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Conserved domains on  [gi|48428495|sp|Q9QXH4|]
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RecName: Full=Integrin alpha-X; AltName: Full=CD11 antigen-like family member C; AltName: Full=Leukocyte adhesion glycoprotein p150,95 alpha chain; AltName: Full=Leukocyte adhesion receptor p150,95; AltName: CD_antigen=CD11c; Flags: Precursor

Protein Classification

vWA_integrins_alpha_subunit and Int_alpha domain-containing protein( domain architecture ID 11546373)

protein containing domains vWA_integrins_alpha_subunit, Int_alpha, Integrin_alpha2, and Integrin_alpha

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 ...
 151-326 3.70e-73

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: 240.34  E-value: 3.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  151 QDIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQR--PSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQLRGYTY 228
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSYDsVIPMAEAASIIRYAIGVGKAFYNEHSKQELKAIASM 308
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKD-VIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 48428495  309 PSHEYVFSVENFDALKDI 326
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 ...
 617-1041 2.73e-36

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: 143.62  E-value: 2.73e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    617 RPILRVSPTVHFTPAEISRSVFECQEQVAPeQTLSDATVCLHIHESPKTQlGDLRSTVTFDL-ALDHGRLSTRAIFKETK 695
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTGKPIPN-PSLVLNYELELdRQKKKGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    696 TRALTRVKTLGLN--KHCESVKLLLPACVEDSVTPITLRLNFSLVGVPI--SSLQNLQPMLAVDDQTYFTASLPFEKNCG 771
Cdd:pfam08441   79 QPSLTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    772 ADHICQDDL--SVVFGFPDL-KTLVVGSDLELNVDVTVSNDGEDSYGTTVTLFYPVGLSFRRVaegqvfLRKKEDQQwqr 848
Cdd:pfam08441  159 EDNVCVPDLqlSAKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ--- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    849 rgqhslhLMCDSTpdrsqglwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRL--LLRARVGSENNVPGTP 920
Cdd:pfam08441  230 -------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELsfDLQIRSTNEQNSNSNP 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    921 KTtfqLELPVKYAVYTMIS--SH-DQ-FTKYLNFSTSEKEKT-----SVVEHRFQVNNLGQRDVP-VSINFWVPIELKGE 990
Cdd:pfam08441  294 VS---LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELSNG 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    991 aVW----TVMVSH------PQNPLTQC--------------YRNRLKPTQFDLLTHMQKSP----VLDC-SIADCLHLRC 1041
Cdd:pfam08441  371 -KWllylLDVQGQgkgecsPQNEINPLnltqslesskplrtSRVHHVVKRRDVLKSEKATQtasvLLSCdSGARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 518-573 1.18e-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: 57.77  E-value: 1.18e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 48428495     518 PWGRFGAALTVLGDVNGDSLADVAIGAPGEEENR--GAVYIFHGaSRQDIAPSPSQRI 573
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-505 2.28e-09

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: 54.30  E-value: 2.28e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 48428495     455 IGSYFGASLCSV-DMDRDGSTDLVlIGVPHYYEHTRGGQVSVCPMPGVGSRW 505
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNS 51
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1138-1152 1.99e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.99e-03
                           10
                   ....*....|....*
gi 48428495   1138 KAGFFKRQYKEMLEE 1152
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
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 ...
 151-326 3.70e-73

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: 240.34  E-value: 3.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  151 QDIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQR--PSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQLRGYTY 228
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSYDsVIPMAEAASIIRYAIGVGKAFYNEHSKQELKAIASM 308
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKD-VIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 48428495  309 PSHEYVFSVENFDALKDI 326
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
152-329 9.60e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.39  E-value: 9.60e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQL-RGYTY 228
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSydSVIPMAEAASIIRYAIGVGKAFYNehskqELKAIASM 308
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPE--EVARELKSAGVTVFAVGVGNADDE-----ELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 48428495    309 PSHEYVFSVENFDALKDIENQ 329
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 152-326 2.32e-42

