ID X0CVC6_FUSOX Unreviewed; 834 AA.
AC X0CVC6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=FOQG_03636 {ECO:0000313|EMBL:EXK94814.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK94814.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK94814.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK94814.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR EMBL; JH658366; EXK94814.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CVC6; -.
DR eggNOG; KOG2937; Eukaryota.
DR HOGENOM; CLU_008108_4_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; Dcp2p; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 95..231
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 364..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 90874 MW; BAA0FD6F791648C8 CRC64;
MSGSQMQLED WLDDLCVRFI INLPQEDLSS VARICFQVEE AQWFYEDFIR PLDPTLPSMT
LRTFCLRIFQ HCPLLASFSV ENHTKAFEEF LEYKTRVPVR GAIMLNEAMD STVLVKGWKK
GANWSFPRGK INKDEDDLDC AVREVYEETG LDLRAAGLVP TEHKPKYIEI SMREQHMRLY
VFRDVPMDTV FEPKTRKEIS KIQWYKLSEL PAFRRKNGQA NDANTAPNAN KFYMVAPFLV
PLKKWVMAQK KIEARRAANS SQGYGPISEA QYEDEAWNDT GAETTDQGPA IETLAGATQE
LQRLLKVQPP TQGLQGVSAP ALAQQDKGSA LLSILQAKDG PPNAMPQAGA HYPQTPLDHT
VTNAPQPHTP HHHNLHQMPS TNTQQPPPPF PYAPNQGAHW NMGLGQQVGN LQLYNQQYSI
QEGQYKSNQA PLVHPQPLPP QVERAVFNRS VFQDVNQPNH NPPVPGQFLN QQQAQYGHPG
QMPQQPLNAP GQPRPQPLNG QSMALLNAFK GGNTAPQVQQ KPQQAPFPPG FPAQSQGPMY
SNLGGVQAQQ VLQQVPHAAG PVGGQDRSGP SPKELPGSKV GPPADNHRSA LLGMFRKDDQ
NQPPAQGPQP AGQPAPGSMM SELLRSVGGD NFRANIPQQA PADPNPLPSM DGLSLQQRPT
QTGTPGSHGT ADYSQQYGAQ AHAPAASQPT QPIRILQRGQ GEQLFGIGGA SASPQTSFAS
PSGLSSHLQP AGAGISPSIA QAFPAVNRRR ESGPAQKREL LSLFGKQPSP ASLEAAKGKE
VIAGTPRSRL ASLASGVEDP AGPPSRRGSQ TPISPAERTF LLDYLQSVTK NANH
//
