ID DCPS_SCHPO Reviewed; 304 AA.
AC Q9P7C9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=m7GpppX diphosphatase;
DE EC=3.6.1.59 {ECO:0000269|PubMed:12366830};
DE AltName: Full=Hint-related 7meGMP-directed hydrolase 1;
DE AltName: Full=Nuclear histidine triad (HIT) motif protein 1;
DE AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
GN Name=nhm1; Synonyms=dcps; ORFNames=SPBP4H10.20;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PROTEIN SEQUENCE OF 95-101 AND 127-145, FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12366830; DOI=10.1046/j.1365-2958.2002.03151.x;
RA Salehi Z., Geffers L., Vilela C., Birkenhaeger R., Ptushkina M.,
RA Berthelot K., Ferro M., Gaskell S., Hagan I., Stapley B., McCarthy J.E.G.;
RT "A nuclear protein in Schizosaccharomyces pombe with homology to the human
RT tumour suppressor Fhit has decapping activity.";
RL Mol. Microbiol. 46:49-62(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. Hydrolyzes cap analog structures
CC like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10
CC nucleotide substrates (small capped oligoribonucleotides) and
CC specifically releases 5'-phosphorylated RNA fragments and 7-
CC methylguanosine monophosphate (m7GMP). Has no activity towards mRNA
CC molecules longer than 25 nucleotides. May also play a role in the 5'->3
CC mRNA decay pathway; m7GDP, the downstream product released by the
CC 5'->3' mRNA mediated decapping activity, may be also converted by DCS1
CC to m7GMP. Inhibits mRNA translation. Binds to the m7GpppG cap analog.
CC {ECO:0000269|PubMed:12366830}.
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:0000269|PubMed:12366830};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000305}.
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DR EMBL; CU329671; CAB83178.1; -; Genomic_DNA.
DR RefSeq; NP_596194.1; NM_001022113.2.
DR AlphaFoldDB; Q9P7C9; -.
DR SMR; Q9P7C9; -.
DR STRING; 284812.Q9P7C9; -.
DR MaxQB; Q9P7C9; -.
DR PaxDb; 4896-SPBP4H10-20-1; -.
DR EnsemblFungi; SPBP4H10.20.1; SPBP4H10.20.1:pep; SPBP4H10.20.
DR GeneID; 2541340; -.
DR KEGG; spo:SPBP4H10.20; -.
DR PomBase; SPBP4H10.20; nhm1.
DR VEuPathDB; FungiDB:SPBP4H10.20; -.
DR eggNOG; KOG3969; Eukaryota.
DR HOGENOM; CLU_041045_1_0_1; -.
DR InParanoid; Q9P7C9; -.
DR OMA; HVHINPI; -.
DR PhylomeDB; Q9P7C9; -.
DR Reactome; R-SPO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:Q9P7C9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0140932; F:5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1..304
FT /note="m7GpppX diphosphatase"
FT /id="PRO_0000362149"
FT MOTIF 242..246
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235..246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 304 AA; 35107 MW; B845332DC767FD96 CRC64;
MEESSAAKIQ LLKEFKFEKI LKDDTKSKII TLYGKIRNEV ALLLLEKTAF DLNTIKLDQL
ATFLQDTKLV ENNDVFHWFL STNFQDCSTL PSVKSTLIWP ASETHVRKYS SQKKRMVCET
PEMYLKVTKP FIETQRGPQI QWVENILTHK AEAERIVVED PDPLNGFIVI PDLKWDRQTM
SALNLMAIVH ATDIASIRDL KYKHIPLLEN IRNKVLTEVP KQFSVDKNQL KMFVHYLPSY
YHLHVHILHV DHETGDGSAV GRAILLDDVI DRLRNSPDGL ENVNITFNIG EQHFLFQPLT
NMNA
//
