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Database: UniProt
Entry: A0A0W8CNX7_PHYNI
LinkDB: A0A0W8CNX7_PHYNI
Original site: A0A0W8CNX7_PHYNI 
ID   A0A0W8CNX7_PHYNI        Unreviewed;       101 AA.
AC   A0A0W8CNX7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN   ORFNames=AM587_10011532 {ECO:0000313|EMBL:KUF85705.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF85705.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF85705.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) 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:KUF85705.1}.
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DR   EMBL; LNFO01002433; KUF85705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CNX7; -.
DR   STRING; 4790.A0A0W8CNX7; -.
DR   EnsemblProtists; KUF85705; KUF85705; AM587_10011532.
DR   OMA; YERHAPE; -.
DR   Proteomes; UP000052943; 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:SF29; 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:KUF85705.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   Transferase {ECO:0000313|EMBL:KUF85705.1}.
FT   REGION          72..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   101 AA;  12116 MW;  EB9B701BE3A6F980 CRC64;
     MTHDLSSRIE YSEKYVDDTH EYRHVILPKE MQRSLPDRLL TETEWRQLGV QQSRGWVHYA
     IHKPEPHILL FRRPLGTDPT TGRVNPEMEK QAKEKYAKEF N
//
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