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Conserved domains on  [gi|930588920|ref|NP_001300970|]
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integrin alpha-5 isoform 2 [Mus musculus]

Protein Classification

integrin alpha( domain architecture ID 12192630)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
169-597 0e+00

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: 553.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  169 RPIISASASLTIFPSMFNPEERSCSLEGNPVSCINLSFCLNASGKHVPN-SIGFEVELQLDWQKQKGGVRRALFLTSKQA 247
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIPNpSLVLNYELELDRQKKKGLPPRVLFLDSQQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  248 TLTQTLLIQNGAREDCREMKIYLRNEseFRDKLSPIHIALNFSL--DPKAPMDSHGLRPVLHYQSKSRIEDKAQILLDCG 325
Cdd:pfam08441  81 SLTGTLVLLSQGRKVCRTTKAYLRDE--FRDKLSPIVISLNYSLrvDPRAPSDLPGLKPILDQNQPSTVQEQANFLKDCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  326 EDNICVPDLQLDVYGE----KKHVYLGDKNALNLTFHAQNLGEGgAYEAELRVTAPLEAEYSGlVRHPGNFSSLSCDYFA 401
Cdd:pfam08441 159 EDNVCVPDLQLSAKFDsresDEPLLLGDDNDLALEITVTNLGED-AYEAELYVTLPPGLDYSG-VRREGSEKQLSCTAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  402 VNQSRQLVCDLGNPMK----LWGGLRFTVPHLQDTKKTIQFDFQILSKNLNNSQSNVVSFPLSVEAQAQVSLNGVSKPEA 477
Cdd:pfam08441 237 ENSTRQVVCDLGNPMKrgtqVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVSLKVPVVAEAQLSLSGVSKPDQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  478 VIFPVSDWNPQDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQAL-EGQQLLYVTKVTGLS--NCTSNYTPNSQ 554
Cdd:pfam08441 317 VVGGSVKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELsNGKWLLYLLDVQGQGkgECSPQNEINPL 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 930588920  555 GLELDPETS-------PHHLQKREAPGRS--STASGTQVLKCPE-AKCFRLRC 597
Cdd:pfam08441 397 NLTQSLESSkplrtsrVHHVVKRRDVLKSekATQTASVLLSCDSgARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
68-122 1.82e-15

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: 70.87  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 930588920    68 FSRFGSSLTPLGDLDQDGYNDVAIGAPFGGEAQ-QGVVFIFPGGPGGLSTKPSQVL 122
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGeTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
1-58 8.76e-13

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: 63.55  E-value: 8.76e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 930588920     1 MASYFGYAVA-ATDTNGDGLDDLLVGAPLlmertaDGRPQEVGRVYIYLQRPAGIDPTP 58
Cdd:smart00191   1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPR------ANDAGETGAVYVYFGSSGGGNSIP 53
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
134-186 6.69e-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: 43.90  E-value: 6.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 930588920   134 FFGSALRGGRDLDGNGYPDLIVGSFGVDKALVYRGRPIISASASLTIFPSMFN 186
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQN 56
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
169-597 0e+00

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: 553.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  169 RPIISASASLTIFPSMFNPEERSCSLEGNPVSCINLSFCLNASGKHVPN-SIGFEVELQLDWQKQKGGVRRALFLTSKQA 247
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIPNpSLVLNYELELDRQKKKGLPPRVLFLDSQQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  248 TLTQTLLIQNGAREDCREMKIYLRNEseFRDKLSPIHIALNFSL--DPKAPMDSHGLRPVLHYQSKSRIEDKAQILLDCG 325
Cdd:pfam08441  81 SLTGTLVLLSQGRKVCRTTKAYLRDE--FRDKLSPIVISLNYSLrvDPRAPSDLPGLKPILDQNQPSTVQEQANFLKDCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  326 EDNICVPDLQLDVYGE----KKHVYLGDKNALNLTFHAQNLGEGgAYEAELRVTAPLEAEYSGlVRHPGNFSSLSCDYFA 401
Cdd:pfam08441 159 EDNVCVPDLQLSAKFDsresDEPLLLGDDNDLALEITVTNLGED-AYEAELYVTLPPGLDYSG-VRREGSEKQLSCTAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  402 VNQSRQLVCDLGNPMK----LWGGLRFTVPHLQDTKKTIQFDFQILSKNLNNSQSNVVSFPLSVEAQAQVSLNGVSKPEA 477
Cdd:pfam08441 237 ENSTRQVVCDLGNPMKrgtqVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVSLKVPVVAEAQLSLSGVSKPDQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  478 VIFPVSDWNPQDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQAL-EGQQLLYVTKVTGLS--NCTSNYTPNSQ 554
Cdd:pfam08441 317 VVGGSVKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELsNGKWLLYLLDVQGQGkgECSPQNEINPL 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 930588920  555 GLELDPETS-------PHHLQKREAPGRS--STASGTQVLKCPE-AKCFRLRC 597
Cdd:pfam08441 397 NLTQSLESSkplrtsrVHHVVKRRDVLKSekATQTASVLLSCDSgARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
68-122 1.82e-15

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: 70.87  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 930588920    68 FSRFGSSLTPLGDLDQDGYNDVAIGAPFGGEAQ-QGVVFIFPGGPGGLSTKPSQVL 122
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGeTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
1-58 8.76e-13

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: 63.55  E-value: 8.76e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 930588920     1 MASYFGYAVA-ATDTNGDGLDDLLVGAPLlmertaDGRPQEVGRVYIYLQRPAGIDPTP 58
Cdd:smart00191   1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPR------ANDAGETGAVYVYFGSSGGGNSIP 53
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
5-47 3.23e-09

