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Database: UniProt
Entry: A0AAF0IHA3_9EURO
LinkDB: A0AAF0IHA3_9EURO
Original site: A0AAF0IHA3_9EURO 
ID   A0AAF0IHA3_9EURO        Unreviewed;       315 AA.
AC   A0AAF0IHA3;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=Decapping enzyme Dcp1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PRK78_001869 {ECO:0000313|EMBL:WEW56426.1};
OS   Emydomyces testavorans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Nannizziopsiaceae; Emydomyces.
OX   NCBI_TaxID=2070801 {ECO:0000313|EMBL:WEW56426.1, ECO:0000313|Proteomes:UP001219355};
RN   [1] {ECO:0000313|EMBL:WEW56426.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16-2883 {ECO:0000313|EMBL:WEW56426.1};
RA   Hoyer L.;
RT   "Emydomyces testavorans Genome Sequence.";
RL   Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DCP1 family.
CC       {ECO:0000256|ARBA:ARBA00008778}.
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DR   EMBL; CP120627; WEW56426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAF0IHA3; -.
DR   Proteomes; UP001219355; Chromosome 1.
DR   GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR   GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IEA:TreeGrafter.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd13182; EVH1-like_Dcp1; 1.
DR   FunFam; 2.30.29.30:FF:000444; Decapping enzyme Dcp1, putative; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010334; Dcp1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR16290:SF0; DECAPPING PROTEIN 1, ISOFORM A; 1.
DR   PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR   Pfam; PF06058; DCP1; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Reference proteome {ECO:0000313|Proteomes:UP001219355}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  34611 MW;  9B7FC35ECF04E558 CRC64;
     MTLRKTRVNP QRQSRHQHAL SASSINNIQP SDYESDIQNY ALQENQMATS PPANPPPTRS
     NEDLNITVVR RYNPSISTIL SLAPFAVVYI FSATTQLWEK TGIEGTLFVC QLTKGEQGEE
     RYSVMVLNRR GMDNFEANLC NGDDVELTDE YVILKVDGLE KGYKGATRSA DERSSVIYGL
     WIFSEPAPSS TAETRTLNAQ MLKECAIHAG ESKKLAEERA AAERSQSAHA EEASGSVPMN
     RQFSLKDLFG QQRAQDDAWS VKVHSAVNEL DPQALLQPAA NQPGGWHVPP GDPEGKASNG
     NDVLGNLFRK AGLGH
//
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