ID A0A9P6UT76_9FUNG Unreviewed; 567 AA.
AC A0A9P6UT76;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=mRNA-decapping enzyme subunit 2 {ECO:0000313|EMBL:KAG0319789.1};
GN Name=DCP2 {ECO:0000313|EMBL:KAG0319789.1};
GN ORFNames=BGZ97_001462 {ECO:0000313|EMBL:KAG0319789.1};
OS Linnemannia gamsii.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=64522 {ECO:0000313|EMBL:KAG0319789.1, ECO:0000313|Proteomes:UP000823405};
RN [1] {ECO:0000313|EMBL:KAG0319789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NVP60 {ECO:0000313|EMBL:KAG0319789.1};
RX PubMed=33364917;
RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K.,
RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.;
RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene
RT phylogenetics and phylogenomics.";
RL Fungal Divers. 104:267-289(2020).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG0319789.1}.
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DR EMBL; JAAAIN010000130; KAG0319789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P6UT76; -.
DR OrthoDB; 18996at2759; -.
DR Proteomes; UP000823405; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:InterPro.
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; 1.10.10.1050:FF:000003; Decapping enzyme Dcp2, putative; 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};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000823405};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 94..221
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 206..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..296
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61855 MW; CC1AE00337BBBB21 CRC64;
MAWTNATFDN VLDDLSSRFI INVPDEELAS VERICFQIEQ AHWFYEDFIR EQNPALPSFN
LKSFSAKFFQ HCPLLHEWAN EHETAFANFM EYKIRVPVCG AIILNDAMDK CILVKGWTAR
SGWGFPKGKI NKDEPDTSCA VREVWEETGF DVTEKIRDED YVEQTIKDQR IRLYIIKSVP
ESTVFEPQTR KEISKIEWHY IADLPTSKPK PIEKGTHSGR ESGTERSNGI KNPSRYYMVT
PFVHKLKNWI ITQRRSNKRG NNKGQHNQLA HLQAQGNDSS TSTGSHQQQH SSNRHQTGVP
TVSSSEARLD SEVLKNMLGI GKPVAFSQES TPVHHQQGQH PAHQSPPLSR NARDSSESLK
ALLGIQGGVN MLNADGTATG SPVIQSSTAY SSYPVSMPSS TTSNSSGSVP FQNGSNALKA
MLGIPTQSNS PLLHPSHLAT PHGGSPLMAN AGVAMPHNSN SSNNNNGNRG SHGSNYSPQL
QHASAASSPM RARNGPVDLL ALLKGGGGGA EALQNGNGQY DNGMHQAGAG NGLGSNNNNG
IAPGPGHVSV TKPKTMQNFT FDMEALF
//
