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Conserved domains on  [gi|386831|gb|AAA51620|]
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integrin alpha subunit precursor [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 11546373)

integrin alpha forms a heterodimer with integrin beta to mediate cell-extracellular matrix and cell-cell interactions; integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 150-325 2.71e-90

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: 287.72  E-value: 2.71e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    150 QDIVFLIDGSGSISSRNFATMMNFVRAVISQFQR--PSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGFTY 227
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDyKDVIPMADAAGIIRYAIGVGLAFQNRNSWKELNDIASK 307
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 386831    308 PSQEHIFKVEDFDALKDI 325
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 616-1032 8.54e-31

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


The actual alignment was detected with superfamily member pfam08441:

Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 127.05  E-value: 8.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      616 RPVLWVGVSMQFIPAEIPRSAFECREQVVSeQTLVQSNICLYID-KRSKNllGSRDLQSSVTLDLALDPGRlSPRATFQE 694
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTgKPIPN--PSLVLNYELELDRQKKKGL-PPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      695 TKNRSLSRVRVL--GLKAHCENFNLLLPSCVEDSVTPITLRLNFTLVGKPL--LAFRNLRPMLAADAQRYFTASLPFEKN 770
Cdd:pfam08441   77 SQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      771 CGADHICQDNLGIS--FSFPGLKS-LLVGSNLELNAEVMVWNDGEDSYGTTITFSHPAGLSYRYVAEGQKQGQlrslhLT 847
Cdd:pfam08441  157 CGEDNVCVPDLQLSakFDSRESDEpLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-----LS 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      848 CDSAPVGSqgTWSTSCRI-NhlIFRGGAQITFLATFDVSPKAVLGDRLLLTANVSSEN-NTPRTSKTTfqLELPVKYAV- 924
Cdd:pfam08441  232 CTAKKENS--TRQVVCDLgN--PMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPVS--LKVPVVAEAq 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      925 --YTVVSSHEQFtkYLNFSESEEKESHVAM--------HRYQVNNLGQRDLP-VSINFWVPVELnQEAVW----MDVEvs 989
Cdd:pfam08441  306 lsLSGVSKPDQV--VGGSVKGESAMKPRSEedigplveHTYEVINNGPSTVSgASLEISWPYEL-SNGKWllylLDVQ-- 380

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386831      990 lPQNPsLRCSSEKIAGP------------ASDFLAHIQKNP---------------VLDC-SIAGCLRFRC 1032
Cdd:pfam08441  381 -GQGK-GECSPQNEINPlnltqslesskpLRTSRVHHVVKRrdvlksekatqtasvLLSCdSGARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 6.29e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 386831       517 PWGRFGAALTVLGDVNGDKLTDVVIGAPGEEENR--GAVYLFHG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-504 3.20e-06

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.44  E-value: 3.20e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386831       454 IGSYFGPSLCSV-DVDSDGSTDLVlIGPPHYYEQTRGAQVSVCPLPRGWRRW 504
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNS 51
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 7.28e-05

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 40.56  E-value: 7.28e-05
                           10
                   ....*....|....*
gi 386831     1129 KVGFFKRQYKEMMEE 1143
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-628 1.32e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.32e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 386831       582 QYFGQALSGGQDLTQDGLVDLAVGA--------RGQVLLLRTRPVLWVGVSMQFI 628
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQNL 57
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 150-325 2.71e-90

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: 287.72  E-value: 2.71e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    150 QDIVFLIDGSGSISSRNFATMMNFVRAVISQFQR--PSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGFTY 227
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDyKDVIPMADAAGIIRYAIGVGLAFQNRNSWKELNDIASK 307
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 386831    308 PSQEHIFKVEDFDALKDI 325
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
151-328 4.69e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 171.69  E-value: 4.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASV-HQLQGFTY 227
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDtlDYKDVIPMADAAGIIRYAIGVGlafqnRNSWKELNDIASK 307
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVG-----NADDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 386831      308 PSQEHIFKVEDFDALKDIQTQ 328
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 151-326 1.61e-41

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: 150.30  E-value: 1.61e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831       151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQR--PSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVH-QLQGFTY 227
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831       228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIGVGlafqNRNSWKELNDIASK 307
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASA 156

                           170
                    ....*....|....*....
gi 386831       308 PSQEHIFKVEDFDALKDIQ 326
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 616-1032 8.54e-31

