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Conserved domains on  [gi|281360997|ref|NP_728021|]
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inflated, isoform C [Drosophila melanogaster]

Protein Classification

integrin alpha( domain architecture ID 12192572)

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:  2.60.40.1460|2.130.10.130
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 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 475-867 5.61e-87

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: 291.15  E-value: 5.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   475 RPVAAVNAETSFASNSklISLDDRSCQLVRdhKKVPCMLLTTCWSYTGRYLPEQ-LDFDVSWLLDA--KKLLNPRMFFLR 551
Cdd:pfam08441    1 RPVVSVSASLQVEPNS--INPEKKNCTLTG--TPVSCFTVRACFSYTGKPIPNPsLVLNYELELDRqkKKGLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   552 DEGKNIRNQTIRLNYGQKYCLNETVYLLDKVQDKLTPLEVEARYNLRSSRPLDPmvrhRRSILEPVIDQNREIVLRDAIN 631
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPS----DLPGLKPILDQNQPSTVQEQAN 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   632 IQKNCGPDNICEPDLKLKVSTVDK-----YLFGSPEPLVIEVFISNTNEDAFEAAFYMVTPPDLQFRKLQQLGEKKdtPI 706
Cdd:pfam08441  153 FLKDCGEDNVCVPDLQLSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEK--QL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   707 TCSPPTPENNHTLKCDIGNPLESGKIAHFKISLVPEEKYGSSSSYDFYWEANSTNLEKPGseyDNKIRQSVGIWVDTDLD 786
Cdd:pfam08441  231 SCTAKKENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLS 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   787 IKGTSLPDyQLYKAD-DYKELENATKEDDIGPQVVHIYEIRNNRPSIIEEAEVFIHLPYETIVGDPLMYLLNQPETgGKI 865
Cdd:pfam08441  308 LSGVSKPD-QVVGGSvKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ-GKG 385


                   ..
gi 281360997   866 QC 867
Cdd:pfam08441  386 EC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-426 9.46e-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: 63.93  E-value: 9.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 281360997    373 GRFGLALTTLGDVNGDGYGDFAVGAPYDGPEGR-GVVYIFHGSPMGPLAKPSQII 426
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGEtGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 250-291 4.29e-06

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.06  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 281360997    250 DDSYLGYSMV-TGDFDGDRSEDVAIGMPRGGN--LVGRIVVNRWN 291
Cdd:smart00191    1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPRANDagETGAVYVYFGS 45
Glutenin_hmw super family cl26620
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1096-1191 4.77e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


The actual alignment was detected with superfamily member pfam03157:

Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 44.55  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997  1096 GQYQNPSQSlgqSQGQFQANANQGHYQGQNQaQFQARNPGFQGQTSYQGQTQYSGQPGGYQTHHVTYSSGSKP----YYG 1171
Cdd:pfam03157  542 GQLQQPTQG---QQGQQSGQGQQGQQPGQGQ-QGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPgqwqQPG 617

                           90       100
                   ....*....|....*....|..
gi 281360997  1172 RENEDFYDEDNLQ--QATPGHW 1191
Cdd:pfam03157  618 QGQPGYYPTSSLQlgQGQQGYY 639
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 46-110 6.13e-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: 39.28  E-value: 6.13e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281360997     46 SNSMFGFSIAMHkgrsGFYGNQNNVSLIVGAPKFDTSRyqqgvtEAGGVFKC--SLNDDDCKLVPFD 110
Cdd:smart00191    1 PGSYFGYSVAGV----GDVNGDGYPDLLVGAPRANDAG------ETGAVYVYfgSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 441-472 4.40e-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: 4.40e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 281360997    441 FGFALSGGLDMDGNTYPDLAVGAYSSD------QVFIF 472
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANdagetgAVYVY 42
 
