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Conserved domains on  [gi|578828549|ref|XP_006721107|]
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integrin alpha-L isoform X2 [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 11619903)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 106-240 1.98e-60

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


The actual alignment was detected with superfamily member cd01469:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 177  Bit Score: 204.13  E-value: 1.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  106 GSILFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEAT 185
Cdd:cd01469    37 TKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTATAIQYVVTELFSESNGARKDATKVLVVITDGESH 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828549  186 DSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDL 240
Cdd:cd01469   117 DDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 530-916 1.58e-35

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


The actual alignment was detected with superfamily member pfam08441:

Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 141.30  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   530 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 606
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   607 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtpRDQRAQGKDIPPiLRPSLH----- 676
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL-------RVDPRAPSDLPG-LKPILDqnqps 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   677 SETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEML 752
Cdd:pfam08441  146 TVQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   753 KPHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATT 832
Cdd:pfam08441  225 GSEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   833 IIPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP- 900
Cdd:pfam08441  297 KVPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKw 372

                          410
                   ....*....|....*....
gi 578828549   901 ---ITHqwsVQMEPPVPCH 916
Cdd:pfam08441  373 llyLLD---VQGQGKGECS 388
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-486 3.46e-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: 65.09  E-value: 3.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 578828549    434 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 486
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-420 1.67e-08

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: 51.61  E-value: 1.67e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 578828549    373 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 420
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1030-1044 2.25e-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: 2.25e-03
                           10
                   ....*....|....*
gi 578828549  1030 KVGFFKRNLKEKMEA 1044
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 496-520 3.48e-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: 36.58  E-value: 3.48e-03
                            10        20
                    ....*....|....*....|....*
gi 578828549    496 QWFGRSIHGVKDLEGDGLADVAVGA 520
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 106-240 1.98e-60

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 204.13  E-value: 1.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  106 GSILFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEAT 185
Cdd:cd01469    37 TKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTATAIQYVVTELFSESNGARKDATKVLVVITDGESH 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828549  186 DSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDL 240
Cdd:cd01469   117 DDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 530-916 1.58e-35

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: 141.30  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   530 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 606
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   607 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtpRDQRAQGKDIPPiLRPSLH----- 676
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL-------RVDPRAPSDLPG-LKPILDqnqps 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   677 SETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEML 752
Cdd:pfam08441  146 TVQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   753 KPHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATT 832
Cdd:pfam08441  225 GSEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   833 IIPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP- 900
Cdd:pfam08441  297 KVPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKw 372

                          410
                   ....*....|....*....
gi 578828549   901 ---ITHqwsVQMEPPVPCH 916
Cdd:pfam08441  373 llyLLD---VQGQGKGECS 388
VWA pfam00092
von Willebrand factor type A domain;
107-243 1.04e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.52  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   107 SILFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL----TNTFGAINYVATEVFREELGARPDATKVLIIITDG 182
Cdd:pfam00092   37 GTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLgggtTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDG 113

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828549   183 EATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFASKPASEFVKILDTFEKLKDLFTE 243
Cdd:pfam00092  114 RSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 110-237 2.06e-22

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 95.60  E-value: 2.06e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549    110 FAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL----TNTFGAINYVATEVFREELGARPDATKVLIIITDGEAT 185
Cdd:smart00327   40 VGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgggTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESN 116

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 578828549    186 DSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKFASKPASEFVKILDTFEKL 237
Cdd:smart00327  117 DGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKLASAPGGVYVFLPELLDLL 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-486 3.46e-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: 65.09  E-value: 3.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 578828549    434 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 486
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-420 1.67e-08

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: 51.61  E-value: 1.67e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 578828549    373 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 420
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 438-471 1.58e-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: 48.28  E-value: 1.58e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 578828549   438 FGEAItALTDINGDGLVDVAVGAPLE---EQGAVYIF 471
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 377-414 4.37e-04

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: 38.65  E-value: 4.37e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578828549   377 FGGELCGVDVDQDGETElLLIGAPlFYGEQRGGRVFIY 414
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1030-1044 2.25e-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: 2.25e-03
                           10
                   ....*....|....*
gi 578828549  1030 KVGFFKRNLKEKMEA 1044
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 148-244 2.77e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 40.69  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  148 TNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETLHKFA 220
Cdd:COG1240   166 TPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLLREIA 238