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 127.05  E-value: 8.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      616 RPVLWVGVSMQFIPAEIPRSAFECREQVVSeQTLVQSNICLYID-KRSKNllGSRDLQSSVTLDLALDPGRlSPRATFQE 694
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTgKPIPN--PSLVLNYELELDRQKKKGL-PPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      695 TKNRSLSRVRVL--GLKAHCENFNLLLPSCVEDSVTPITLRLNFTLVGKPL--LAFRNLRPMLAADAQRYFTASLPFEKN 770
Cdd:pfam08441   77 SQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      771 CGADHICQDNLGIS--FSFPGLKS-LLVGSNLELNAEVMVWNDGEDSYGTTITFSHPAGLSYRYVAEGQKQGQlrslhLT 847
Cdd:pfam08441  157 CGEDNVCVPDLQLSakFDSRESDEpLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-----LS 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      848 CDSAPVGSqgTWSTSCRI-NhlIFRGGAQITFLATFDVSPKAVLGDRLLLTANVSSEN-NTPRTSKTTfqLELPVKYAV- 924
Cdd:pfam08441  232 CTAKKENS--TRQVVCDLgN--PMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPVS--LKVPVVAEAq 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      925 --YTVVSSHEQFtkYLNFSESEEKESHVAM--------HRYQVNNLGQRDLP-VSINFWVPVELnQEAVW----MDVEvs 989
Cdd:pfam08441  306 lsLSGVSKPDQV--VGGSVKGESAMKPRSEedigplveHTYEVINNGPSTVSgASLEISWPYEL-SNGKWllylLDVQ-- 380

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386831      990 lPQNPsLRCSSEKIAGP------------ASDFLAHIQKNP---------------VLDC-SIAGCLRFRC 1032
Cdd:pfam08441  381 -GQGK-GECSPQNEINPlnltqslesskpLRTSRVHHVVKRrdvlksekatqtasvLLSCdSGARCVVIRC 449
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 127-330 7.46e-14

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: 73.05  E-value: 7.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    127 FLLGPTQLTQRLPVSRQECPRQEQDIVFLIDGSGSISSRNfatMMNFVRAVISQF---QRPSTQFSLMQFSNKFQTHLTF 203
Cdd:COG1240   70 LAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAEN---RLEAAKGALLDFlddYRPRDRVGLVAFGGEAEVLLPL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    204 eefrrTSNPLSLLASVHQLQGFTYTAT--AIQNVVHRLFHASYGARrdatKILIVITDGKKEGDTLDYKDVIPMADAAGI 281
Cdd:COG1240  147 -----TRDREALKRALDELPPGGGTPLgdALALALELLKRADPARR----KVIVLLTDGRDNAGRIDPLEAAELAAAAGI 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 386831    282 IRYAIGVGLAFQNRnswKELNDIASKpSQEHIFKVEDFDALKDIQTQLR 330
Cdd:COG1240  218 RIYTIGVGTEAVDE---GLLREIAEA-TGGRYFRADDLSELAAIYREID 262
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 6.29e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 386831       517 PWGRFGAALTVLGDVNGDKLTDVVIGAPGEEENR--GAVYLFHG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 152-287 1.59e-07

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 54.24  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      152 IVFLIDGSGSIS-SRNFAT--MMNFVRAVIsqfqRPSTQFSLMQFSNKFQTHLTFeefrrTSNPLSLLASVHQLQ--GFT 226
Cdd:TIGR03436   56 VGLVIDTSGSMRnDLDRARaaAIRFLKTVL----RPNDRVFVVTFNTRLRLLQDF-----TSDPRLLEAALNRLKppLRT 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386831      227 YTATAIQNVVHRLFHASYGARRDAT--------------KILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIG 287
Cdd:TIGR03436  127 DYNSSGAFVRDGGGTALYDAITLAAleqlanalagipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 2.49e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.89  E-value: 2.49e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 386831      521 FGAALTVlGDVNGDKLTDVVIGAPGE-EENRGAVYLF 556
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-504 3.20e-06

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.44  E-value: 3.20e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386831       454 IGSYFGPSLCSV-DVDSDGSTDLVlIGPPHYYEQTRGAQVSVCPLPRGWRRW 504
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNS 51
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 7.28e-05

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 40.56  E-value: 7.28e-05
                           10
                   ....*....|....*
gi 386831     1129 KVGFFKRQYKEMMEE 1143
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-628 1.32e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.32e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 386831       582 QYFGQALSGGQDLTQDGLVDLAVGA--------RGQVLLLRTRPVLWVGVSMQFI 628
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 458-494 6.87e-03