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: 152.61  E-value: 2.32e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495     152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQR--PSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVR-QLRGYTY 228
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495     229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGkafyNEHSKQELKAIASM 308
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASA 156

                           170
                    ....*....|....*...
gi 48428495     309 PSHEYVFSVENFDALKDI 326
Cdd:smart00327  157 PGGVYVFLPELLDLLIDL 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 617-1041 2.73e-36

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: 143.62  E-value: 2.73e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    617 RPILRVSPTVHFTPAEISRSVFECQEQVAPeQTLSDATVCLHIHESPKTQlGDLRSTVTFDL-ALDHGRLSTRAIFKETK 695
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTGKPIPN-PSLVLNYELELdRQKKKGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    696 TRALTRVKTLGLN--KHCESVKLLLPACVEDSVTPITLRLNFSLVGVPI--SSLQNLQPMLAVDDQTYFTASLPFEKNCG 771
Cdd:pfam08441   79 QPSLTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    772 ADHICQDDL--SVVFGFPDL-KTLVVGSDLELNVDVTVSNDGEDSYGTTVTLFYPVGLSFRRVaegqvfLRKKEDQQwqr 848
Cdd:pfam08441  159 EDNVCVPDLqlSAKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ--- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    849 rgqhslhLMCDSTpdrsqglwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRL--LLRARVGSENNVPGTP 920
Cdd:pfam08441  230 -------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELsfDLQIRSTNEQNSNSNP 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    921 KTtfqLELPVKYAVYTMIS--SH-DQ-FTKYLNFSTSEKEKT-----SVVEHRFQVNNLGQRDVP-VSINFWVPIELKGE 990
Cdd:pfam08441  294 VS---LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELSNG 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    991 aVW----TVMVSH------PQNPLTQC--------------YRNRLKPTQFDLLTHMQKSP----VLDC-SIADCLHLRC 1041
Cdd:pfam08441  371 -KWllylLDVQGQgkgecsPQNEINPLnltqslesskplrtSRVHHVVKRRDVLKSEKATQtasvLLSCdSGARCVVIRC 449
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 147-326 3.59e-15

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: 76.90  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  147 PKQDQDIVFLIDGSGSISSTDfeKMlDFVKAVMSQL---QRPSTRFSLMQFSDYFRVHFTFnnfisTSSPLSLLGSVRQL 223
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAEN--RL-EAAKGALLDFlddYRPRDRVGLVAFGGEAEVLLPL-----TRDREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  224 R--GYTYTASAIKHVITELfttqSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGKAFYNEhskQE 301
Cdd:COG1240  161 PpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDE---GL 233

                        170       180
                 ....*....|....*....|....*
gi 48428495  302 LKAIASMPSHEYvFSVENFDALKDI 326
Cdd:COG1240  234 LREIAEATGGRY-FRADDLSELAAI 257
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 518-573 1.18e-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: 57.77  E-value: 1.18e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 48428495     518 PWGRFGAALTVLGDVNGDSLADVAIGAPGEEENR--GAVYIFHGaSRQDIAPSPSQRI 573
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-505 2.28e-09

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: 54.30  E-value: 2.28e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 48428495     455 IGSYFGASLCSV-DMDRDGSTDLVlIGVPHYYEHTRGGQVSVCPMPGVGSRW 505
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNS 51
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 522-557 3.02e-08

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: 50.59  E-value: 3.02e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 48428495    522 FGAALTVlGDVNGDSLADVAIGAPGE-EENRGAVYIF 557
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 153-288 7.99e-08

