ID   A0A1I7TE16_9PELO        Unreviewed;       779 AA.
AC   A0A1I7TE16;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Nudix hydrolase domain-containing protein {ECO:0000313|WBParaSite:Csp11.Scaffold589.g5015.t1};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold589.g5015.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold589.g5015.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I7TE16; -.
DR   STRING; 1561998.A0A1I7TE16; -.
DR   WBParaSite; Csp11.Scaffold589.g5015.t1; Csp11.Scaffold589.g5015.t1; Csp11.Scaffold589.g5015.
DR   eggNOG; KOG2937; Eukaryota.
DR   Proteomes; UP000095282; Unplaced.
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   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          209..337
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  87945 MW;  3CD20EDDC623F5C0 CRC64;
     MASNNTNAKK MNKKPEEPSN VQKLLASLQQ AQNKVIGETS EPSTSKPKKH EKRKKNFEEK
     RKTKTGSVGA RMQQQAENAR MQAKRPRHIS SSKSGARNPS GLDYSQQPTT QHQQHRGPRI
     PADILDELEF RFISNMVDYE INDDIRVCFH LELAHWYYID HMVEDDKYTN CPNVGSRDFT
     VQMCQHCSVL RKYAHRADEV IAKFREYKST VPTYGAILIE PEMEYVLLVQ SYFSKGNNWG
     FPKGKINQNE PPRDAAIRET FEETGYDFGI NSEREKKFQR FINDILVRLY LVKNVPKDFN
     FQPQTRKEIR KIEWFKIADL PTDKTDEIPA YLHGNKFFMV IPFVKDIQLY VQKEKEKMKR
     RKVETRNMNV ASPKQTPAQS SVLSQLFSTT TQTNPPTHPV YKRLTSEELL SAFKKQENES
     SSTIARPTLP EMSPAVNGLD SLAVLGICTP LKPGASLNQF SASESCPMIS EEISSPKQIF
     SSDTEAEIGF AMPTDLKQPV VTTDHPWQHN KSSESNAAPP ELVSHQGWLD TQLVNTIMQS
     PNPPIPSSNS PATPTTVLGH LIGKPIQPQA IFPQAATPTA FGSAEKPKSS RINLSDNSAF
     KAINSSQKQS VPKATAPPGS TKTRSASLSG SQKTDNRKAA RNLFNSVTSP VSSGDPEYGD
     EPSMWEEVWF REQFAATAGT SISSLAASNQ ELAMINRETP IEDRNPSMKI VYQKLPNQLK
     QDLIPNCQQW TKRIQFDTEF IAGPLSLWTQ QFSLKDKTLS AENNVLKRRE TEEFSYQSK
//