                          90       100
                  ....*....|....*....|....
gi 578828549  221 SKPASEFVKILDTfEKLKDLFTEL 244
Cdd:COG1240   239 EATGGRYFRADDL-SELAAIYREI 261
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 496-520 3.48e-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: 36.58  E-value: 3.48e-03
                            10        20
                    ....*....|....*....|....*
gi 578828549    496 QWFGRSIHGVKDLEGDGLADVAVGA 520
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 106-240 1.98e-60

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 204.13  E-value: 1.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  106 GSILFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEAT 185
Cdd:cd01469    37 TKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTATAIQYVVTELFSESNGARKDATKVLVVITDGESH 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828549  186 DSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDL 240
Cdd:cd01469   117 DDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 530-916 1.58e-35

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: 141.30  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   530 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 606
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   607 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtpRDQRAQGKDIPPiLRPSLH----- 676
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL-------RVDPRAPSDLPG-LKPILDqnqps 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   677 SETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEML 752
Cdd:pfam08441  146 TVQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   753 KPHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATT 832
Cdd:pfam08441  225 GSEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSL 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   833 IIPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP- 900
Cdd:pfam08441  297 KVPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKw 372

                          410
                   ....*....|....*....
gi 578828549   901 ---ITHqwsVQMEPPVPCH 916
Cdd:pfam08441  373 llyLLD---VQGQGKGECS 388
VWA pfam00092
von Willebrand factor type A domain;
107-243 1.04e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.52  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549   107 SILFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL----TNTFGAINYVATEVFREELGARPDATKVLIIITDG 182
Cdd:pfam00092   37 GTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLgggtTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDG 113

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828549   183 EATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFASKPASEFVKILDTFEKLKDLFTE 243
Cdd:pfam00092  114 RSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 110-237 2.06e-22

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 95.60  E-value: 2.06e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549    110 FAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL----TNTFGAINYVATEVFREELGARPDATKVLIIITDGEAT 185
Cdd:smart00327   40 VGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgggTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESN 116

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 578828549    186 DSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKFASKPASEFVKILDTFEKL 237
Cdd:smart00327  117 DGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKLASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 105-228 1.78e-20

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 89.27  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  105 DGSILFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL----TNTFGAINYVATEVFREElGARPDATKVLIIIT 180
Cdd:cd01450    36 PDKTRVGLVQYSDDVRVEFSLNDYKSKDD---LLKAVKNLKYLggggTNTGKALQYALEQLFSES-NARENVPKVIIVLT 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578828549  181 DGEATDSGNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKFASKPASEFV 228
Cdd:cd01450   112 DGRSDDGGDPKEAAAKLKdegikvFVVGVGPA-----DEEELREIASCPSERHV 160
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 110-234 1.84e-17

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 80.79  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  110 FAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL---TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATD 186
Cdd:cd01482    41 VGLVQYSDDPRTEFDLNAYTSKED---VLAAIKNLPYKggnTRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578828549  187 sgNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKFASKPASEFVKILDTF 234
Cdd:cd01482   118 --DVELPARVLRnlgvnvFAVGVKDA-----DESELKMIASKPSETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 102-234 1.03e-15

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 75.73  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  102 DPTDGSILFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL---TNTFGAINYVATEVFREELGARPDATKVLII 178
Cdd:cd01472    33 DIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDD---VLEAVKNLRYIgggTNTGKALKYVRENLFTEASGSREGVPKVLVV 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  179 ITDGEATDSGNIDAAKD----IIRYIIGIGKHfqtkeSQETLHKFASKPASEFVKILDTF 234
Cdd:cd01472   110 ITDGKSQDDVEEPAVELkqagIEVFAVGVKNA-----DEEELKQIASDPKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 113-248 4.60e-15

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 75.50  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  113 VQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDAT---KVLIIITDGEATDSGN 189
Cdd:cd01475    46 VQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVS 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828549  190 IDAAK----DIIRYIIGIGkhfqtKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKI 248
Cdd:cd01475   126 EVAAKaralGIEMFAVGVG-----RADEEELREIASEPLADHVFYVEDFSTIEELTKKFQGKI 183
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-486 3.46e-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: 65.09  E-value: 3.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 578828549    434 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 486
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-420 1.67e-08

