ID A0AAF0J6V2_9BASI Unreviewed; 630 AA.
AC A0AAF0J6V2;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE SubName: Full=5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase {ECO:0000313|EMBL:WFD35593.1};
DE EC=3.6.1.62 {ECO:0000313|EMBL:WFD35593.1};
GN Name=DCP2 {ECO:0000313|EMBL:WFD35593.1};
GN ORFNames=MCUN1_002449 {ECO:0000313|EMBL:WFD35593.1};
OS Malassezia cuniculi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=948313 {ECO:0000313|EMBL:WFD35593.1, ECO:0000313|Proteomes:UP001219933};
RN [1] {ECO:0000313|EMBL:WFD35593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 11721 {ECO:0000313|EMBL:WFD35593.1};
RA Coelho M.A.;
RT "Mating type loci evolution in Malassezia.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR EMBL; CP119879; WFD35593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAF0J6V2; -.
DR Proteomes; UP001219933; Chromosome 3.
DR GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; NUDIX_Dcp2p_Nudt20; 1.
DR FunFam; 3.90.79.10:FF:000003; M7GpppN-mRNA hydrolase isoform 2; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:WFD35593.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001219933};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 119..250
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 288..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..489
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..601
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68372 MW; 6931AA7CFAF11168 CRC64;
MASAQARSCG VCDDATQIWH TLSFPEILEE LSCRFIVNLP ANELTSIERI GFQVEQAHWY
YLDFVRPHNQ TFPQWNLRRF SSELLNVAAN VVPLIRIYTS SGGQHSLEAA YARFVEYKTR
VPVCGAIMLN EDWTKCILVK GWRAKASWTF PGGKINQDES ERDCAVREVK EETGFDCSPL
LAPDSTDYLQ LTMREQRIRL YIVPGVSEKT EMEPMTRHEI SRIEWFTLSD LPTGKKPRTP
SADFGGKFFL IAPFVDRLRQ WINTNKRTHP NRPRKKSQPA AQSVNLDELF GAPSPAPTQN
AVPAQATQAP PQGTVPAPHP MLPNEAPWPA PVPFGGMPVP MRLAPMGPIT PMHQQTPHQH
ALLSILSTPK PPAPSWPAPL PHMPSADWHA PNQPTPQEEQ GRILLANMLG QGADTPREQK
KQSTSVPAST PAPSSAPAST SSAPAPANAP ANAPANAPTS SSASAPASAS TSAPAPQAPR
AASRQQSRQG TPSGTPKPSQ KPVYTHQQPP MLLRPQQSQQ GPDALQQLFG AQAKPPAHPA
PQQVKPPPAQ SAQQTLLNDL LNGPKPDAPP ADDQARATPQ PEQPKQSAQQ SQPAQPAQPA
AQSPPPAQPQ AQAPSPSRAL LTLNRRYSPP
//