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: 55.39  E-value: 7.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    153 IVFLIDGSGSIS-STDFEK--MLDFVKAVMsqlqRPSTRFSLMQFSDYFRVHFTFnnfisTSSPLSLLGSVRQLR----- 224
Cdd:TIGR03436   56 VGLVIDTSGSMRnDLDRARaaAIRFLKTVL----RPNDRVFVVTFNTRLRLLQDF-----TSDPRLLEAALNRLKpplrt 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    225 ------------GYTYTASAIKhviteLFTTQSGARQDAT----KVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIG 288
Cdd:TIGR03436  127 dynssgafvrdgGGTALYDAIT-----LAALEQLANALAGipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 459-495 1.04e-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: 37.49  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 48428495    459 FGASLCSVDMDRDGSTDLVlIGVPHYYEhTRGGQVSV 495
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGG-AGAGAVYV 35
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1138-1152 1.99e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.99e-03
                           10
                   ....*....|....*
gi 48428495   1138 KAGFFKRQYKEMLEE 1152
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
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 ...
 151-326 3.70e-73

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: 240.34  E-value: 3.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  151 QDIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQR--PSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQLRGYTY 228
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSYDsVIPMAEAASIIRYAIGVGKAFYNEHSKQELKAIASM 308
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKD-VIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 48428495  309 PSHEYVFSVENFDALKDI 326
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
152-329 9.60e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.39  E-value: 9.60e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQL-RGYTY 228
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSydSVIPMAEAASIIRYAIGVGKAFYNehskqELKAIASM 308
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPE--EVARELKSAGVTVFAVGVGNADDE-----ELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 48428495    309 PSHEYVFSVENFDALKDIENQ 329
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 152-326 2.32e-42

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: 152.61  E-value: 2.32e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495     152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQR--PSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVR-QLRGYTY 228
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495     229 TASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGkafyNEHSKQELKAIASM 308
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASA 156

                           170
                    ....*....|....*...
gi 48428495     309 PSHEYVFSVENFDALKDI 326
Cdd:smart00327  157 PGGVYVFLPELLDLLIDL 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 617-1041 2.73e-36

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: 143.62  E-value: 2.73e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    617 RPILRVSPTVHFTPAEISRSVFECQEQVAPeQTLSDATVCLHIHESPKTQlGDLRSTVTFDL-ALDHGRLSTRAIFKETK 695
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP-VSCFTVRACFSYTGKPIPN-PSLVLNYELELdRQKKKGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    696 TRALTRVKTLGLN--KHCESVKLLLPACVEDSVTPITLRLNFSLVGVPI--SSLQNLQPMLAVDDQTYFTASLPFEKNCG 771
Cdd:pfam08441   79 QPSLTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    772 ADHICQDDL--SVVFGFPDL-KTLVVGSDLELNVDVTVSNDGEDSYGTTVTLFYPVGLSFRRVaegqvfLRKKEDQQwqr 848
Cdd:pfam08441  159 EDNVCVPDLqlSAKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ--- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    849 rgqhslhLMCDSTpdrsqglwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRL--LLRARVGSENNVPGTP 920
Cdd:pfam08441  230 -------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELsfDLQIRSTNEQNSNSNP 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    921 KTtfqLELPVKYAVYTMIS--SH-DQ-FTKYLNFSTSEKEKT-----SVVEHRFQVNNLGQRDVP-VSINFWVPIELKGE 990
Cdd:pfam08441  294 VS---LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELSNG 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    991 aVW----TVMVSH------PQNPLTQC--------------YRNRLKPTQFDLLTHMQKSP----VLDC-SIADCLHLRC 1041
Cdd:pfam08441  371 -KWllylLDVQGQgkgecsPQNEINPLnltqslesskplrtSRVHHVVKRRDVLKSEKATQtasvLLSCdSGARCVVIRC 449
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 152-320 1.97e-35

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: 132.41  E-value: 1.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFistSSPLSLLGSVRQLR---GY 226
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAY---TSKEDVLAAIKNLPykgGN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  227 TYTASAIKHVITELFTTQSGARQDATKVLIVITDGRKQGDnlsydsvipMAEAASIIR------YAIGVGKAFYNehskq 300
Cdd:cd01482   79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDD---------VELPARVLRnlgvnvFAVGVKDADES----- 144

