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Database: UniProt
Entry: A0A1R2CSW0_9CILI
LinkDB: A0A1R2CSW0_9CILI
Original site: A0A1R2CSW0_9CILI 
ID   A0A1R2CSW0_9CILI        Unreviewed;       294 AA.
AC   A0A1R2CSW0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OMJ92053.1};
GN   ORFNames=SteCoe_5257 {ECO:0000313|EMBL:OMJ92053.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ92053.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ92053.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ92053.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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:OMJ92053.1}.
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DR   EMBL; MPUH01000069; OMJ92053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CSW0; -.
DR   OrthoDB; 994264at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR   CDD; cd20507; CYCLIN_CCNB1-like_rpt1; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF583; G2_MITOTIC-SPECIFIC CYCLIN-A; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT   DOMAIN          90..174
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          183..292
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          187..262
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  34486 MW;  19C8DC8A6C19089E CRC64;
     MLENKPTQEN TAKPEKPPLQ VLTRPPLQNL SYENLPQPIA ISTQNPQLVK IYSNEIFEFL
     EATEEETLIK GDYFLLHTEI NHTSRAFLID WLVNIHAKFK LYQETLYITV NLIDRYLSKR
     MVTKKQLQLV GVTAMFIASK YEEIYPPNAR DFLMTTDQAY SKQHLLKMEV DMLKVINFHI
     TFPTAWRFME KYPELFHNGA GILAEYLLEL GLIEYMMIKY RPSIQAAAVI CLANFLQNKS
     FTWKAEDPNE SLIKECVKDF YKIFKSSSNH PLTSVREKYM RKKLDVVRLE EDAQ
//
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