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Conserved domains on  [gi|937834194|ref|NP_001303241|]
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integrin alpha-4 isoform 2 precursor [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 10640645)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-105 1.49e-06

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.90  E-value: 1.49e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937834194    48 HNTLFGYSVVLHSHGANR---WLLVGAPTANWLAnasviNPGAIYRCRIGKNpGQTCEQLQ 105
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDgypDLLVGAPRANDAG-----ETGAVYVYFGSSG-GGNSIPLQ 55
 
Name Accession Description Interval E-value
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-105 1.49e-06

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.90  E-value: 1.49e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937834194    48 HNTLFGYSVVLHSHGANR---WLLVGAPTANWLAnasviNPGAIYRCRIGKNpGQTCEQLQ 105
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDgypDLLVGAPRANDAG-----ETGAVYVYFGSSG-GGNSIPLQ 55
 
Name Accession Description Interval E-value
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-105 1.49e-06

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.90  E-value: 1.49e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937834194    48 HNTLFGYSVVLHSHGANR---WLLVGAPTANWLAnasviNPGAIYRCRIGKNpGQTCEQLQ 105
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDgypDLLVGAPRANDAG-----ETGAVYVYFGSSG-GGNSIPLQ 55
 
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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