                        170       180
                 ....*....|....*....|
gi 48428495  301 ELKAIASMPSHEYVFSVENF 320
Cdd:cd01482  145 ELKMIASKPSETHVFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 152-315 3.14e-35

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: 131.64  E-value: 3.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQRP--STRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQLRG-YTY 228
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  229 TASAIKHVITELFtTQSGARQDATKVLIVITDGRKQGDnlsyDSVIPMAEAA---SIIRYAIGVGKAfynehSKQELKAI 305
Cdd:cd01450   82 TGKALQYALEQLF-SESNARENVPKVIIVLTDGRSDDG----GDPKEAAAKLkdeGIKVFVVGVGPA-----DEEELREI 151

                        170
                 ....*....|
gi 48428495  306 ASMPSHEYVF 315
Cdd:cd01450  152 ASCPSERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 152-320 1.99e-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: 129.66  E-value: 1.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQL-QRP-STRFSLMQFSDYFRVHFTFNNFistSSPLSLLGSVRQLR---GY 226
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLdIGPdGVRVGVVQYSDDPRTEFYLNTY---RSKDDVLEAVKNLRyigGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  227 TYTASAIKHVITELFTTQSGARQDATKVLIVITDGRkqgdnlSYDSVIPMAEA---ASIIRYAIGVGKAfynehSKQELK 303
Cdd:cd01472   79 TNTGKALKYVRENLFTEASGSREGVPKVLVVITDGK------SQDDVEEPAVElkqAGIEVFAVGVKNA-----DEEELK 147

                        170
                 ....*....|....*..
gi 48428495  304 AIASMPSHEYVFSVENF 320
Cdd:cd01472  148 QIASDPKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 152-334 2.18e-29

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: 117.10  E-value: 2.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLLGSVRQLRGYTYT 229
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDvgPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  230 ASAIKHVITELFTTQSGAR---QDATKVLIVITDGRKQgDNLSydSVIPMAEAASIIRYAIGVGKAfynehSKQELKAIA 306
Cdd:cd01475   84 GLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQ-DDVS--EVAAKARALGIEMFAVGVGRA-----DEEELREIA 155

                        170       180
                 ....*....|....*....|....*...
gi 48428495  307 SMPSHEYVFSVENFDALKDIENQLKEKI 334
Cdd:cd01475  156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 152-315 3.83e-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: 108.81  E-value: 3.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFISTSSPLSLL-GSVRQLRGYTY 228
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIdALKKGLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  229 TASAIKHVITELFttqSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGKAFYNEhskqELKAIASM 308
Cdd:cd00198   82 IGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANED----ELKEIADK 154


                 ....*..
gi 48428495  309 PSHEYVF 315
Cdd:cd00198  155 TTGGAVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 152-320 6.36e-20

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: 88.15  E-value: 6.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNnfiSTSSPLSLLGSVRQLR---GY 226
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLN---THSTKADVLGAVRRLRlrgGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  227 -TYTASAIKHVITELFTTQSGAR--QDATKVLIVITDGRKQgDNLSYDSVIpmAEAASIIRYAIGVGKAfynehSKQELK 303
Cdd:cd01481   79 qLNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQ-DDVERPAVA--LKRAGIVPFAIGARNA-----DLAELQ 150

                        170
                 ....*....|....*..
gi 48428495  304 AIASMPSheYVFSVENF 320
Cdd:cd01481  151 QIAFDPS--FVFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 152-311 2.10e-16

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 77.82  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTdFEKMLDFVKAVMSQLQ--RPSTRFSLMQFSDYFR--VHFTFNNFISTSSPLSLLGSVRQLRGYT 227
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEigPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  228 YTASAIKhVITELFTTQSGARQDATKVLIVITDGRkqgdnlSYDSVIPMAEAA----SIIRYAIGVGkaFYNEHSKQELK 303
Cdd:cd01476   81 ATGAAIE-VALQQLDPSEGRREGIPKVVVVLTDGR------SHDDPEKQARILravpNIETFAVGTG--DPGTVDTEELH 151