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 ...
 475-867 5.61e-87

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: 291.15  E-value: 5.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   475 RPVAAVNAETSFASNSklISLDDRSCQLVRdhKKVPCMLLTTCWSYTGRYLPEQ-LDFDVSWLLDA--KKLLNPRMFFLR 551
Cdd:pfam08441    1 RPVVSVSASLQVEPNS--INPEKKNCTLTG--TPVSCFTVRACFSYTGKPIPNPsLVLNYELELDRqkKKGLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   552 DEGKNIRNQTIRLNYGQKYCLNETVYLLDKVQDKLTPLEVEARYNLRSSRPLDPmvrhRRSILEPVIDQNREIVLRDAIN 631
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPS----DLPGLKPILDQNQPSTVQEQAN 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   632 IQKNCGPDNICEPDLKLKVSTVDK-----YLFGSPEPLVIEVFISNTNEDAFEAAFYMVTPPDLQFRKLQQLGEKKdtPI 706
Cdd:pfam08441  153 FLKDCGEDNVCVPDLQLSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEK--QL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   707 TCSPPTPENNHTLKCDIGNPLESGKIAHFKISLVPEEKYGSSSSYDFYWEANSTNLEKPGseyDNKIRQSVGIWVDTDLD 786
Cdd:pfam08441  231 SCTAKKENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLS 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   787 IKGTSLPDyQLYKAD-DYKELENATKEDDIGPQVVHIYEIRNNRPSIIEEAEVFIHLPYETIVGDPLMYLLNQPETgGKI 865
Cdd:pfam08441  308 LSGVSKPD-QVVGGSvKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ-GKG 385


                   ..
gi 281360997   866 QC 867
Cdd:pfam08441  386 EC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-426 9.46e-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: 63.93  E-value: 9.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 281360997    373 GRFGLALTTLGDVNGDGYGDFAVGAPYDGPEGR-GVVYIFHGSPMGPLAKPSQII 426
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGEtGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 375-411 7.12e-09

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 52.51  E-value: 7.12e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 281360997   375 FGLALTTlGDVNGDGYGDFAVGAPYDGPEGRGVVYIF 411
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEGGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 250-291 4.29e-06

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.06  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 281360997    250 DDSYLGYSMV-TGDFDGDRSEDVAIGMPRGGN--LVGRIVVNRWN 291
Cdd:smart00191    1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPRANDagETGAVYVYFGS 45
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1096-1191 4.77e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 44.55  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997  1096 GQYQNPSQSlgqSQGQFQANANQGHYQGQNQaQFQARNPGFQGQTSYQGQTQYSGQPGGYQTHHVTYSSGSKP----YYG 1171
Cdd:pfam03157  542 GQLQQPTQG---QQGQQSGQGQQGQQPGQGQ-QGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPgqwqQPG 617

                           90       100
                   ....*....|....*....|..
gi 281360997  1172 RENEDFYDEDNLQ--QATPGHW 1191
Cdd:pfam03157  618 QGQPGYYPTSSLQlgQGQQGYY 639
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 46-110 6.13e-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: 39.28  E-value: 6.13e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281360997     46 SNSMFGFSIAMHkgrsGFYGNQNNVSLIVGAPKFDTSRyqqgvtEAGGVFKC--SLNDDDCKLVPFD 110
Cdd:smart00191    1 PGSYFGYSVAGV----GDVNGDGYPDLLVGAPRANDAG------ETGAVYVYfgSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 441-472 4.40e-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: 4.40e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 281360997    441 FGFALSGGLDMDGNTYPDLAVGAYSSD------QVFIF 472
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANdagetgAVYVY 42
 
