761 194 EELHALASEPRGQHVLlaeQVED 216
Cdd:cd01469  151 EELKTIASKPPEEHFF---NVTD 170
VWA_2 pfam13519
von Willebrand factor type A domain;
535-642 2.08e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.38  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  535 LVFMLDTSAS-----VGPENFAQMQSFVRSCalqFEVNPDVtQVGLVVYGSQVQTAFGLDTkpTRAAMLRAISQAPYLGG 609
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLAL---LKSLPGD-RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767962761  610 vgsaGTALLHIYDKVMTVQRGARPGVPKAVVVL 642
Cdd:pfam13519  75 ----GTNLAAALQLARAALKHRRKNQPRRIVLI 103
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 716-751 3.38e-09

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: 52.64  E-value: 3.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767962761 716 VNLCK-PSPCMNEGSCVLQNGSYRCKCRDGWEGPHCE 751
Cdd:cd00054    2 IDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 128-208 1.81e-08

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: 54.49  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 128 GGRTETELALKYLLHRgLPGGRNASVPQILIIVTDGKSQGDVALP---SKQLKERGVTVFAVGVRFPR-WEELHALASEP 203
Cdd:cd00198   77 GGGTNIGAALRLALEL-LKSAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDDAnEDELKEIADKT 155


                 ....*
gi 767962761 204 RGQHV 208
Cdd:cd00198  156 TGGAV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 533-662 2.36e-08

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: 54.70  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPEN-FAQMQSFVRSCALQFEVNPDVTQVGLVVYGSQVQTAFGLDT-----KPTRAAMLRAISQAPY 606
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnstnKDLALNAIRALLSLYY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767962761 607 LGGVGSAGTALLHIyDKVMTVQRGARPGVPKAVVVLTGG--RGAEDAAVPAQKLRNNG 662
Cdd:cd01471   81 PNGSTNTTSALLVV-EKHLFDTRGNRENAPQLVIIMTDGipDSKFRTLKEARKLRERG 137
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 532-698 2.62e-08

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: 54.31  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 532 ALDLVFMLDTSASVGPENFAQMQSFVRSCALQFEVN------PDVTQVGLVVYGSQVQTAFGLDTKPT-RAAMLRAISQA 604
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 605 PYLGGVGSAGTALLHIYDKvmtVQRGARPGVPKAVVVLTGGR-------GAEDAAVPAQKLrnnGISVLVVGVGPVLSEG 677
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQ---LLEGSHQKENKFLLVITDGHsdgspdgGIEKAVNEADHL---GIKIFFVAVGSQNEEP 155

                        170       180
                 ....*....|....*....|.
gi 767962761 678 LRRLAGPRDSLIHVAAYADLR 698
Cdd:cd01480  156 LSRIACDGKSALYRENFAELL 176
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 463-663 2.67e-08

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: 55.71  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 463 EVAGPARHARARELLLLGVGSEAVRAELEEITGSPKHVMVYSDPQDLFNQIPELQGKLCSRQRPGCRTQALDLVFMLDTS 542
Cdd:COG1240   23 LLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDAS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 543 ASVGPEN-FAQMQSFVRSCALQFEVNpdvTQVGLVVYGSQVQTAFGLDTkpTRAAMLRAISQAPyLGGvgsaGTALLHIY 621
Cdd:COG1240  103 GSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGG----GTPLGDAL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767962761 622 DKVMTVQRGARPGVPKAVVVLTGGR---GAEDAAVPAQKLRNNGI 663
Cdd:COG1240  173 ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGI 217
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 123-204 3.39e-08

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: 53.48  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 123 RLKKKGGRT-ETELALKYLLHRGL--PGGRNAS--VPQILIIVTDGKSQGDVALPSKQLKERGVTVFAVGVRFPRWEELH 197
Cdd:cd01481   71 RLRLRGGSQlNTGSALDYVVKNLFtkSAGSRIEegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQ 150


                 ....*..
gi 767962761 198 ALASEPR 204
Cdd:cd01481  151 QIAFDPS 157
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 345-505 6.38e-08

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: 53.13  E-value: 6.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 345 VDLLFLLDSSAGTTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGEYQDVPDLVWSLDGIPFRGGPTL 424
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 425 TGSALRQAAERGFgSATRTGQDRPRRVVVLLTESHSED-----------EVAGPARHArarelllLGVG----SEAVRAE 489
Cdd:cd01469   81 TATAIQYVVTELF-SESNGARKDATKVLVVITDGESHDdpllkdvipqaEREGIIRYA-------IGVGghfqRENSREE 152

                        170
                 ....*....|....*...
gi 767962761 490 LEEITGSP--KHVMVYSD 505
Cdd:cd01469  153 LKTIASKPpeEHFFNVTD 170
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 721-751 1.38e-06

