ID A0A517LNQ2_9PEZI Unreviewed; 1121 AA.
AC A0A517LNQ2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 02-APR-2025, entry version 21.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=FKW77_002837 {ECO:0000313|EMBL:QDS77216.1};
OS Venturia effusa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Venturiaceae; Venturia.
OX NCBI_TaxID=50376 {ECO:0000313|EMBL:QDS77216.1, ECO:0000313|Proteomes:UP000316270};
RN [1] {ECO:0000313|EMBL:QDS77216.1, ECO:0000313|Proteomes:UP000316270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=albino {ECO:0000313|Proteomes:UP000316270};
RA Young C.A., Cox M.P., Ganley A.R.D., David W.J.;
RT "Finished genome of Venturia effusa.";
RL Submitted (JUL-2019) 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; CP042201; QDS77216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A517LNQ2; -.
DR STRING; 50376.A0A517LNQ2; -.
DR OrthoDB; 18996at2759; -.
DR Proteomes; UP000316270; Chromosome 17.
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; 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:UP000316270};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 94..227
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 285..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..298
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..499
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..627
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1066
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 122594 MW; 0C15E5330ED5C1D3 CRC64;
MTEKKMQLAD WLDDLSARFI INCPPEELIS QGRLCFQIEE AQWFYEDFIR PLDPKLPSKD
LRTFCADMFR HCPILAPYSD QADEVYTAFM AYKTRVPVRG AIMLNHNMDS VVLVRGWKAS
SQWGFPRGKI NKDEKDLHCA IREVYEETGF DIQAAGLVPE DEEHAKYIRM NLRGQDISLY
VFRSVPEDTS FEPRTRKEIG KIDWFKIDNL PTQKKSQQFV LSKGGDSVKE SGFYHVAPFL
RPLKAWVNEQ RRLDKQHQRA LKRTTIVLEE DTTEAEEEIL YADGESADED PVEFEDTDAQ
FPTPSPSQPK FARPSGEEHT SHFDRLLSGL TSNPEREQVE PANLPEVSGA HATTEDLATA
LKRMLSVGGP SQGAALPQMP YTAPQEKEAM ANPLLNILRG PQHPAPATSL PPRTPADQIL
PTPDAARTPH HNHPRQPQFP MGPPPDYGLH PGHGQPVQHP HHPQGPRPFP QQQHQLPFGH
GPSQNGQPQY QNQMQAAQSF PYRGSSNFRA GLPHAAQTPS NPGPLAEHRM PPVGHPHPSG
PYQQSADSQS APLYSQYGHN IAIPSASKLP PPKLTSHALN LLSVFKSPAA QNAHLVHPIH
MNRPSVSGLE VPEPRAPPQQ SAPSSHARPV KLSSPELAQP QAQKPRNPHQ DSLLNLFRSP
STPAIPAPIP PPSQQRREPV ELSAQSSPHI GHMRNTSGHQ HSIQEAQQVQ QVHHKLSMRR
LPNLDTQSPH NIRQSPGLTS ATVSGPLNAP DFASVRKNQK PAELGTGTSP STGTPPHQPQ
GFQPKAILSR TPHRQHQQQH LRMAPPPLSQ TPPVPVHTVN GKTAMEAPRP FHPLSILKRQ
EEGMPGENES KPESQQPLRM LPGAVPLIPK SQVGHQPPPM LPGAVPLVPK NQMGPPPPYH
QQEQPVLQRE NSFDRRDIAP ADQKSALLGL FAAKSTSSKP KTSTYSQVAA SIPAPDDKRQ
QLLSLFGSAK SVATSNAQNL GHVGSATISA RPGNASSVNS PVSPLPAHAA PVRSDSYNSA
PTSAPNSVPL PNPNVDSGVS AIRASIGGHN ESNPRSRISS IASIPSVEQG RSSRKAPHPL
SGNTEGGSGT QSPITPKEKG FLLDYLMGVA KEGDRNANTV R
//