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 35.18  E-value: 6.87e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 386831      458 FGPSLCSVDVDSDGSTDLVlIGPPHYYEQTRGAqVSV 494
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGAGAGA-VYV 35
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 150-325 2.71e-90

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: 287.72  E-value: 2.71e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    150 QDIVFLIDGSGSISSRNFATMMNFVRAVISQFQR--PSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGFTY 227
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDyKDVIPMADAAGIIRYAIGVGLAFQNRNSWKELNDIASK 307
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 386831    308 PSQEHIFKVEDFDALKDI 325
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
151-328 4.69e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 171.69  E-value: 4.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASV-HQLQGFTY 227
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDtlDYKDVIPMADAAGIIRYAIGVGlafqnRNSWKELNDIASK 307
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVG-----NADDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 386831      308 PSQEHIFKVEDFDALKDIQTQ 328
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 151-326 1.61e-41

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: 150.30  E-value: 1.61e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831       151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQR--PSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVH-QLQGFTY 227
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831       228 TATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIGVGlafqNRNSWKELNDIASK 307
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASA 156

                           170
                    ....*....|....*....
gi 386831       308 PSQEHIFKVEDFDALKDIQ 326
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 151-314 1.61e-31

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 121.24  E-value: 1.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQRP--STQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGF-TY 227
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHASyGARRDATKILIVITDGKKEGDTlDYKDVIPMADAAGIIRYAIGVGLAFQNrnswkELNDIASK 307
Cdd:cd01450   82 TGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPADEE-----ELREIASC 154


                 ....*..
gi 386831    308 PSQEHIF 314
Cdd:cd01450  155 PSERHVF 161
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 616-1032 8.54e-31

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 127.05  E-value: 8.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      616 RPVLWVGVSMQFIPAEIPRSAFECREQVVSeQTLVQSNICLYID-KRSKNllGSRDLQSSVTLDLALDPGRlSPRATFQE 694
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTgKPIPN--PSLVLNYELELDRQKKKGL-PPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      695 TKNRSLSRVRVL--GLKAHCENFNLLLPSCVEDSVTPITLRLNFTLVGKPL--LAFRNLRPMLAADAQRYFTASLPFEKN 770
Cdd:pfam08441   77 SQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      771 CGADHICQDNLGIS--FSFPGLKS-LLVGSNLELNAEVMVWNDGEDSYGTTITFSHPAGLSYRYVAEGQKQGQlrslhLT 847
Cdd:pfam08441  157 CGEDNVCVPDLQLSakFDSRESDEpLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-----LS 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      848 CDSAPVGSqgTWSTSCRI-NhlIFRGGAQITFLATFDVSPKAVLGDRLLLTANVSSEN-NTPRTSKTTfqLELPVKYAV- 924
Cdd:pfam08441  232 CTAKKENS--TRQVVCDLgN--PMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPVS--LKVPVVAEAq 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      925 --YTVVSSHEQFtkYLNFSESEEKESHVAM--------HRYQVNNLGQRDLP-VSINFWVPVELnQEAVW----MDVEvs 989
Cdd:pfam08441  306 lsLSGVSKPDQV--VGGSVKGESAMKPRSEedigplveHTYEVINNGPSTVSgASLEISWPYEL-SNGKWllylLDVQ-- 380

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386831      990 lPQNPsLRCSSEKIAGP------------ASDFLAHIQKNP---------------VLDC-SIAGCLRFRC 1032
Cdd:pfam08441  381 -GQGK-GECSPQNEINPlnltqslesskpLRTSRVHHVVKRrdvlksekatqtasvLLSCdSGARCVVIRC 449
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 151-319 1.36e-28

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: 112.71  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQF-QRP-STQFSLMQFSNkfQTHLTFeEFRRTSNPLSLLASVHQLQ---GF 225
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLdIGPdGVRVGVVQYSD--DPRTEF-YLNTYRSKDDVLEAVKNLRyigGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    226 TYTATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLdyKDVIPMADaAGIIRYAIGVGLAFQNrnswkELNDIA 305
Cdd:cd01472   79 TNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVE--EPAVELKQ-AGIEVFAVGVKNADEE-----ELKQIA 150

                        170
                 ....*....|....
gi 386831    306 SKPSQEHIFKVEDF 319
Cdd:cd01472  151 SDPKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 151-319 1.37e-28