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: 45.16  E-value: 1.38e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767962761 721 PSPCMNEGSCVLQNGSYRCKCRDGWEGP-HCE 751
Cdd:cd00053    5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
716-751 1.66e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.66e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767962761   716 VNLCK-PSPCMNEGSCVLQNGSYRCKCRDGWE-GPHCE 751
Cdd:smart00179   2 IDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
VWA_2 pfam13519
von Willebrand factor type A domain;
347-455 2.13e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.90  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761  347 LLFLLDSSAG-TTLDGFLRAKVFVKRFVRAVLSEDSRARVGVATYSRELLVAVPVGeyQDVPDLVWSLDGIPFRGGPTLT 425
Cdd:pfam13519   1 LVFVLDTSGSmRNGDYGPTRLEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGGGTNL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 767962761  426 GSALRQAAergfgSATRTGQDRPRRVVVLL 455
Cdd:pfam13519  79 AAALQLAR-----AALKHRRKNQPRRIVLI 103
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 302-332 3.77e-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: 43.91  E-value: 3.77e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767962761  302 CDSQPCQNGGTCVPEGlDGYQCLCPLAFGGE 332
Cdd:pfam00008   1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 124-204 1.27e-05

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: 46.24  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 124 LKKKGGRTETELALKYLLHRGLPG-GRNASVPQILIIVTDGKSQGDVALPSKQLKER-GVTVFAVGVRFPRW---EELHA 198
Cdd:cd01476   73 LRFIGGTTATGAAIEVALQQLDPSeGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDPGTvdtEELHS 152


                 ....*.
gi 767962761 199 LASEPR 204
Cdd:cd01476  153 ITGNED 158
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 301-335 2.73e-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: 41.69  E-value: 2.73e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767962761 301 PCD-SQPCQNGGTCVPeGLDGYQCLCPLAFGGEANC 335
Cdd:cd00053    1 ECAaSNPCSNGGTCVN-TPGSYRCVCPPGYTGDRSC 35
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 448-664 3.24e-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: 46.63  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 448 PRRVVVLLTESHSEDEVAGPARHARARELLLLGVGSEAVRAELEEITGSPKhvmVYSDPQDLFNQIPELQGK------LC 521
Cdd:COG2304    4 GFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPY---DYPLPTGRLAQSPWNPQTrlllvgLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 522 SRQRPGCRTQALDLVFMLDTSASvgpenfaqMQSF----VRSCALQF--EVNPDVTqVGLVVYGSQVQTAFGLDTKPTRA 595
Cdd:COG2304   81 PPKAAAEERPPLNLVFVIDVSGS--------MSGDklelAKEAAKLLvdQLRPGDR-VSIVTFAGDARVLLPPTPATDRA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767962761 596 AMLRAISQApYLGGVGSAGTALLHIYDkvmTVQRGARPGVPKAVVVLTGGR---GAEDAAVP---AQKLRNNGIS 664
Cdd:COG2304  152 KILAAIDRL-QAGGGTALGAGLELAYE---LARKHFIPGRVNRVILLTDGDanvGITDPEELlklAEEAREEGIT 222
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 719-749 1.39e-04

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: 39.67  E-value: 1.39e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767962761  719 CKPSPCMNEGSCVLQNGSYRCKCRDGWEGPH 749
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 724-750 1.85e-04

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


Pssm-ID: 400365  Cd Length: 26  Bit Score: 39.25  E-value: 1.85e-04
                          10        20
                  ....*....|....*....|....*..
gi 767962761  724 CMNEGSCVLQNGsyRCKCRDGWEGPHC 750
Cdd:pfam07974   2 CSGRGTCVNQCG--KCVCDSGYQGATC 26
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 302-335 2.11e-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: 39.16  E-value: 2.11e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767962761 302 CDSQ-PCQNGGTCVPeGLDGYQCLCPLAFGGEaNC 335
Cdd:cd00054    5 CASGnPCQNGGTCVN-TVGSYRCSCPPGYTGR-NC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
302-335 2.56e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 2.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767962761   302 CDS-QPCQNGGTCVPeGLDGYQCLCPLAFGGEANC 335
Cdd:smart00179   5 CASgNPCQNGGTCVN-TVGSYRCECPPGYTDGRNC 38
EGF smart00181
Epidermal growth factor-like domain;
721-751 5.26e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.88  E-value: 5.26e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767962761   721 PSPCMNeGSCVLQNGSYRCKCRDGWEG-PHCE 751
Cdd:smart00181   5 GGPCSN-GTCINTPGSYTCSCPPGYTGdKRCE 35
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 307-326 1.71e-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: 36.16  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|
gi 767962761  307 CQNGGTCVpEGLDGYQCLCP 326
Cdd:pfam12661   1 CQNGGTCV-DGVNGYKCQCP 19
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 127-187 2.03e-03

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: 40.06  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767962761 127 KGGRTETELALK-----YLLHRGlpgGRNaSVPQILIIVTDGKSQGD---VALpSKQLKERGV--TVFAVG 187
Cdd:cd01471   81 PNGSTNTTSALLvvekhLFDTRG---NRE-NAPQLVIIMTDGIPDSKfrtLKE-ARKLRERGViiAVLGVG 146
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 724-745 2.41e-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: 35.77  E-value: 2.41e-03
                          10        20
                  ....*....|....*....|..
gi 767962761  724 CMNEGSCVLQNGSYRCKCRDGW 745
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 533-646 9.89e-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: 37.64  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962761 533 LDLVFMLDTSASVGPENFAQMQSfvrscALQF---EVNPDvTQVGLVVYGSQVQTAFGLDTKPTRAAMLRAISQAPYLGG 609
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKS-----ALKLlvdQLRPD-DRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGS 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767962761 610 V-GSAGTALlhIYDkvmTVQRGARPGVPKAVVVLTGGR 646
Cdd:cd01465   75 TaGGAGIQL--GYQ---EAQKHFVPGGVNRILLATDGD 107
 
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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