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: 51.61  E-value: 1.67e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 578828549    373 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 420
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 110-228 3.71e-08

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 54.11  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  110 FAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLL-LTNTFGAINYVATEVFREelgARPDATKVLIIITDGEATDSG 188
Cdd:cd00198    41 VGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGgGTNIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGP 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578828549  189 N-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKFASKPASEFV 228
Cdd:cd00198   118 EllaeaARELRKlgITVYTIGIGDDANEDE----LKEIADKTTGGAV 160
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 438-471 1.58e-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: 48.28  E-value: 1.58e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 578828549   438 FGEAItALTDINGDGLVDVAVGAPLE---EQGAVYIF 471
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 111-187 1.97e-05

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 46.16  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  111 AAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLLT----NTFGAINYVATEVFREELGARPD--ATKVLIIITDGEA 184
Cdd:cd01481    42 AVVQFSDTPRPEFYLNTHSTKAD---VLGAVRRLRLRGgsqlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKS 118


                  ...
gi 578828549  185 TDS 187
Cdd:cd01481   119 QDD 121
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 447-518 5.26e-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: 5.26e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828549   447 DINGDGLVDVAVGAPleEQGAVYIFNGrhgglspqpsqriEGTQVLSGIQWFGRSIHG----VKDLEGDGLADVAV 518
Cdd:pfam13517    1 DLDGDGKLDLVVAND--GGLRLYLNNG-------------DGTFTFITSVSLGGGGGGlsvaVGDLDGDGRLDLLV 61
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 111-227 8.74e-05

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 44.31  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  111 AAVQFSTSYKT--EFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYvATEVFREELGARPDATKVLIIITDGEATDsg 188
Cdd:cd01476    41 ALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTTATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHD-- 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 578828549  189 NIDAAKDIIR-----YIIGIGKHFQTKESQETLHKFASKPASEF 227
Cdd:cd01476   118 DPEKQARILRavpniETFAVGTGDPGTVDTEELHSITGNEDHIF 161
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 377-414 4.37e-04

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: 38.65  E-value: 4.37e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578828549   377 FGGELCGVDVDQDGETElLLIGAPlFYGEQRGGRVFIY 414
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 385-458 1.71e-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: 1.71e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828549   385 DVDQDGETELLLIGAplfygeqrgGRVFIYQRRQLG-FEEVSELQGDPGYplgrFGEAITALtDINGDGLVDVAV 458
Cdd:pfam13517    1 DLDGDGKLDLVVAND---------GGLRLYLNNGDGtFTFITSVSLGGGG----GGLSVAVG-DLDGDGRLDLLV 61
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1030-1044 2.25e-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: 2.25e-03
                           10
                   ....*....|....*
gi 578828549  1030 KVGFFKRNLKEKMEA 1044
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 148-244 2.77e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 40.69  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  148 TNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETLHKFA 220
Cdd:COG1240   166 TPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLLREIA 238

                          90       100
                  ....*....|....*....|....
gi 578828549  221 SKPASEFVKILDTfEKLKDLFTEL 244
Cdd:COG1240   239 EATGGRYFRADDL-SELAAIYREI 261
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 496-520 3.48e-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: 36.58  E-value: 3.48e-03
                            10        20
                    ....*....|....*....|....*
gi 578828549    496 QWFGRSIHGVKDLEGDGLADVAVGA 520
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 113-204 4.88e-03

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 39.29  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828549  113 VQFSTSYKTEFDFSDYvKRKDPDALLKHVKHMLLL------TNTFGAINYVATEVFrEELGARPDATKVLIIITDGEA-T 185
Cdd:cd01471    45 VTFSTNAKELIRLSSP-NSTNKDLALNAIRALLSLyypngsTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPdS 122

                          90       100
                  ....*....|....*....|....
gi 578828549  186 DSGNIDAAKDI-----IRYIIGIG 204
Cdd:cd01471   123 KFRTLKEARKLrergvIIAVLGVG 146
 
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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