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Conserved domains on  [gi|21389391|ref|NP_653201|]
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centrosomal protein 20 isoform 1 [Homo sapiens]

Protein Classification

LisH domain-containing protein( domain architecture ID 1007505)

LIS1 homology (LisH) domain-containing protein similar to Homo sapiens centrosomal protein 20 which is involved in the biogenesis of cilia and required for the recruitment of PLK1 to centrosomes and S phase progression

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
LisH_2 super family cl29685
LisH;
43-113 6.93e-20

LisH;


The actual alignment was detected with superfamily member pfam09398:

Pssm-ID: 475244  Cd Length: 81  Bit Score: 79.13  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389391    43 RPSLSHENL----------LINELIREYLEFNKYKYTASVLIAESGQPVVPLDRQFLIHELNAFEESKDNTIPLLYGILA 112
Cdd:pfam09398   1 KPPLCNENLkkvqstkegrLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 21389391   113 H 113
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 ...
 43-113 6.93e-20

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: 79.13  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389391    43 RPSLSHENL----------LINELIREYLEFNKYKYTASVLIAESGQPVVPLDRQFLIHELNAFEESKDNTIPLLYGILA 112
Cdd:pfam09398   1 KPPLCNENLkkvqstkegrLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 21389391   113 H 113
Cdd:pfam09398  81 H 81
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 52-81 4.37e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 33.56  E-value: 4.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 21389391     52 LINELIREYLEFNKYKYTASVLIAESGQPV 81
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
FOP_dimer pfam09398
FOP N terminal dimerization domain; Fibroblast growth factor receptor 1 (FGFR1) oncogene ...
 43-113 6.93e-20

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: 79.13  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389391    43 RPSLSHENL----------LINELIREYLEFNKYKYTASVLIAESGQPVVPLDRQFLIHELNAFEESKDNTIPLLYGILA 112
Cdd:pfam09398   1 KPPLCNENLkkvqstkegrLVAELIREFLEFFELDYTASVFSPEANLPEEILDRDALSKELNINESDNGKNKPLLHEVVS 80


                  .
gi 21389391   113 H 113
Cdd:pfam09398  81 H 81
LisH_2 pfam16045
LisH;
53-78 2.21e-04

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 37.05  E-value: 2.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 21389391    53 INELIREYLEFNKYKYTASVLIAESG 78
Cdd:pfam16045   1 LNSLIAEYLQSQGYNYTLSVFLPESG 26
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 52-81 4.37e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 33.56  E-value: 4.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 21389391     52 LINELIREYLEFNKYKYTASVLIAESGQPV 81
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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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