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: 112.77  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGFTYT 228
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    229 ATAIQNVVHRLFHASYGARRDATKILIVITDGKKEGDTLDYKDVipmADAAGIIRYAIGVGLAFQNrnswkELNDIASKP 308
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARV---LRNLGVNVFAVGVKDADES-----ELKMIASKP 153

                        170
                 ....*....|.
gi 386831    309 SQEHIFKVEDF 319
Cdd:cd01482  154 SETHVFNVADF 164
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 151-314 5.66e-27

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: 108.04  E-value: 5.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVH-QLQGFTY 227
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHAsygARRDATKILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIGVGLAFQNrnswKELNDIASK 307
Cdd:cd00198   82 IGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANE----DELKEIADK 154


                 ....*..
gi 386831    308 PSQEHIF 314
Cdd:cd00198  155 TTGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 151-333 2.32e-24

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: 102.85  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVIsQFQRPS---TQFSLMQFSNKFQTHLTFEEFRRTSNPLSLLASVHQLQGFTY 227
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQII-DSLDVGpdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    228 TATAIQNVVHRLFHASYGAR---RDATKILIVITDGKKEGDTldyKDVIPMADAAGIIRYAIGVGLAFQNrnswkELNDI 304
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDV---SEVAAKARALGIEMFAVGVGRADEE-----ELREI 154

                        170       180
                 ....*....|....*....|....*....
gi 386831    305 ASKPSQEHIFKVEDFDALKDIQTQLREKI 333
Cdd:cd01475  155 ASEPLADHVFYVEDFSTIEELTKKFQGKI 183
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 127-330 7.46e-14

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: 73.05  E-value: 7.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    127 FLLGPTQLTQRLPVSRQECPRQEQDIVFLIDGSGSISSRNfatMMNFVRAVISQF---QRPSTQFSLMQFSNKFQTHLTF 203
Cdd:COG1240   70 LAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAEN---RLEAAKGALLDFlddYRPRDRVGLVAFGGEAEVLLPL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    204 eefrrTSNPLSLLASVHQLQGFTYTAT--AIQNVVHRLFHASYGARrdatKILIVITDGKKEGDTLDYKDVIPMADAAGI 281
Cdd:COG1240  147 -----TRDREALKRALDELPPGGGTPLgdALALALELLKRADPARR----KVIVLLTDGRDNAGRIDPLEAAELAAAAGI 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 386831    282 IRYAIGVGLAFQNRnswKELNDIASKpSQEHIFKVEDFDALKDIQTQLR 330
Cdd:COG1240  218 RIYTIGVGTEAVDE---GLLREIAEA-TGGRYFRADDLSELAAIYREID 262
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 151-313 1.26e-13

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 70.49  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQRP--------STQFSLMQFSNkfQTHLTFEEFRRTSNPLSLLASVHQL 222
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpagSWRVGVVQYSD--QQEVEAGFLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    223 Q---GFTYTATAIQNVVHRLFHASYGARRdatKILIVITDGK--KEGDTLDyKDVIPMADAAGIIRYAIGVGlafqNRNS 297
Cdd:cd01480   82 EyigGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHsdGSPDGGI-EKAVNEADHLGIKIFFVAVG----SQNE 153

                        170
                 ....*....|....*.
gi 386831    298 WKeLNDIASKPSQEHI 313
Cdd:cd01480  154 EP-LSRIACDGKSALY 168
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 151-325 2.53e-13

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 69.46  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSrNFATMMNFVRAVISQFQRPSTQFSLMQFSNKFQTHLTFEEFRRTSNP-LSLLASVHQlQGFTYTA 229
Cdd:cd01474    6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP-SGQTYIH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    230 TAIQNVVHRLFHASYGARRDAtKILIVITDGKKEGDTLDYkdviPMADAA-----GIIRYAIGVgLAFqnrnSWKELNDI 304
Cdd:cd01474   84 EGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKY----PEHEAKlsrklGAIVYCVGV-TDF----LKSQLINI 153

                        170       180
                 ....*....|....*....|..
gi 386831    305 ASkpSQEHIFKVED-FDALKDI 325
Cdd:cd01474  154 AD--SKEYVFPVTSgFQALSGI 173
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 151-319 3.18e-13