                 ....*...
gi 48428495  304 AIASMPSH 311
Cdd:cd01476  152 SITGNEDH 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 147-326 3.59e-15

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: 76.90  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  147 PKQDQDIVFLIDGSGSISSTDfeKMlDFVKAVMSQL---QRPSTRFSLMQFSDYFRVHFTFnnfisTSSPLSLLGSVRQL 223
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAEN--RL-EAAKGALLDFlddYRPRDRVGLVAFGGEAEVLLPL-----TRDREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  224 R--GYTYTASAIKHVITELfttqSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGKAFYNEhskQE 301
Cdd:COG1240  161 PpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDE---GL 233

                        170       180
                 ....*....|....*....|....*
gi 48428495  302 LKAIASMPSHEYvFSVENFDALKDI 326
Cdd:COG1240  234 LREIAEATGGRY-FRADDLSELAAI 257
VWA_2 pfam13519
von Willebrand factor type A domain;
153-258 6.30e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 68.86  E-value: 6.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    153 IVFLIDGSGSISSTD-----FEKMLDFVKAVMSQLqrPSTRFSLMQFSDYFRVHFTFNNfiSTSSPLSLLGSVRQLRGYT 227
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSL--PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 48428495    228 YTASAIKHVITELFTTQSGARqdatKVLIVI 258
Cdd:pfam13519   77 NLAAALQLARAALKHRRKNQP----RRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 152-265 3.25e-13

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 69.34  E-value: 3.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQRP--------STRFSLMQFSDYFRVHFTFNNFISTSSPL-SLLGSVRQ 222
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpagSWRVGVVQYSDQQEVEAGFLRDIRNYTSLkEAVDNLEY 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 48428495  223 LRGYTYTASAIKHVITELfttQSGARQDATKVLIVITDGRKQG 265
Cdd:cd01480   84 IGGGTFTDCALKYATEQL---LEGSHQKENKFLLVITDGHSDG 123
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 152-333 3.24e-12

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 66.38  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEkMLDFVKAVMSQLQRPSTRFSLMQFSDYFRVHFTFNNFIST-SSPLSLLGSVRQlRGYTYTA 230
Cdd:cd01474    6 DLYFVLDKSGSVAANWIE-IYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTP-SGQTYIH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  231 SAIKHVITELFTTQSGARQDAtKVLIVITDGRKQGDNLSYdsviPMAEAA-----SIIRYAIGVgKAFynehSKQELKAI 305
Cdd:cd01474   84 EGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKY----PEHEAKlsrklGAIVYCVGV-TDF----LKSQLINI 153

                        170       180
                 ....*....|....*....|....*....
gi 48428495  306 ASmpSHEYVFSV-ENFDALKDIENQLKEK 333
Cdd:cd01474  154 AD--SKEYVFPVtSGFQALSGIIESVVKK 180
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 518-573 1.18e-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: 57.77  E-value: 1.18e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 48428495     518 PWGRFGAALTVLGDVNGDSLADVAIGAPGEEENR--GAVYIFHGaSRQDIAPSPSQRI 573
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 152-290 5.83e-10

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: 59.71  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSIS-STDFEKMLDFVKAVMSQL--QRPSTRFSLMQFSDYFRVHFTFNNFISTS--SPLSLLGSVRQL--- 223
Cdd:cd01471    2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSPNSTNkdLALNAIRALLSLyyp 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48428495  224 RGYTYTASAIKHVITELFTTQsGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAASIIrYAIGVG 290
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVII-AVLGVG 146
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-505 2.28e-09

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: 54.30  E-value: 2.28e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 48428495     455 IGSYFGASLCSV-DMDRDGSTDLVlIGVPHYYEHTRGGQVSVCPMPGVGSRW 505
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 ...
 152-291 8.77e-09