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: 52.51  E-value: 3.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 930588920    5 FGYAVAATDTNGDGLDDLLVGAPLlmertadGRPQEVGRVYIY 47
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLAVGAPG-------EGGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
71-107 4.55e-09

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: 52.13  E-value: 4.55e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 930588920   71 FGSSLTpLGDLDQDGYNDVAIGAPFGGEAQQGVVFIF 107
Cdd:pfam01839   1 FGYSVA-VGDLNGDGYADLAVGAPGEGGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
134-186 6.69e-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: 43.90  E-value: 6.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 930588920   134 FFGSALRGGRDLDGNGYPDLIVGSFGVDKALVYRGRPIISASASLTIFPSMFN 186
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQN 56
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
135-157 8.98e-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: 34.41  E-value: 8.98e-03
                          10        20
                  ....*....|....*....|...
gi 930588920  135 FGSALRGGrDLDGNGYPDLIVGS 157
Cdd:pfam01839   1 FGYSVAVG-DLNGDGYADLAVGA 22
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
169-597 0e+00

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: 553.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  169 RPIISASASLTIFPSMFNPEERSCSLEGNPVSCINLSFCLNASGKHVPN-SIGFEVELQLDWQKQKGGVRRALFLTSKQA 247
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIPNpSLVLNYELELDRQKKKGLPPRVLFLDSQQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  248 TLTQTLLIQNGAREDCREMKIYLRNEseFRDKLSPIHIALNFSL--DPKAPMDSHGLRPVLHYQSKSRIEDKAQILLDCG 325
Cdd:pfam08441  81 SLTGTLVLLSQGRKVCRTTKAYLRDE--FRDKLSPIVISLNYSLrvDPRAPSDLPGLKPILDQNQPSTVQEQANFLKDCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  326 EDNICVPDLQLDVYGE----KKHVYLGDKNALNLTFHAQNLGEGgAYEAELRVTAPLEAEYSGlVRHPGNFSSLSCDYFA 401
Cdd:pfam08441 159 EDNVCVPDLQLSAKFDsresDEPLLLGDDNDLALEITVTNLGED-AYEAELYVTLPPGLDYSG-VRREGSEKQLSCTAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  402 VNQSRQLVCDLGNPMK----LWGGLRFTVPHLQDTKKTIQFDFQILSKNLNNSQSNVVSFPLSVEAQAQVSLNGVSKPEA 477
Cdd:pfam08441 237 ENSTRQVVCDLGNPMKrgtqVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVSLKVPVVAEAQLSLSGVSKPDQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920  478 VIFPVSDWNPQDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQAL-EGQQLLYVTKVTGLS--NCTSNYTPNSQ 554
Cdd:pfam08441 317 VVGGSVKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELsNGKWLLYLLDVQGQGkgECSPQNEINPL 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 930588920  555 GLELDPETS-------PHHLQKREAPGRS--STASGTQVLKCPE-AKCFRLRC 597
Cdd:pfam08441 397 NLTQSLESSkplrtsrVHHVVKRRDVLKSekATQTASVLLSCDSgARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
68-122 1.82e-15

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: 70.87  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 930588920    68 FSRFGSSLTPLGDLDQDGYNDVAIGAPFGGEAQ-QGVVFIFPGGPGGLSTKPSQVL 122
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGeTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
1-58 8.76e-13

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: 63.55  E-value: 8.76e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 930588920     1 MASYFGYAVA-ATDTNGDGLDDLLVGAPLlmertaDGRPQEVGRVYIYLQRPAGIDPTP 58
Cdd:smart00191   1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPR------ANDAGETGAVYVYFGSSGGGNSIP 53
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
5-47 3.23e-09

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: 52.51  E-value: 3.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 930588920    5 FGYAVAATDTNGDGLDDLLVGAPLlmertadGRPQEVGRVYIY 47
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLAVGAPG-------EGGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
71-107 4.55e-09

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: 52.13  E-value: 4.55e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 930588920   71 FGSSLTpLGDLDQDGYNDVAIGAPFGGEAQQGVVFIF 107
Cdd:pfam01839   1 FGYSVA-VGDLNGDGYADLAVGAPGEGGAGAGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
13-91 2.18e-06

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 45.29  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930588920   13 DTNGDGLDDLLVGAPllmertadgrpqevGRVYIYLQRPAGidptpTLTLTGQDEFSRFGSSLTP-LGDLDQDGYNDVAI 91
Cdd:pfam13517   1 DLDGDGKLDLVVAND--------------GGLRLYLNNGDG-----TFTFITSVSLGGGGGGLSVaVGDLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
134-186 6.69e-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: 43.90  E-value: 6.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 930588920   134 FFGSALRGGRDLDGNGYPDLIVGSFGVDKALVYRGRPIISASASLTIFPSMFN 186
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQN 56
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
80-155 1.42e-03

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 37.59  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930588920   80 DLDQDGYNDVAIgapfggeAQQGVVFIFPGGPGGLSTKPSQVLQPLWAAGRTPDFFgsalrggrDLDGNGYPDLIV 155
Cdd:pfam13517   1 DLDGDGKLDLVV-------ANDGGLRLYLNNGDGTFTFITSVSLGGGGGGLSVAVG--------DLDGDGRLDLLV 61
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
135-157 8.98e-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: 34.41  E-value: 8.98e-03
                          10        20
                  ....*....|....*....|...
gi 930588920  135 FGSALRGGrDLDGNGYPDLIVGS 157
Cdd:pfam01839   1 FGYSVAVG-DLNGDGYADLAVGA 22
 
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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