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Database: UniProt
Entry: A0A0L6X386_9AGAR
LinkDB: A0A0L6X386_9AGAR
Original site: A0A0L6X386_9AGAR 
ID   A0A0L6X386_9AGAR        Unreviewed;       311 AA.
AC   A0A0L6X386;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=Scavenger mRNA-decapping enzyme DcpS {ECO:0000313|EMBL:KNZ82033.1};
GN   ORFNames=J132_08378 {ECO:0000313|EMBL:KNZ82033.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ82033.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208}.
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DR   EMBL; KQ412175; KNZ82033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6X386; -.
DR   STRING; 1306850.A0A0L6X386; -.
DR   OrthoDB; 5490768at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT   BINDING         238..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ   SEQUENCE   311 AA;  35184 MW;  C85D85B5C8F7F259 CRC64;
     MSHPAAPTNL NKLKYFQFDK VINEDPLTHS LTLLGTFPSP DEVQDRVTAI VRVEKTALDA
     GTAEHLFAAD GLVRRVALEE STDIYTWLFG WLGEERERDI KINIVCPATE VHICKYTRQN
     IVMVRETPDL YGSIVKPYIT AFPKSRTQWV ENILLGLSEQ DKILFSSPDF VILPDMKWDL
     KTISSLYLVA LVQDRGIRSL RDLRKQHIPL LKAIRSEGER VVEEKWALGK GAVRMYIHYQ
     PSYYHFHVHI VNANQVGMVG MAVGQAHLLD NVISLLEIES ENGPATFERI VLTYGLGDQH
     GLFEAMQAAS A
//
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