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Database: UniProt
Entry: C6HRT2_AJECH
LinkDB: C6HRT2_AJECH
Original site: C6HRT2_AJECH 
ID   C6HRT2_AJECH            Unreviewed;       672 AA.
AC   C6HRT2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Cyclin {ECO:0000313|EMBL:EER37216.1};
GN   ORFNames=HCDG_08667 {ECO:0000313|EMBL:EER37216.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER37216.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC       regulatory module of the Mediator complex which is itself involved in
CC       regulation of basal and activated RNA polymerase II-dependent
CC       transcription. The SRB8-11 complex may be involved in the
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC       It may inhibit the association of the Mediator complex with RNA
CC       polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC       phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC       RNA polymerase II. {ECO:0000256|ARBA:ARBA00025278}.
CC   -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the
CC       Mediator complex. {ECO:0000256|ARBA:ARBA00011612}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; GG692436; EER37216.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HRT2; -.
DR   STRING; 544712.C6HRT2; -.
DR   VEuPathDB; FungiDB:HCDG_08667; -.
DR   eggNOG; KOG0834; Eukaryota.
DR   HOGENOM; CLU_022000_7_2_1; -.
DR   OMA; TAYYMAT; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20545; CYCLIN_SpCG1C-like_rpt1; 1.
DR   CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF51; CYCLIN-K; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          62..168
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          181..268
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          283..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..510
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  75729 MW;  B3E38DDC2EC71204 CRC64;
     MPATTSSSTR EPAHSVLMPS NPVLVAAQSQ WIFTDAELYR TPSVLDGMAI EAEHTSRSKG
     VNFITQVGIL LKLPQLTLCT ASVYLHRFFM RYSMKDLPQR PGMHPYSVAA TALFLATKVE
     ENCRKMKELI VACCRIAQKK PSMIVDEQSK EFWRWRDTIL HNEDLLLEAL CFDLQLEQPY
     RLLYDFLCYF KVQENKRLRN SAWAFLNDST YTVLCVQFPA RTIAAAALYA AARHCEVAFE
     DDSLNRPWWR QLDVDLHEMR RACNRMADIY EFVSVPVPGQ QYVHLSTRDD EPTDMTRTSY
     HPKSEGSIDD SANNSMSPGE INGRKRERDS HSGSFSQHPI SIPPNGATSG EPDPQPSPKR
     QRREGSEGDT ETSSFSQPQQ PSSSQISLTE ATANMNVASN SSSQTAISIP SSQKQPEMNG
     HGHPRNVSPS KSRIPQAARI PLNQPRQEHP LPPPPPVTVP PLPHQQPQPP RRGSYSNNPQ
     PPNRQPPPRG PPPATVSSMF HLPPPPADPS NVDKLQQRID AIIQQGMPQE NDRSHEPRGN
     YYYHPSSSER DRDRDRDRHR ERDRYRDNDR DKDMARERGR DHDRDHGIDH HGRSRRHSSE
     TSGPGAMSTS LPTLPPQQSV APPVPSSEPR HDLEQDQQIK RDVVGTNTAS LQDHDTKTNE
     ADDDGGSEEG EL
//
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