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 ...
 475-867 5.61e-87

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: 291.15  E-value: 5.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   475 RPVAAVNAETSFASNSklISLDDRSCQLVRdhKKVPCMLLTTCWSYTGRYLPEQ-LDFDVSWLLDA--KKLLNPRMFFLR 551
Cdd:pfam08441    1 RPVVSVSASLQVEPNS--INPEKKNCTLTG--TPVSCFTVRACFSYTGKPIPNPsLVLNYELELDRqkKKGLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   552 DEGKNIRNQTIRLNYGQKYCLNETVYLLDKVQDKLTPLEVEARYNLRSSRPLDPmvrhRRSILEPVIDQNREIVLRDAIN 631
Cdd:pfam08441   77 SQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPS----DLPGLKPILDQNQPSTVQEQAN 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   632 IQKNCGPDNICEPDLKLKVSTVDK-----YLFGSPEPLVIEVFISNTNEDAFEAAFYMVTPPDLQFRKLQQLGEKKdtPI 706
Cdd:pfam08441  153 FLKDCGEDNVCVPDLQLSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEK--QL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   707 TCSPPTPENNHTLKCDIGNPLESGKIAHFKISLVPEEKYGSSSSYDFYWEANSTNLEKPGseyDNKIRQSVGIWVDTDLD 786
Cdd:pfam08441  231 SCTAKKENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLS 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997   787 IKGTSLPDyQLYKAD-DYKELENATKEDDIGPQVVHIYEIRNNRPSIIEEAEVFIHLPYETIVGDPLMYLLNQPETgGKI 865
Cdd:pfam08441  308 LSGVSKPD-QVVGGSvKGESAMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ-GKG 385


                   ..
gi 281360997   866 QC 867
Cdd:pfam08441  386 EC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 373-426 9.46e-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: 63.93  E-value: 9.46e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 281360997    373 GRFGLALTTLGDVNGDGYGDFAVGAPYDGPEGR-GVVYIFHGSPMGPLAKPSQII 426
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGEtGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 375-411 7.12e-09

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 52.51  E-value: 7.12e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 281360997   375 FGLALTTlGDVNGDGYGDFAVGAPYDGPEGRGVVYIF 411
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEGGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 250-291 4.29e-06

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 45.06  E-value: 4.29e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 281360997    250 DDSYLGYSMV-TGDFDGDRSEDVAIGMPRGGN--LVGRIVVNRWN 291
Cdd:smart00191    1 PGSYFGYSVAgVGDVNGDGYPDLLVGAPRANDagETGAVYVYFGS 45
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1096-1191 4.77e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 44.55  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997  1096 GQYQNPSQSlgqSQGQFQANANQGHYQGQNQaQFQARNPGFQGQTSYQGQTQYSGQPGGYQTHHVTYSSGSKP----YYG 1171
Cdd:pfam03157  542 GQLQQPTQG---QQGQQSGQGQQGQQPGQGQ-QGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPgqwqQPG 617

                           90       100
                   ....*....|....*....|..
gi 281360997  1172 RENEDFYDEDNLQ--QATPGHW 1191
Cdd:pfam03157  618 QGQPGYYPTSSLQlgQGQQGYY 639
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 46-110 6.13e-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: 39.28  E-value: 6.13e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281360997     46 SNSMFGFSIAMHkgrsGFYGNQNNVSLIVGAPKFDTSRyqqgvtEAGGVFKC--SLNDDDCKLVPFD 110
Cdd:smart00191    1 PGSYFGYSVAGV----GDVNGDGYPDLLVGAPRANDAG------ETGAVYVYfgSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 441-472 4.40e-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: 4.40e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 281360997    441 FGFALSGGLDMDGNTYPDLAVGAYSSD------QVFIF 472
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANdagetgAVYVY 42
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1093-1191 5.59e-03

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 41.09  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360997  1093 RSQGQYQNPSQSLGQSQ-GQFQANANQ------GHYQGQNQAQFQARNPGFQGQTSYQGQTQYSGQPGgyqthhvtysSG 1165
Cdd:pfam03157  335 GQQGQQPAQGQQPGQGQpGYYPTSPQQpgqgqpGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPG----------QG 404

                           90       100
                   ....*....|....*....|....*...
gi 281360997  1166 SKPyyGRENEDFYDEDNLQ--QATPGHW 1191
Cdd:pfam03157  405 QQP--GQGQPGYYPTSPQQsgQGQPGYY 430
 
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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