ID B9WK08_CANDC Unreviewed; 303 AA.
AC B9WK08;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Non-essential hydrolase involved in mRNA decapping, putative {ECO:0000313|EMBL:CAX40659.1};
GN OrderedLocusNames=Cd36_71050 {ECO:0000313|CGD:CAL0000168531};
GN ORFNames=CD36_71050 {ECO:0000313|EMBL:CAX40659.1};
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:CAX40659.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40659.1, 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 {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
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DR EMBL; FM992694; CAX40659.1; -; Genomic_DNA.
DR RefSeq; XP_002421325.1; XM_002421280.1.
DR AlphaFoldDB; B9WK08; -.
DR GeneID; 8049292; -.
DR KEGG; cdu:CD36_71050; -.
DR CGD; CAL0000168531; Cd36_71050.
DR VEuPathDB; FungiDB:CD36_71050; -.
DR eggNOG; KOG3969; Eukaryota.
DR HOGENOM; CLU_041045_1_0_1; -.
DR OrthoDB; 5490768at2759; -.
DR Proteomes; UP000002605; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR Gene3D; 3.30.200.40; Scavenger mRNA decapping enzyme, N-terminal domain; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; HISTIDINE TRIAD HIT PROTEIN MEMBER; 1.
DR PANTHER; PTHR12978:SF0; M7GPPPX DIPHOSPHATASE; 1.
DR Pfam; PF05652; DcpS; 1.
DR Pfam; PF11969; DcpS_C; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
DR PROSITE; PS00892; HIT_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:CAX40659.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 227..238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 303 AA; 35131 MW; 4C5498E391DB364C CRC64;
MSLNELVSQF RFTRVLKSDS QTKTISILGK INNKDAIVTI EKSHFSTGSD LDLQKLITDL
SIINSNDVYY WSTANLFQDV LELPGAKLNL IYPATETHIR KYDDQKLHYV RETPEMYQKY
VVPYIETMKG DRLKWVYNIL FEGKESETFI YHDKSPTGFV LLPDMKWDGK NLDTLYLCCI
VNRLDISCVR DLNQSHIAYL SNLQKIVKEV TVNKYGIKPD QLRVFLHYQP SYYHFHLHIV
NVQHPGLGDG IAIGKAILLD DVIDNLKLDG SYYSEKTIGF VLGENHGLWQ IEGYRDLHFK
QKN
//
