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Database: UniProt
Entry: A0A319EGY9_ASPSB
LinkDB: A0A319EGY9_ASPSB
Original site: A0A319EGY9_ASPSB 
ID   A0A319EGY9_ASPSB        Unreviewed;       418 AA.
AC   A0A319EGY9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=G1/S-specific cyclin {ECO:0000313|EMBL:PYI05808.1};
GN   ORFNames=BO78DRAFT_142044 {ECO:0000313|EMBL:PYI05808.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI05808.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI05808.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI05808.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|ARBA:ARBA00008742, ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KZ826355; PYI05808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EGY9; -.
DR   STRING; 1448318.A0A319EGY9; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd20537; CYCLIN_CCNO-like_rpt2; 1.
DR   CDD; cd20559; CYCLIN_ScCLN_like; 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; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF523; G1_S-SPECIFIC CYCLIN CLN1-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 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:UP000248423}.
FT   DOMAIN          97..183
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          192..299
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          196..276
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
SQ   SEQUENCE   418 AA;  47288 MW;  5682A00CED4AEE07 CRC64;
     MVYQKRPTSS YQPCDTFFVE SYDEFPAPRM DPKEHAKLMA RERQYAMAEQ LSKVASDEFR
     DDVLAHMLDM DAATLPDVES IDIQTEIQWF MRPYLLDFLI EAHTAFQLLP STLFLTINLL
     DRYCSKRVVY KRHYQLVGCA ALLIASKYGD KKDRVPTIKE LKSMCCSLYD DDMFIQMEWH
     VLQTLGWTIG HPTVDNFLQM AVMDCAYDAE VEHLALYISE ISLFHREFVS KPSSDLARAS
     LALARCILNR TQPRHTEWAS QYDSMTLVGL SQQLHQPSQV LSRKYSSAHY SRVSKVLEQF
     LARQASIASY TPPSPQTEVV QPEPKPYEGE IGLATPQKAT QSSSAMAHGY ITPPITPENE
     VFANGGNPTF VKGAAASACS PSPTPPSMQY VSSHAYTQET TTYPQQFLQP NMSFSTGY
//
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