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Conserved domains on  [gi|530400182|ref|XP_005268897|]
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integrin alpha-7 isoform X1 [Homo sapiens]

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

CATH:  2.130.10.130|2.60.40.1510|2.60.40.1530|2.60.40.1460
Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368
SCOP:  4003137

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 ...
 516-1000 2.88e-143

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: 439.83  E-value: 2.88e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   516 RPILHVSHEVSIAPRSIDLEQPNCA--GGHSVCVDLRVCFSYIAVPSsYSP------TVDADTDRRlRGQVPRVTFLSRN 587
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTltGTPVSCFTVRACFSYTGKPI-PNPslvlnyELELDRQKK-KGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   588 LeepkHQASGTVWLKHQHDRVCGDAMFQLQENVKDKLRAIVVTLSYSLQtprlRRQAPGQGLPPVAPILNAHQPSTQRAE 667
Cdd:pfam08441   79 Q----PSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLR----VDPRAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   668 IHFLKQgCGEDKICQSNLQLvRARFCTRVSDTEFqplpmdvdgttalfALSGQPVIGLELMVTNlpsdpaqpqaDGDDAH 747
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQL-SAKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   748 EAQLLVMLPDSLHYSGVRALDPAEKPLCLSNENAS--HVECELGNPMKRGAQVTFYLILSTSGISIETTELEVELLLATI 825
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   826 SEQELH--PVSARARVFIELPLSIAGMAIPQQLFFsGVVRGERAMQ--SERDVGSKVKYEVTVSNQGQSlrTLGSAFLNI 901
Cdd:pfam08441  285 NEQNSNsnPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   902 MWPHEIANGKWLLYPMQVElegGQGPGQkglCSPRPNILHLDVDSRDRRRRELEPPEQQEPGERQEPSMSWWPVSSAEKk 981
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTASV- 434

                          490
                   ....*....|....*....
gi 530400182   982 kniTLDCARGtANCVVFSC 1000
Cdd:pfam08441  435 ---LLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 1.10e-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: 72.41  E-value: 1.10e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    421 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVAKPSQVL 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 362-415 7.84e-11

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: 58.54  E-value: 7.84e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    362 SGFGYSLA-VADLNSDGWPDLIVGAPYFFERQEelGGAVYVYLNQ--GGHWAGISPL 415
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 2.76e-07

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: 48.53  E-value: 2.76e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400182     48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-522 1.30e-03

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530400182    483 FGYSLSGSLDMDGNQYPDLLVGS-LADTAVLFRARPILHVS 522
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGS 45
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 304-345 1.66e-03

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.66e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 530400182    304 NSYLGFSIDSGKGLVRAEELSFVAGAPRANHK---GAVVILRKDS 345
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSS 46
 
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 ...
 516-1000 2.88e-143

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: 439.83  E-value: 2.88e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   516 RPILHVSHEVSIAPRSIDLEQPNCA--GGHSVCVDLRVCFSYIAVPSsYSP------TVDADTDRRlRGQVPRVTFLSRN 587
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTltGTPVSCFTVRACFSYTGKPI-PNPslvlnyELELDRQKK-KGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   588 LeepkHQASGTVWLKHQHDRVCGDAMFQLQENVKDKLRAIVVTLSYSLQtprlRRQAPGQGLPPVAPILNAHQPSTQRAE 667
Cdd:pfam08441   79 Q----PSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLR----VDPRAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   668 IHFLKQgCGEDKICQSNLQLvRARFCTRVSDTEFqplpmdvdgttalfALSGQPVIGLELMVTNlpsdpaqpqaDGDDAH 747
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQL-SAKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   748 EAQLLVMLPDSLHYSGVRALDPAEKPLCLSNENAS--HVECELGNPMKRGAQVTFYLILSTSGISIETTELEVELLLATI 825
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   826 SEQELH--PVSARARVFIELPLSIAGMAIPQQLFFsGVVRGERAMQ--SERDVGSKVKYEVTVSNQGQSlrTLGSAFLNI 901
Cdd:pfam08441  285 NEQNSNsnPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   902 MWPHEIANGKWLLYPMQVElegGQGPGQkglCSPRPNILHLDVDSRDRRRRELEPPEQQEPGERQEPSMSWWPVSSAEKk 981
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTASV- 434

                          490
                   ....*....|....*....
gi 530400182   982 kniTLDCARGtANCVVFSC 1000
Cdd:pfam08441  435 ---LLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 1.10e-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: 72.41  E-value: 1.10e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    421 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVAKPSQVL 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 362-415 7.84e-11

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: 58.54  E-value: 7.84e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    362 SGFGYSLA-VADLNSDGWPDLIVGAPYFFERQEelGGAVYVYLNQ--GGHWAGISPL 415
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 364-402 1.59e-10

