ID B9WJ30_CANDC Unreviewed; 474 AA.
AC B9WJ30;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Histone deacetylase complex subunit, putative {ECO:0000313|EMBL:CAX41250.1};
GN OrderedLocusNames=Cd36_63730 {ECO:0000313|CGD:CAL0000169854};
GN ORFNames=CD36_63730 {ECO:0000313|EMBL:CAX41250.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX41250.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX41250.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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DR EMBL; FM992693; CAX41250.1; -; Genomic_DNA.
DR RefSeq; XP_002421092.1; XM_002421047.1.
DR AlphaFoldDB; B9WJ30; -.
DR GeneID; 8048873; -.
DR KEGG; cdu:CD36_63730; -.
DR CGD; CAL0000169854; Cd36_63730.
DR VEuPathDB; FungiDB:CD36_63730; -.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_020879_1_0_1; -.
DR OrthoDB; 5491784at2759; -.
DR Proteomes; UP000002605; Chromosome 6.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47793; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR PANTHER; PTHR47793:SF1; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR Pfam; PF20826; PHD_5; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 60..127
FT /note="Zinc finger PHD-type"
FT /evidence="ECO:0000259|SMART:SM00249"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 54546 MW; EF3BF8B88A54CDAE CRC64;
MSRKSGRRGY NSDTTTSSHR GGGGGGRERQ EEDIVDLEEE EEEEEEEELI EDGEEDEITR
CICGQDELTN DSINPELSTF LKKTYKIEID QGLFIQCEKC SVWQHGYCVG LFESQDVPDE
YWCESCKPEF HILVNNDGYS KRTLYKPVND KRKKLEQMTF KNNETSHNST RRRGVKNERN
VPQQEIMSNT KDKRKERRHH HHHHNIDEDD DEYNEQLKRA LRESARESGV KLSESESNEK
GNGNSVKRED NKSDGNNSSG RESSRGNGSG SRKRETSRRD DDSNDSKRLK VERLDHPSGS
ELNENSEQEL MSGSEESRSR RRGGATSKTA RQKKKKSTPP RSSANNNNKK QDDSSNETNS
LGPTKEELIQ QPSKPRYVND KSSIFELRKR TIAILEWLGR SQVELQEEKQ QKLELFSFIS
DDDEKEGSTN SKENVNSNAD TLALKETFDE NLLLMEQLTE RILAWQDTFG KYAV
//
