NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|5901954|ref|NP_008976|]
View 

centrosomal protein 43 isoform a [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 3.62e-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: 103.02  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901954     54 KTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 5901954    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 3.62e-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: 103.02  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901954     54 KTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 5901954    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 3.62e-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: 103.02  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901954     54 KTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIR 133
Cdd:pfam09398   1 KPPLCNENLKKVQSTKEGRLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 5901954    134 R 134
Cdd:pfam09398  81 H 81
LisH_2 pfam16045
LisH;
74-98 1.29e-05

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 41.68  E-value: 1.29e-05
                          10        20
                  ....*....|....*....|....*
gi 5901954     74 VASLVAEFLQFFNLDFTLAVFQPET 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH