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Database: UniProt
Entry: B9WGE9_CANDC
LinkDB: B9WGE9_CANDC
Original site: B9WGE9_CANDC 
ID   B9WGE9_CANDC            Unreviewed;       775 AA.
AC   B9WGE9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Topoisomerase II-associated deadenylation-dependent mRNA-decapping factor, putative {ECO:0000313|EMBL:CAX42323.1};
GN   OrderedLocusNames=Cd36_44510 {ECO:0000313|CGD:CAL0000169672};
GN   ORFNames=CD36_44510 {ECO:0000313|EMBL:CAX42323.1};
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:CAX42323.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX42323.1, 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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
CC   -!- SIMILARITY: Belongs to the PAT1 family.
CC       {ECO:0000256|ARBA:ARBA00009138}.
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DR   EMBL; FM992691; CAX42323.1; -; Genomic_DNA.
DR   RefSeq; XP_002420103.1; XM_002420058.1.
DR   AlphaFoldDB; B9WGE9; -.
DR   GeneID; 8047935; -.
DR   KEGG; cdu:CD36_44510; -.
DR   CGD; CAL0000169672; Cd36_44510.
DR   VEuPathDB; FungiDB:CD36_44510; -.
DR   eggNOG; KOG4592; Eukaryota.
DR   HOGENOM; CLU_012622_1_0_1; -.
DR   OrthoDB; 2786412at2759; -.
DR   Proteomes; UP000002605; Chromosome 4.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR   InterPro; IPR039900; Pat1-like.
DR   InterPro; IPR019167; PAT1_dom.
DR   PANTHER; PTHR21551:SF0; PROTEIN ASSOCIATED WITH TOPO II RELATED-1, ISOFORM A; 1.
DR   PANTHER; PTHR21551; TOPOISOMERASE II-ASSOCIATED PROTEIN PAT1; 1.
DR   Pfam; PF09770; PAT1; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000313|EMBL:CAX42323.1}.
FT   DOMAIN          63..496
FT                   /note="mRNA decay factor PAT1"
FT                   /evidence="ECO:0000259|Pfam:PF09770"
FT   DOMAIN          498..763
FT                   /note="mRNA decay factor PAT1"
FT                   /evidence="ECO:0000259|Pfam:PF09770"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..202
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  87315 MW;  5E5E670456B82399 CRC64;
     MSFFGFDPAA PPQGANQKDD VYDFENTYDG LGELQEDDAF NQETFGTSTS EIRKDFEFSQ
     GESQQSESYA KASAPPAQTI SYAQAATVPV NDDEFMQELW GSSNAPSKNH TDSTEEKTAG
     GQSEKKILSL EEIEAQLTAI DPSQQPPLPQ QQFPPQPYGV PGMMPPPPQF GYMMAPGFMP
     PQYPYPGMIP QQMPPMQQGQ FPPPQPQQQQ QQQQQQPQPQ QQQQTAGPVD KQVSEGPARS
     PASKKTQKVD LSNFPVLGSK EAQSHQQSTP QQQVQSQQQR HHHHYNQHYQ HGHQREPSQE
     LTPEQQEKAA RRQEKVSRIM KYSGIMNPKD KDFVTRFQLS QIVTEDPYNE DFYAQVFKVI
     HPKTINGAQQ STQQNNSIAQ AYLDHSGHRL GGRYKRADVA LQRMQQQVQK AVTVAKERPK
     LTQYAKEGAL GKISFGSGKK PRQQLEIISK AAERQKQENQ IGKKEGVKHY SKKDILSILE
     NIIGELMNVE SESRTRADVD TSKLWESLKV LEQSSSSGDE ESEVNPFIQC LNYNKMLKIL
     LRLFKFLTRE QILTIVTLIM SNLENLLVIK NGSYTTYPNK KVPENIVKLV EAYTLTFSKV
     LMNAVLDFKF NEIIGLLVIL IEHNNVSFVS TTKIGLSILT TLLSRAELII GEGSISATDL
     SEWSSCYDEL FTSLESRIAA IFPPNPEDVD DGSSGENYIW QFLATLSLGG KLSHQRIIVD
     EVRDEIFCVM NRAKAIANTD MANLYKKQNL LNNLNMYLVV MGLVADETEI KELQQ
//
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