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: 57.14  E-value: 1.59e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530400182   364 FGYSLAVADLNSDGWPDLIVGAPYFFERQeelGGAVYVY 402
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAPGEGGAG---AGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 425-458 1.01e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 49.05  E-value: 1.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530400182   425 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 458
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 2.76e-07

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: 48.53  E-value: 2.76e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400182     48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-522 1.30e-03

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530400182    483 FGYSLSGSLDMDGNQYPDLLVGS-LADTAVLFRARPILHVS 522
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGS 45
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 304-345 1.66e-03

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.66e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 530400182    304 NSYLGFSIDSGKGLVRAEELSFVAGAPRANHK---GAVVILRKDS 345
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSS 46
 
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 ...
 516-1000 2.88e-143

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: 439.83  E-value: 2.88e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   516 RPILHVSHEVSIAPRSIDLEQPNCA--GGHSVCVDLRVCFSYIAVPSsYSP------TVDADTDRRlRGQVPRVTFLSRN 587
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTltGTPVSCFTVRACFSYTGKPI-PNPslvlnyELELDRQKK-KGLPPRVLFLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   588 LeepkHQASGTVWLKHQHDRVCGDAMFQLQENVKDKLRAIVVTLSYSLQtprlRRQAPGQGLPPVAPILNAHQPSTQRAE 667
Cdd:pfam08441   79 Q----PSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLR----VDPRAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   668 IHFLKQgCGEDKICQSNLQLvRARFCTRVSDTEFqplpmdvdgttalfALSGQPVIGLELMVTNlpsdpaqpqaDGDDAH 747
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQL-SAKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   748 EAQLLVMLPDSLHYSGVRALDPAEKPLCLSNENAS--HVECELGNPMKRGAQVTFYLILSTSGISIETTELEVELLLATI 825
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   826 SEQELH--PVSARARVFIELPLSIAGMAIPQQLFFsGVVRGERAMQ--SERDVGSKVKYEVTVSNQGQSlrTLGSAFLNI 901
Cdd:pfam08441  285 NEQNSNsnPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   902 MWPHEIANGKWLLYPMQVElegGQGPGQkglCSPRPNILHLDVDSRDRRRRELEPPEQQEPGERQEPSMSWWPVSSAEKk 981
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTASV- 434

                          490
                   ....*....|....*....
gi 530400182   982 kniTLDCARGtANCVVFSC 1000
Cdd:pfam08441  435 ---LLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 1.10e-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: 72.41  E-value: 1.10e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    421 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVAKPSQVL 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 362-415 7.84e-11

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: 58.54  E-value: 7.84e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400182    362 SGFGYSLA-VADLNSDGWPDLIVGAPYFFERQEelGGAVYVYLNQ--GGHWAGISPL 415
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 364-402 1.59e-10

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: 57.14  E-value: 1.59e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530400182   364 FGYSLAVADLNSDGWPDLIVGAPYFFERQeelGGAVYVY 402
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAPGEGGAG---AGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 372-445 1.37e-09

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: 54.92  E-value: 1.37e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400182   372 DLNSDGWPDLIVGAPyfferqeelgGAVYVYLNQG-GHWAGISPLRLcgsPDSMFGISLAVlGDLNQDGFPDIAV 445
Cdd:pfam13517    1 DLDGDGKLDLVVAND----------GGLRLYLNNGdGTFTFITSVSL---GGGGGGLSVAV-GDLDGDGRLDLLV 61
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 425-458 1.01e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 49.05  E-value: 1.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530400182   425 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 458
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 2.76e-07

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: 48.53  E-value: 2.76e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400182     48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 434-503 5.98e-05

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: 41.83  E-value: 5.98e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400182   434 DLNQDGFPDIAVGapfdGDGKVFIYHGSSLGVVAKPSQVLEGEAVGIKSFgyslsGSLDMDGNQYPDLLV 503
Cdd:pfam13517    1 DLDGDGKLDLVVA----NDGGLRLYLNNGDGTFTFITSVSLGGGGGGLSV-----AVGDLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-522 1.30e-03

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 38.13  E-value: 1.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530400182    483 FGYSLSGSLDMDGNQYPDLLVGS-LADTAVLFRARPILHVS 522
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGS 45
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 304-345 1.66e-03

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.66e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 530400182    304 NSYLGFSIDSGKGLVRAEELSFVAGAPRANHK---GAVVILRKDS 345
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSS 46
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 333-383 2.46e-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: 37.20  E-value: 2.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 530400182   333 NHKGAVVILRKDSASRLVPEVMLSgerlTSGFGYSLAVADLNSDGWPDLIV 383
Cdd:pfam13517   15 DGGLRLYLNNGDGTFTFITSVSLG----GGGGGLSVAVGDLDGDGRLDLLV 61
 
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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