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Database: UniProt
Entry: A0A2T4CH85_TRILO
LinkDB: A0A2T4CH85_TRILO
Original site: A0A2T4CH85_TRILO 
ID   A0A2T4CH85_TRILO        Unreviewed;       511 AA.
AC   A0A2T4CH85;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=A/B/D/E cyclin {ECO:0000313|EMBL:PTB80882.1};
GN   ORFNames=M440DRAFT_63059 {ECO:0000313|EMBL:PTB80882.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB80882.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB80882.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB80882.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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DR   EMBL; KZ679126; PTB80882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4CH85; -.
DR   STRING; 983965.A0A2T4CH85; -.
DR   Proteomes; UP000240760; 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; 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; 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:SF587; S-PHASE ENTRY CYCLIN-5-RELATED; 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:UP000240760}.
FT   DOMAIN          282..366
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          375..489
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          379..460
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  56457 MW;  282B5727B5B8EE0E CRC64;
     MPPGRPRTRV VSNENDENST TTRMTRAKSA ALNVSDSAVP SKAGLQTKKT VGVTTSNGLR
     KRAALGDVSN VSKTEVVEAK KVTASKGLVS KAAAPTGIQK STRPTAGRTA LSSKELKKPE
     VKKSGAGTIG PKRKVPTAAP KEETVPEAAE PARKRAHLDA EKRVRAEVVD VENKAPAPAT
     TKSAPVKSAP VKSAPVKAAP AKAAPAKAAP PQLDPKEAAK AELLANIKSL DEEDLDDPLM
     VAEYANDIFE YLRELEVQSI PNPDYMSHQD DLEWKTRGIL IDWLIEVHTR FHLLPETLFL
     AVNIIDRFLS EKVVQLDRLQ LVGITAMFIA SKYEEVLSPH VENFKKIADD GFSEAEILSA
     ERFILSTLNY DLSYPNPMNF LRRVSKADNY DIQSRTIGKY LTEISLLDHR FMVYRPSHVA
     AASMYLARLM LDRGEWDPTI AYYAGYTEDE VEPVVNLMVD YLARPPIHEA FFKKYASKKF
     LKASILSRQW AKKNAPLFGI EDLHLSLDEI S
//
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