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: 56.18  E-value: 8.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKM--LDFVKAVMSQL--QRPSTRFSLMQFSD--YFRVHFT-----FNNFISTSSPLsLLGSv 220
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFidRRENDRIGLVVFAGaaFTQAPLTldresLKELLEDIKIG-LAGQ- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48428495  221 rqlrgYTYTASAIKHVITELftTQSGARQdatKVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIGVGK 291
Cdd:cd01467   82 -----GTAIGDAIGLAIKRL--KNSEAKE---RVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGK 142
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 522-557 3.02e-08

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: 50.59  E-value: 3.02e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 48428495    522 FGAALTVlGDVNGDSLADVAIGAPGE-EENRGAVYIF 557
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 140-306 5.88e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 55.46  E-value: 5.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  140 PTAQQECPKQDQDIVFLIDGSGSISSTdfekMLDFVKAVMSQL---QRPSTRFSLMQFSDYFRVHFTFNNFISTSSPLSL 216
Cdd:COG2425  108 APASAAVPLLEGPVVLCVDTSGSMAGS----KEAAAKAAALALlraLRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEF 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  217 LGSVrQLRGYTYTASAIKHVITELfttqsGARQDATKVLIVITDGrkQGDNLSYDSVIPMAEAASIIR-YAIGVGkafyN 295
Cdd:COG2425  184 LSGL-FAGGGTDIAPALRAALELL-----EEPDYRNADIVLITDG--EAGVSPEELLREVRAKESGVRlFTVAIG----D 251

                        170
                 ....*....|.
gi 48428495  296 EHSKQELKAIA 306
Cdd:COG2425  252 AGNPGLLEALA 262
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 153-288 7.99e-08

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: 55.39  E-value: 7.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    153 IVFLIDGSGSIS-STDFEK--MLDFVKAVMsqlqRPSTRFSLMQFSDYFRVHFTFnnfisTSSPLSLLGSVRQLR----- 224
Cdd:TIGR03436   56 VGLVIDTSGSMRnDLDRARaaAIRFLKTVL----RPNDRVFVVTFNTRLRLLQDF-----TSDPRLLEAALNRLKpplrt 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495    225 ------------GYTYTASAIKhviteLFTTQSGARQDAT----KVLIVITDGRKQGDNLSYDSVIPMAEAASIIRYAIG 288
Cdd:TIGR03436  127 dynssgafvrdgGGTALYDAIT-----LAALEQLANALAGipgrKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 152-306 2.04e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 50.87  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEKMLDFVKAVMSQLqRPSTRFSLMQFSDYFRVHFTfnnFISTSSPLSLLGSVRQLR--GYTYT 229
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLLP---PTPATDRAKILAAIDRLQagGGTAL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  230 ASAIKHVITELfttQSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAAS---IIRYAIGVGKAfYNEhskQELKAIA 306
Cdd:COG2304  169 GAGLELAYELA---RKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAReegITLTTLGVGSD-YNE---DLLERLA 241
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 152-334 1.12e-05

