ID A0A316V600_9BASI Unreviewed; 379 AA.
AC A0A316V600;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Scavenger mRNA decapping enzyme {ECO:0000313|EMBL:PWN30855.1};
GN ORFNames=BDZ90DRAFT_229846 {ECO:0000313|EMBL:PWN30855.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN30855.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN30855.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN30855.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819662; PWN30855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316V600; -.
DR STRING; 1569628.A0A316V600; -.
DR OrthoDB; 5490768at2759; -.
DR Proteomes; UP000245884; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245884}.
FT REGION 81..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 314..325
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 379 AA; 41627 MW; 65041190E24B115F CRC64;
MASTSGAEDN NAPAGGAAAF LAGFQLVRVL SQDAKTRSAA LLGTLPAQGD GETVNNGGGE
REQAIVLLEK THFEDSFYSA LGETEGGEKG NGQAAAPEDG RRETKKVKLD RTDGAEDGRH
DTTASSTLST SIQLRNLSDI QSLGHNDIYT WLLARIGSSF VTSPPDVKLT LIRPATSSHI
EKHSAQEKIM VYETPQMYSE KTLPWISAQD PKRIQWVYNI LEGKKEQENV VYRDEDPMMG
FVLLPDLKWD RKTLSSLYLQ AIVQDRSLRS LRDLTPSHSP LLRKIRSVAS QIVAEKYGLG
SVDDQGKKVR CFLHYHPSYY HLHVHVLSAD YTSHAGAIVG QAHLLDDVID LLELGVEMKQ
RTIGCALGAR HELLGVLRG
//