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: 68.89  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEEFRRTSNplsLLASVHQLQGFT-- 226
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTKAD---VLGAVRRLRLRGgs 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    227 --YTATAIQNVVHRLFHASYGAR-RDAT-KILIVITDGKKEGDTLDYKDVIpmaDAAGIIRYAIGVGLAFQNrnswkELN 302
Cdd:cd01481   79 qlNTGSALDYVVKNLFTKSAGSRiEEGVpQFLVLITGGKSQDDVERPAVAL---KRAGIVPFAIGARNADLA-----ELQ 150

                        170
                 ....*....|....*..
gi 386831    303 DIASKPSqeHIFKVEDF 319
Cdd:cd01481  151 QIAFDPS--FVFQVSDF 165
VWA_2 pfam13519
von Willebrand factor type A domain;
152-257 9.26e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 59.61  E-value: 9.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      152 IVFLIDGSGSISSR-----NFATMMNFVRAVISqfQRPSTQFSLMQFSNKFQTHLTFeefrrTSNPLSLLASVHQLQ--- 223
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLK--SLPGDRVGLVTFGDGPEVLIPL-----TKDRAKILRALRRLEpkg 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 386831      224 GFTYTATAIQNVVHRLFHASYGARRdatkILIVI 257
Cdd:pfam13519   74 GGTNLAAALQLARAALKHRRKNQPR----RIVLI 103
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 6.29e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 386831       517 PWGRFGAALTVLGDVNGDKLTDVVIGAPGEEENR--GAVYLFHG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 151-314 8.36e-08

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: 53.17  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRnFATMMNFVRAVISQFQ--RPSTQFSLMQFSNKFQTHLTFEeFRRTSNPLSLLASVHQLQ---GF 225
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEigPTATRVALITYSGRGRQRVRFN-LPKHNDGEELLEKVDNLRfigGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    226 TYTATAIQnVVHRLFHASYGARRDATKILIVITDGKKegdtldYKDVIPMADAA----GIIRYAIGVG--LAFQNRnswk 299
Cdd:cd01476   80 TATGAAIE-VALQQLDPSEGRREGIPKVVVVLTDGRS------HDDPEKQARILravpNIETFAVGTGdpGTVDTE---- 148

                        170
                 ....*....|....*
gi 386831    300 ELNDIASkpSQEHIF 314
Cdd:cd01476  149 ELHSITG--NEDHIF 161
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 152-287 1.59e-07

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 54.24  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831      152 IVFLIDGSGSIS-SRNFAT--MMNFVRAVIsqfqRPSTQFSLMQFSNKFQTHLTFeefrrTSNPLSLLASVHQLQ--GFT 226
Cdd:TIGR03436   56 VGLVIDTSGSMRnDLDRARaaAIRFLKTVL----RPNDRVFVVTFNTRLRLLQDF-----TSDPRLLEAALNRLKppLRT 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386831      227 YTATAIQNVVHRLFHASYGARRDAT--------------KILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIG 287
Cdd:TIGR03436  127 DYNSSGAFVRDGGGTALYDAITLAAleqlanalagipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 2.49e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.89  E-value: 2.49e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 386831      521 FGAALTVlGDVNGDKLTDVVIGAPGE-EENRGAVYLF 556
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 127-289 1.44e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 51.22  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    127 FLLGPTQLTQRLPVSRQECPRQEQDIVFLIDGSGSISSrnfaTMMNFVRAVISQF---QRPSTQFSLMQFSNKFQTHLTF 203
Cdd:COG2425   96 ALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAG----SKEAAAKAAALALlraLRPNRRFGVILFDTEVVEDLPL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    204 EEFRRTSNPLSLLASVhQLQGFTYTATAIQNVVHRLfhasyGARRDATKILIVITDGKkegDTLDYKDVIPMADA--AGI 281
Cdd:COG2425  172 TADDGLEDAIEFLSGL-FAGGGTDIAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLREVRAkeSGV 242


                 ....*...
gi 386831    282 IRYAIGVG 289
Cdd:COG2425  243 RLFTVAIG 250
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 151-289 1.57e-06

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 49.69  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRN-FATMMNFVRAVISQF--QRPSTQFSLMQFSNKFQTHLTFEEFRRTsNPLSLLASVHQLQ---- 223
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSPNST-NKDLALNAIRALLslyy 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386831    224 --GFTYTATAIQNVVHRLFHASyGARRDATKILIVITDGKKEGDTLDYKDVIPMADAAGIIrYAIGVG 289
Cdd:cd01471   81 pnGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVII-AVLGVG 146
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-504 3.20e-06