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 47.31  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEK-MLDFVKAVMSQLQ--RPSTRFSLMQFSDYFRVHFTFNNFISTSSPlSLLGSVRQLR---- 224
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNisKDKVHVGILLFAEKNRDVVPFSDEERYDKN-ELLKKINDLKnsyr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  225 --GYTYTASAIKHVITElFTTQSGARQDATKVLIVITDGrkqGDNLSYDSVIPmaEAASIIR------YAIGVGKAfyne 296
Cdd:cd01473   81 sgGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDG---NDTSASKKELQ--DISLLYKeenvklLVVGVGAA---- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 48428495  297 hSKQELKAIA--SMPSHEYVFSVE-NFDALKDIENQLKEKI 334
Cdd:cd01473  151 -SENKLKLLAgcDINNDNCPNVIKtEWNNLNGISKFLTDKI 190
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
147-326 2.15e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 43.76  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  147 PKQDQDIVFLIDGSGSISSTDFEKMLDFVKAVMSQLQ-----RPSTRFSLMqfsdyfrvhfTFNNFISTSSPLSLLGSVR 221
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRqdpyaLETVEVSVI----------TFDGEAKVLLPLTDLEDFQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  222 ----QLRGYTYTASAIKHVITEL-----FTTQSGARQDATkVLIVITDGRKQGdnLSYDSVIPMAEAAS----IIRYAIG 288
Cdd:COG4245   72 ppdlSASGGTPLGAALELLLDLIerrvqKYTAEGKGDWRP-VVFLITDGEPTD--SDWEAALQRLKDGEaakkANIFAIG 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 48428495  289 VGkAFYNEhskQELKAIAsmpSHEYVFSVENFDALKDI 326
Cdd:COG4245  149 VG-PDADT---EVLKQLT---DPVRALDALDGLDFREF 179
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 153-297 4.81e-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: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  153 IVFLIDGSGSISST---DFEKMLdfVKAVMSQLQRPSTRFSLMQF-SDYFRVHFT-------FNNFISTSSPLSLLGSVR 221
Cdd:cd01454    3 VTLLLDLSGSMRSDrriDVAKKA--AVLLAEALEACGVPHAILGFtTDAGGRERVrwikikdFDESLHERARKRLAALSP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48428495  222 QlrGYTYTASAIKHVITELfttqsGARQDATKVLIVITDGrkQGDNLSYDSVIPMA--EAASIIRYAIGVGKAFYNEH 297
Cdd:cd01454   81 G--GNTRDGAAIRHAAERL-----LARPEKRKILLVISDG--EPNDLDYYEGNVFAteDALRAVIEARKLGIEVFGIT 149
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 459-495 1.04e-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: 37.49  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 48428495    459 FGASLCSVDMDRDGSTDLVlIGVPHYYEhTRGGQVSV 495
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGG-AGAGAVYV 35
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1138-1152 1.99e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.99e-03
                           10
                   ....*....|....*
gi 48428495   1138 KAGFFKRQYKEMLEE 1152
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 154-324 2.06e-03

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 40.33  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  154 VFLIDGSGSISSTDFEKMLDFVKAVMSQLqRPSTRFSLMQFSDYFRVhftfnnfISTSSPLS----LLGSVRQLR--GYT 227
Cdd:cd01465    4 VFVIDRSGSMDGPKLPLVKSALKLLVDQL-RPDDRLAIVTYDGAAET-------VLPATPVRdkaaILAAIDRLTagGST 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  228 YTASAIKHVITELfttQSGARQDATKVLIVITDGRKQGDNLSYDSVIPMAEAAS---IIRYAIGVGKAfYNEHsKQELKA 304
Cdd:cd01465   76 AGGAGIQLGYQEA---QKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKResgITLSTLGFGDN-YNED-LMEAIA 150

                        170       180
                 ....*....|....*....|
gi 48428495  305 IASMPSHEYVFSVEnfDALK 324
Cdd:cd01465  151 DAGNGNTAYIDNLA--EARK 168
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 152-325 7.73e-03

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: 39.19  E-value: 7.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  152 DIVFLIDGSGSISSTDFEK----MLDFVKAVMSQLQRPstRFSLMQFSDYFRVHFTFNNFIStSSPLSLLGSVRQL---- 223
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEaknaIKTLIEKISSYEVSP--RYEIISYASDPKEIVSIRDFNS-NDADDVIKRLEDFnydd 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428495  224 ----RGyTYTASAIKHVITELFTTQSGARQDATK---VLIVITDGRKQ--GDNLSY----DSVIPMAEAASIIR------ 284
Cdd:cd01470   79 hgdkTG-TNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDGKSNmgGSPLPTvdkiKNLVYKNNKSDNPRedyldv 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 48428495  285 YAIGVGKAFYnehsKQELKAIASMPSHE-YVFSVENFDALKD 325
Cdd:cd01470  158 YVFGVGDDVN----KEELNDLASKKDNErHFFKLKDYEDLQE 195
 
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.
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