ID A7EU21_SCLS1 Unreviewed; 330 AA.
AC A7EU21;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Decapping nuclease {ECO:0000256|RuleBase:RU367113};
DE EC=3.6.1.- {ECO:0000256|RuleBase:RU367113};
GN ORFNames=SS1G_08828 {ECO:0000313|EMBL:EDN92963.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN92963.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA
CC (By similarity). The NAD-cap is present at the 5'-end of some RNAs and
CC snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G)
CC cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a
CC non-canonical decapping enzyme that removes the entire cap structure of
CC m7G capped or incompletely capped RNAs (By similarity). Has decapping
CC activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated
CC 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose
CC methylated m7G cap (cap1). {ECO:0000256|ARBA:ARBA00025460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-
CC ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphospho-
CC guanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA +
CC H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-
CC COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172876, ChEBI:CHEBI:172877;
CC Evidence={ECO:0000256|ARBA:ARBA00024534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929;
CC Evidence={ECO:0000256|ARBA:ARBA00024534};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-ribonucleoside in mRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000256|ARBA:ARBA00023694};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000256|ARBA:ARBA00023694};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968,
CC ECO:0000256|RuleBase:RU367113};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367113}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family.
CC {ECO:0000256|ARBA:ARBA00006562, ECO:0000256|RuleBase:RU367113}.
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DR EMBL; CH476632; EDN92963.1; -; Genomic_DNA.
DR RefSeq; XP_001590064.1; XM_001590014.1.
DR AlphaFoldDB; A7EU21; -.
DR STRING; 665079.A7EU21; -.
DR GeneID; 5486359; -.
DR KEGG; ssl:SS1G_08828; -.
DR InParanoid; A7EU21; -.
DR OMA; HHHTHEF; -.
DR OrthoDB; 11691at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034353; F:mRNA 5'-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0110155; P:NAD-cap decapping; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0090304; P:nucleic acid metabolic process; IBA:GO_Central.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395:SF9; DECAPPING AND EXORIBONUCLEASE PROTEIN; 1.
DR PANTHER; PTHR12395; DOM-3 RELATED; 1.
DR Pfam; PF08652; RAI1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU367113};
KW Metal-binding {ECO:0000256|RuleBase:RU367113};
KW Nuclease {ECO:0000256|RuleBase:RU367113};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367113};
KW Nucleus {ECO:0000256|RuleBase:RU367113};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW RNA-binding {ECO:0000256|RuleBase:RU367113}.
FT DOMAIN 157..215
FT /note="RAI1-like"
FT /evidence="ECO:0000259|Pfam:PF08652"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 38155 MW; 8C7C9F8E54485503 CRC64;
MNIHKHTHHH THEFNTLPLA QFERTRDAGN TAITRPQEIA HFSYDDSHEF RLDDSSIRWY
YPPDLGTDLN RGFETFRKHD DSKDEHLDSL LRALIEKEKV TNVKTEADVI TWRGMMTKED
HQYKVKTRAR QDARQRPQPG RPSGDAMSFW VYKGSKSEDG KSTEWIELKT TVTPRHRGDE
QNFEKKLLKF WLQSFLLGVP HIIVGKRSPD GILQSIERIN TAQIPGMVKK RGNNSWDGDM
CINFANRFLE FIGDGVWKIR RREKSMAIEV FKTEEVEGHG GILSDEFVEW RNAFNRQTAH
DSHVANNTVQ MNGMNIAAGD APESVLDDVL
//