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.44  E-value: 3.20e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386831       454 IGSYFGPSLCSV-DVDSDGSTDLVlIGPPHYYEQTRGAQVSVCPLPRGWRRW 504
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNS 51
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 151-289 1.06e-05

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 47.32  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFA--TMMNFVRAVISQF--QRPSTQFSLMQFSNKFQTHLTFeefrrTSNPLSLLASVHQLQGF- 225
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVkpSRLEAAKEVLSDFidRRENDRIGLVVFAGAAFTQAPL-----TLDRESLKELLEDIKIGl 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386831    226 ----TYTATAIQNVVHRLFHASYGARrdatkILIVITDGKKEGDTLDYKDVIPMADAAGIIRYAIGVG 289
Cdd:cd01467   79 agqgTAIGDAIGLAIKRLKNSEAKER-----VIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVG 141
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
151-289 3.62e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.07  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFQ-----RPSTQFSLMQFSNKFQTHLtfeefrrtsnPLSLLASVH--QL- 222
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRqdpyaLETVEVSVITFDGEAKVLL----------PLTDLEDFQppDLs 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    223 --------QGFTYTATAIQNVVHRLFHASYGARRdatKILIVITDGKkegDT-LDYKDVIPMADAA----GIIRYAIGVG 289
Cdd:COG4245   77 asggtplgAALELLLDLIERRVQKYTAEGKGDWR---PVVFLITDGE---PTdSDWEAALQRLKDGeaakKANIFAIGVG 150
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 151-324 4.15e-05

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 45.74  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVI---SQFQRpSTQFSLMQFSNKFQTHLTFEEFrRTSNPLSLLASVHQLQ---- 223
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEAKNAIKTLIekiSSYEV-SPRYEIISYASDPKEIVSIRDF-NSNDADDVIKRLEDFNyddh 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    224 ----GfTYTATAIQNVVHRLFHASYGARRDATKI---LIVITDGKKE--GDTL----DYKDVIPMADAAGIIR------Y 284
Cdd:cd01470   80 gdktG-TNTAAALKKVYERMALEKVRNKEAFNETrhvIILFTDGKSNmgGSPLptvdKIKNLVYKNNKSDNPRedyldvY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 386831    285 AIGVGlafQNRNsWKELNDIAS-KPSQEHIFKVEDFDALKD 324
Cdd:cd01470  159 VFGVG---DDVN-KEELNDLASkKDNERHFFKLKDYEDLQE 195
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 151-307 4.27e-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: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    151 DIVFLIDGSGSISSRNFATMMNFVRAVISQFqRPSTQFSLMQFSNKFQTHLtfeEFRRTSNPLSLLASVHQLQ--GFTYT 228
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLL---PPTPATDRAKILAAIDRLQagGGTAL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    229 ATAIQNVVHrlfHASYGARRDATKILIVITDGK---KEGDTLDYKDVIPMADAAGIIRYAIGVGLAFqNRNswkELNDIA 305
Cdd:COG2304  169 GAGLELAYE---LARKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDY-NED---LLERLA 241


                 ..
gi 386831    306 SK 307
Cdd:COG2304  242 DA 243
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 7.28e-05

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 40.56  E-value: 7.28e-05
                           10
                   ....*....|....*
gi 386831     1129 KVGFFKRQYKEMMEE 1143
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 152-289 4.83e-04

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 42.31  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386831    152 IVFLIDGSGSISSRNFATMMNFVRAVISQF-QRPSTQFSLMQFSNKFQTH--------LTFEEFRRtSNPLSLLASVhQL 222
Cdd:cd01454    3 VTLLLDLSGSMRSDRRIDVAKKAAVLLAEAlEACGVPHAILGFTTDAGGRervrwikiKDFDESLH-ERARKRLAAL-SP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386831    223 QGFTYTATAIQNVVHRLfhasyGARRDATKILIVITDGK---------KEGDTLDYKDVIPMADAAGIIRYAIGVG 289
Cdd:cd01454   81 GGNTRDGAAIRHAAERL-----LARPEKRKILLVISDGEpndldyyegNVFATEDALRAVIEARKLGIEVFGITID 151
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-628 1.32e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.32e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 386831       582 QYFGQALSGGQDLTQDGLVDLAVGA--------RGQVLLLRTRPVLWVGVSMQFI 628
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 458-494 6.87e-03

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 35.18  E-value: 6.87e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 386831      458 FGPSLCSVDVDSDGSTDLVlIGPPHYYEQTRGAqVSV 494
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGAGAGA-VYV 35
 
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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