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Conserved domains on  [gi|1720391375|ref|XP_030105984|]
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centrosomal protein 43 isoform X1 [Mus musculus]

Protein Classification

LisH domain-containing protein( domain architecture ID 10559403)

LIS1 homology (LisH) domain-containing protein similar to Homo sapiens centrosomal protein 43 which is required for anchoring microtubules to the centrosomes and for ciliation

CATH:  1.20.960.40
Gene Ontology:  GO:0005515
SCOP:  3001444

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FOP_dimer pfam09398
FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene ...
 54-134 1.24e-27

FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene partner (FOP) is a centrosomal protein that is involved in anchoring microtubules to subcellular structures. This domain includes a Lis-homology motif. It forms an alpha helical bundle and is involved in dimerization.


:

Pssm-ID: 312785  Cd Length: 81  Bit Score: 104.17  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720391375  54 KTPLVNENLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFHPETSTIQGLEGRENLAQDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 1720391375 134 R 134
Cdd:pfam09398  81 H 81
 
Name Accession Description Interval E-value
FOP_dimer pfam09398
FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene ...
 54-134 1.24e-27

FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene partner (FOP) is a centrosomal protein that is involved in anchoring microtubules to subcellular structures. This domain includes a Lis-homology motif. It forms an alpha helical bundle and is involved in dimerization.


Pssm-ID: 312785  Cd Length: 81  Bit Score: 104.17  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720391375  54 KTPLVNENLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFHPETSTIQGLEGRENLAQDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 1720391375 134 R 134
Cdd:pfam09398  81 H 81
 
Name Accession Description Interval E-value
FOP_dimer pfam09398
FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene ...
 54-134 1.24e-27

FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene partner (FOP) is a centrosomal protein that is involved in anchoring microtubules to subcellular structures. This domain includes a Lis-homology motif. It forms an alpha helical bundle and is involved in dimerization.


Pssm-ID: 312785  Cd Length: 81  Bit Score: 104.17  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720391375  54 KTPLVNENLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFHPETSTIQGLEGRENLAQDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 1720391375 134 R 134
Cdd:pfam09398  81 H 81
LisH_2 pfam16045
LisH;
74-98 1.66e-04

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 38.60  E-value: 1.66e-04
                          10        20
                  ....*....|....*....|....*
gi 1720391375  74 VASLVAEFLQFFNLDFTLAVFHPET 98
Cdd:pfam16045   1 LNSLIAEYLQSQGYNYTLSVFLPES 25
 
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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