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Conserved domains on  [gi|187950353|gb|AAI36456|]
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Integrin, alpha 6 [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 12192641)

integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 465-939 3.67e-174

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: 517.26  E-value: 3.67e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   465 RPVINIQKTITVTPNRIDLRQKTaCGAPSG--ICLQVKSCFEYTANPAgYNPSISIVGTLEAEKERRKsGLSSRVQFrNQ 542
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKN-CTLTGTpvSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKKK-GLPPRVLF-LD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   543 GSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPssRRRVNSLPEVLPILNSDEPKTAHIDVHFL 622
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVD--PRAPSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   623 KEgCGDDNVCNSNLKLEYKFCTREGNqdkfsylpiqkgvPELVLKDQKDIALEITVTNspsnprnptkDGDDAHEAKLIA 702
Cdd:pfam08441  155 KD-CGEDNVCVPDLQLSAKFDSRESD-------------EPLLLGDDNDLALEITVTN----------LGEDAYEAELYV 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   703 TFPDTLTYSAYRelRAFPEKQLSCVANQNGS--QADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQD 780
Cdd:pfam08441  211 TLPPGLDYSGVR--REGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQN 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   781 -NLAPITAKAKVVIELLLSVSGVAKPSQVyFGGTVVGEQAMK--SEDEVGSLIEYEFRVINLGKPltNLGTATLNIQWPK 857
Cdd:pfam08441  289 sNSNPVSLKVPVVAEAQLSLSGVSKPDQV-VGGSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEISWPY 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   858 EISNGKWLLYLVKVEskGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQT----LNCSVNVN 933
Cdd:pfam08441  366 ELSNGKWLLYLLDVQ--GQGKGECSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTasvlLSCDSGAR 443


                   ....*.
gi 187950353   934 CVNIRC 939
Cdd:pfam08441  444 CVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 374-425 1.42e-14

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: 68.94  E-value: 1.42e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 187950353    374 DSMFGITVKNIGDINQDGYPDIAVGAPYDD----LGKVFIYHGSANGINTKPTQVL 425
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANdageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 314-367 6.46e-10

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.46e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    314 SSFGYDVA-VVDLNKDGWQDIVIGAPQYFdrDGEVGGAVYVYMNQQ--GRWNNVKPI 367
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRAN--DAGETGAVYVYFGSSggGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 40-100 2.09e-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: 2.09e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187950353     40 PGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEAlplqrANRTGGLYSCDITARG-PCTRIEFD 100
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAND-----AGETGAVYVYFGSSGGgNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 254-306 7.31e-04

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: 38.51  E-value: 7.31e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    254 ANSYLGFSLDSGkGIVSKDEIT-FVSGAPRANHS---GAVVLLKRDMKSAHLLPEHI 306
Cdd:smart00191    1 PGSYFGYSVAGV-GDVNGDGYPdLLVGAPRANDAgetGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1038-1052 2.27e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.27e-03
                           10
                   ....*....|....*
gi 187950353  1038 KCGFFKRNKKDHYDA 1052
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 431-454 2.87e-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: 36.97  E-value: 2.87e-03
                            10        20
                    ....*....|....*....|....
gi 187950353    431 YFGYSIAGNMDLDRNSYPDVAVGS 454
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
 
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 ...
 465-939 3.67e-174

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: 517.26  E-value: 3.67e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   465 RPVINIQKTITVTPNRIDLRQKTaCGAPSG--ICLQVKSCFEYTANPAgYNPSISIVGTLEAEKERRKsGLSSRVQFrNQ 542
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKN-CTLTGTpvSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKKK-GLPPRVLF-LD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   543 GSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPssRRRVNSLPEVLPILNSDEPKTAHIDVHFL 622
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVD--PRAPSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   623 KEgCGDDNVCNSNLKLEYKFCTREGNqdkfsylpiqkgvPELVLKDQKDIALEITVTNspsnprnptkDGDDAHEAKLIA 702
Cdd:pfam08441  155 KD-CGEDNVCVPDLQLSAKFDSRESD-------------EPLLLGDDNDLALEITVTN----------LGEDAYEAELYV 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   703 TFPDTLTYSAYRelRAFPEKQLSCVANQNGS--QADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQD 780
Cdd:pfam08441  211 TLPPGLDYSGVR--REGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQN 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   781 -NLAPITAKAKVVIELLLSVSGVAKPSQVyFGGTVVGEQAMK--SEDEVGSLIEYEFRVINLGKPltNLGTATLNIQWPK 857
Cdd:pfam08441  289 sNSNPVSLKVPVVAEAQLSLSGVSKPDQV-VGGSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEISWPY 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   858 EISNGKWLLYLVKVEskGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQT----LNCSVNVN 933
Cdd:pfam08441  366 ELSNGKWLLYLLDVQ--GQGKGECSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTasvlLSCDSGAR 443


                   ....*.
gi 187950353   934 CVNIRC 939
Cdd:pfam08441  444 CVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 374-425 1.42e-14

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: 68.94  E-value: 1.42e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 187950353    374 DSMFGITVKNIGDINQDGYPDIAVGAPYDD----LGKVFIYHGSANGINTKPTQVL 425
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANdageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 314-367 6.46e-10

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.46e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    314 SSFGYDVA-VVDLNKDGWQDIVIGAPQYFdrDGEVGGAVYVYMNQQ--GRWNNVKPI 367
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRAN--DAGETGAVYVYFGSSggGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 316-354 9.97e-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: 54.44  E-value: 9.97e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 187950353   316 FGYDVAVVDLNKDGWQDIVIGAPQYFDRDgevGGAVYVY 354
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAPGEGGAG---AGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 40-100 2.09e-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: 2.09e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187950353     40 PGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEAlplqrANRTGGLYSCDITARG-PCTRIEFD 100
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAND-----AGETGAVYVYFGSSGGgNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 385-410 6.58e-06

