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Database: UniProt
Entry: A0A139IIH0_9PEZI
LinkDB: A0A139IIH0_9PEZI
Original site: A0A139IIH0_9PEZI 
ID   A0A139IIH0_9PEZI        Unreviewed;       605 AA.
AC   A0A139IIH0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXT14392.1};
DE   Flags: Fragment;
GN   ORFNames=AC579_2758 {ECO:0000313|EMBL:KXT14392.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT14392.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT14392.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT14392.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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:KXT14392.1}.
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DR   EMBL; LFZO01000084; KXT14392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IIH0; -.
DR   STRING; 113226.A0A139IIH0; -.
DR   Proteomes; UP000073492; 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; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
DR   CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 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:SF587; S-PHASE ENTRY CYCLIN-5-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:UP000073492}.
FT   DOMAIN          380..464
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          473..587
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          477..558
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KXT14392.1"
SQ   SEQUENCE   605 AA;  67139 MW;  C0E9A888888B07FE CRC64;
     SSTQHRPASA PAPAPAPARD ALSRKHSSTS RLRLLHPKPP TITITITTIP AQYHHHHHPP
     LHTVSVTGLE SCETSYCQHL HSRRQPSPSA SRTIHPPHHT STSHTMPPAR TVRRTVTDEN
     ADATGTTRLT RAKAAALETT SAGDPPKKAL TTTTRPPTTT NAALAARKRT ALGDVSNVAK
     KEPLAEKGNA KDTLSKATLS KAAKPAGIQK QPARSTSTRT ALGPKTSNNA SSELKRPHSG
     SGIATGPTSK KRNTSSTKPK RAAVVEDDLD DDDAENVPPP PPTNGAKSKV EKRPSVKSML
     SEPIELDDDN SYEQEKSLEQ LIKEAKDLDT EDLDDPLMVA EYVHEIFDYM KDLEIATLPS
     PNYMDNQGEL EWKMRGILVD WLLEVHARFR LLPETLFLAV NIIDRFLSCK VVQLDRLQLV
     GVTAMFIASK YEEVLSPHVQ NFVHVADDGF KDTEILSAER FVLSTLDYDL SYPNPMNFLR
     RISKADNYDI QTRTLGKYLL EIGCLDHRFL KYPPSQVAAA AMYLARLALD RGEWDATLAK
     YAGYTEADIQ PVFKLMVDYL YSPVVHEAFF RKYASKKFLK ASIVLRQWAK KWAPTYLDNV
     KAPRS
//
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