DXO_DEBHA
ID DXO_DEBHA Reviewed; 385 AA.
AC Q6BLU6; B5RUD9;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Decapping nuclease RAI1 {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q5AAT0};
DE AltName: Full=NAD-capped RNA hydrolase RAI1 {ECO:0000305};
DE Short=DeNADding enzyme RAI1 {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:O13836};
GN Name=RAI1; OrderedLocusNames=DEHA2F10626g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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) (By similarity).
CC {ECO:0000250|UniProtKB:O13836, ECO:0000250|UniProtKB:O70348,
CC ECO:0000250|UniProtKB:Q06349, ECO:0000250|UniProtKB:Q5AAT0}.
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:0000250|UniProtKB:O13836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000250|UniProtKB:O13836};
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:0000250|UniProtKB:P53063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929;
CC Evidence={ECO:0000250|UniProtKB:P53063};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q5AAT0};
CC Note=Divalent metal cation. {ECO:0000250|UniProtKB:Q5AAT0};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53063}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
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DR EMBL; CR382138; CAR66317.1; -; Genomic_DNA.
DR RefSeq; XP_002770792.1; XM_002770746.1.
DR AlphaFoldDB; Q6BLU6; -.
DR SMR; Q6BLU6; -.
DR STRING; 4959.XP_002770792.1; -.
DR EnsemblFungi; CAR66317; CAR66317; DEHA2F10626g.
DR GeneID; 8998938; -.
DR KEGG; dha:DEHA2F10626g; -.
DR VEuPathDB; FungiDB:DEHA2F10626g; -.
DR eggNOG; KOG1982; Eukaryota.
DR HOGENOM; CLU_024877_4_1_1; -.
DR InParanoid; Q6BLU6; -.
DR OMA; MAYWGYK; -.
DR OrthoDB; 1034620at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0110152; F:RNA NAD-cap (NAD-forming) hydrolase activity; IEA:RHEA.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395; PTHR12395; 1.
DR Pfam; PF08652; RAI1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..385
FT /note="Decapping nuclease RAI1"
FT /id="PRO_0000249832"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:O13836"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 224
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:O13836"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:O13836"
FT BINDING 244
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:O13836"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
SQ SEQUENCE 385 AA; 44597 MW; 6D4F4A8EF0E95318 CRC64;
MIKTFPLNSR AKTTALKQPK ELFSFARDID GEYIFDSTKV QDENLSYYYL PDASVDKQID
LGAGYSNFKK IPEEENLGDF PALLKGVMNY EQSTGTKINS DIITFRGLMT KILTLPYNLK
DPLDLHVIVY DGQLFIKNND EIELKRRQQN NQHEDPSKQE MMKKFEYSGY KFEAVSTLPK
PWGDCSRQLI EKRNKKVVNN YEQYISVVKT GIGKVKLLLA GEVDCLWDYI PEDGKDILPH
YVELKTSKVI EAPGQVVNFE KKLFRTWAQS FLIGIRKIVY GFRDDNLILR NVEVYNTEEI
PIMLKDTINV NTKIVCMNAL KWYGAVIEWI NNEIPKDADK SWSLTYDPGS KSFSIVELMQ
DSELRNSVIT EDFKEWRISL HKTES