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: 43.65  E-value: 6.58e-06
                           10        20
                   ....*....|....*....|....*....
gi 187950353   385 GDINQDGYPDIAVGAPYDDL---GKVFIY 410
Cdd:pfam01839    8 GDLNGDGYADLAVGAPGEGGagaGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 254-306 7.31e-04

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: 38.51  E-value: 7.31e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    254 ANSYLGFSLDSGkGIVSKDEIT-FVSGAPRANHS---GAVVLLKRDMKSAHLLPEHI 306
Cdd:smart00191    1 PGSYFGYSVAGV-GDVNGDGYPdLLVGAPRANDAgetGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1038-1052 2.27e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.27e-03
                           10
                   ....*....|....*
gi 187950353  1038 KCGFFKRNKKDHYDA 1052
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 431-454 2.87e-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: 36.97  E-value: 2.87e-03
                            10        20
                    ....*....|....*....|....
gi 187950353    431 YFGYSIAGNMDLDRNSYPDVAVGS 454
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
 
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 ...
 465-939 3.67e-174

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: 517.26  E-value: 3.67e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   465 RPVINIQKTITVTPNRIDLRQKTaCGAPSG--ICLQVKSCFEYTANPAgYNPSISIVGTLEAEKERRKsGLSSRVQFrNQ 542
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKN-CTLTGTpvSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKKK-GLPPRVLF-LD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   543 GSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPssRRRVNSLPEVLPILNSDEPKTAHIDVHFL 622
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVD--PRAPSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   623 KEgCGDDNVCNSNLKLEYKFCTREGNqdkfsylpiqkgvPELVLKDQKDIALEITVTNspsnprnptkDGDDAHEAKLIA 702
Cdd:pfam08441  155 KD-CGEDNVCVPDLQLSAKFDSRESD-------------EPLLLGDDNDLALEITVTN----------LGEDAYEAELYV 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   703 TFPDTLTYSAYRelRAFPEKQLSCVANQNGS--QADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQD 780
Cdd:pfam08441  211 TLPPGLDYSGVR--REGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQN 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   781 -NLAPITAKAKVVIELLLSVSGVAKPSQVyFGGTVVGEQAMK--SEDEVGSLIEYEFRVINLGKPltNLGTATLNIQWPK 857
Cdd:pfam08441  289 sNSNPVSLKVPVVAEAQLSLSGVSKPDQV-VGGSVKGESAMKprSEEDIGPLVEHTYEVINNGPS--TVSGASLEISWPY 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187950353   858 EISNGKWLLYLVKVEskGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQT----LNCSVNVN 933
Cdd:pfam08441  366 ELSNGKWLLYLLDVQ--GQGKGECSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTasvlLSCDSGAR 443


                   ....*.
gi 187950353   934 CVNIRC 939
Cdd:pfam08441  444 CVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 374-425 1.42e-14

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: 68.94  E-value: 1.42e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 187950353    374 DSMFGITVKNIGDINQDGYPDIAVGAPYDD----LGKVFIYHGSANGINTKPTQVL 425
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANdageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 314-367 6.46e-10

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.84  E-value: 6.46e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    314 SSFGYDVA-VVDLNKDGWQDIVIGAPQYFdrDGEVGGAVYVYMNQQ--GRWNNVKPI 367
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRAN--DAGETGAVYVYFGSSggGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 316-354 9.97e-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: 54.44  E-value: 9.97e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 187950353   316 FGYDVAVVDLNKDGWQDIVIGAPQYFDRDgevGGAVYVY 354
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 ...
 324-397 7.62e-08

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: 49.92  E-value: 7.62e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187950353   324 DLNKDGWQDIVIGAPqyfdrdgevgGAVYVY-MNQQGRWNNVKPIRLNGTKDSMfGITVkniGDINQDGYPDIAV 397
Cdd:pfam13517    1 DLDGDGKLDLVVAND----------GGLRLYlNNGDGTFTFITSVSLGGGGGGL-SVAV---GDLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 40-100 2.09e-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: 2.09e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187950353     40 PGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEAlplqrANRTGGLYSCDITARG-PCTRIEFD 100
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAND-----AGETGAVYVYFGSSGGgNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 385-410 6.58e-06

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: 43.65  E-value: 6.58e-06
                           10        20
                   ....*....|....*....|....*....
gi 187950353   385 GDINQDGYPDIAVGAPYDDL---GKVFIY 410
Cdd:pfam01839    8 GDLNGDGYADLAVGAPGEGGagaGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 386-452 2.99e-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: 42.60  E-value: 2.99e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187950353   386 DINQDGYPDIAVGAPyddlGKVFIYHGSANGINTKPTQVL-----KGISPYFGysiagnmDLDRNSYPDVAV 452
Cdd:pfam13517    1 DLDGDGKLDLVVAND----GGLRLYLNNGDGTFTFITSVSlggggGGLSVAVG-------DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 254-306 7.31e-04

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: 38.51  E-value: 7.31e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 187950353    254 ANSYLGFSLDSGkGIVSKDEIT-FVSGAPRANHS---GAVVLLKRDMKSAHLLPEHI 306
Cdd:smart00191    1 PGSYFGYSVAGV-GDVNGDGYPdLLVGAPRANDAgetGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1038-1052 2.27e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.27e-03
                           10
                   ....*....|....*
gi 187950353  1038 KCGFFKRNKKDHYDA 1052
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 431-454 2.87e-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: 36.97  E-value: 2.87e-03
                            10        20
                    ....*....|....*....|....
gi 187950353    431 YFGYSIAGNMDLDRNSYPDVAVGS 454
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
 
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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