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Database: UniProt
Entry: A0A1J9RL95_9PEZI
LinkDB: A0A1J9RL95_9PEZI
Original site: A0A1J9RL95_9PEZI 
ID   A0A1J9RL95_9PEZI        Unreviewed;       115 AA.
AC   A0A1J9RL95;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN   ORFNames=BKCO1_8500019 {ECO:0000313|EMBL:OJD29279.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29279.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD29279.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29279.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC       kinases and is essential for their biological function.
CC       {ECO:0000256|RuleBase:RU311113}.
CC   -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|ARBA:ARBA00007782,
CC       ECO:0000256|RuleBase:RU311113}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJD29279.1}.
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DR   EMBL; MNUE01000085; OJD29279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RL95; -.
DR   STRING; 236234.A0A1J9RL95; -.
DR   OrthoDB; 204504at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR   InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR   InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR   PANTHER; PTHR23415:SF48; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23415; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT/60S RIBOSOME SUBUNIT BIOGENESIS PROTEIN NIP7; 1.
DR   Pfam; PF01111; CKS; 1.
DR   PRINTS; PR00296; CYCLINKINASE.
DR   SMART; SM01084; CKS; 1.
DR   SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR   PROSITE; PS00945; CKS_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU311113};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   ECO:0000256|RuleBase:RU311113}; Kinase {ECO:0000313|EMBL:OJD29279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW   Transferase {ECO:0000313|EMBL:OJD29279.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   115 AA;  13843 MW;  1C5503D258BC1199 CRC64;
     MDMGIDITRR NKKPRPLSEA EKDKLDEFVE SIHYSARYSD SEHEYRHVQL PKQMLKVIPK
     EYFDGSRGTL KLLWEEEWRA LGITQSLGWE HYEVHEPEPH ILLFKRPINY QPPMH
//
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