ID W2SKB9_NECAM Unreviewed; 323 AA.
AC W2SKB9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=m7GpppX diphosphatase {ECO:0000256|ARBA:ARBA00015636, ECO:0000256|PIRNR:PIRNR028973};
DE EC=3.6.1.59 {ECO:0000256|ARBA:ARBA00012520, ECO:0000256|PIRNR:PIRNR028973};
GN ORFNames=NECAME_15462 {ECO:0000313|EMBL:ETN69187.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN69187.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a
CC residual cap structure following the degradation of mRNAs by the 3'->5'
CC exosome-mediated mRNA decay pathway. {ECO:0000256|PIRNR:PIRNR028973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616;
CC EC=3.6.1.59; Evidence={ECO:0000256|ARBA:ARBA00024271,
CC ECO:0000256|PIRNR:PIRNR028973};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR028973}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000256|ARBA:ARBA00010208,
CC ECO:0000256|PIRNR:PIRNR028973}.
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DR EMBL; KI669153; ETN69187.1; -; Genomic_DNA.
DR RefSeq; XP_013291414.1; XM_013435960.1.
DR AlphaFoldDB; W2SKB9; -.
DR STRING; 51031.W2SKB9; -.
DR EnsemblMetazoa; NECAME_15462; NECAME_15462; NECAME_15462.
DR GeneID; 25355488; -.
DR KEGG; nai:NECAME_15462; -.
DR CTD; 25355488; -.
DR OMA; RAYFHYQ; -.
DR OrthoDB; 5490768at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR Gene3D; 3.30.200.40; Scavenger mRNA decapping enzyme, N-terminal domain; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; HISTIDINE TRIAD HIT PROTEIN MEMBER; 1.
DR PANTHER; PTHR12978:SF0; M7GPPPX DIPHOSPHATASE; 1.
DR Pfam; PF05652; DcpS; 1.
DR Pfam; PF11969; DcpS_C; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF102860; mRNA decapping enzyme DcpS N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR028973};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR028973};
KW Nucleus {ECO:0000256|PIRNR:PIRNR028973};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
FT BINDING 252..263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR028973-2"
SQ SEQUENCE 323 AA; 37213 MW; ACAF63A00FC6990D CRC64;
MKIDGESAVV AVERTTACEE RVQPVEQTAQ EWLRSACFQE ILGSDTTHKS LFVLVEHING
EKGVLLLNKS PFSEKAEDIS AILKSADLTE ILKNDIFGSY DVSIPPHLNV VKSQLVYPAD
DKVIAKYRQE EKFVIRETAE DYLTITVEYI EKYQMNLQWV YNVLSKRKEA ERIIYEDPDP
HNGFILAPDI KWDGIALENL YVLAMIHRRG VRSIRDLTAD DLPMLENLRT QSLTAIREKY
GVRPDQIRAY FHYQPSFFHL HVHFVSLKYD APATTVLSAV LLDDVINNIQ LIPNYYKKAT
LTFTRKASDK LLEMFREAGR CER
//
