ID A0A452FUS9_CAPHI Unreviewed; 462 AA.
AC A0A452FUS9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=NAD-capped RNA hydrolase NUDT12 {ECO:0000256|ARBA:ARBA00023869};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
DE AltName: Full=NADH pyrophosphatase NUDT12 {ECO:0000256|ARBA:ARBA00030313};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 12 {ECO:0000256|ARBA:ARBA00031178};
GN Name=NUDT12 {ECO:0000313|Ensembl:ENSCHIP00000027892.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000027892.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000027892.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000027892.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC EC=3.6.1.22; Evidence={ECO:0000256|ARBA:ARBA00001758};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC Evidence={ECO:0000256|ARBA:ARBA00001758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC ChEBI:CHEBI:456215; EC=3.6.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000053};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869;
CC Evidence={ECO:0000256|ARBA:ARBA00000053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = adenosine 2',5'-bisphosphate + 2 H(+) + reduced
CC beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:60820,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:90832, ChEBI:CHEBI:194156;
CC Evidence={ECO:0000256|ARBA:ARBA00034999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821;
CC Evidence={ECO:0000256|ARBA:ARBA00034999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC ChEBI:CHEBI:144051; Evidence={ECO:0000256|ARBA:ARBA00023679};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000256|ARBA:ARBA00023679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000256|ARBA:ARBA00004463}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000256|ARBA:ARBA00009595}.
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DR EMBL; LWLT01000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005683532.1; XM_005683475.3.
DR RefSeq; XP_017905480.1; XM_018049991.1.
DR RefSeq; XP_017905481.1; XM_018049992.1.
DR RefSeq; XP_017905482.1; XM_018049993.1.
DR AlphaFoldDB; A0A452FUS9; -.
DR SMR; A0A452FUS9; -.
DR STRING; 9925.ENSCHIP00000027892; -.
DR Ensembl; ENSCHIT00000035761.1; ENSCHIP00000027892.1; ENSCHIG00000023629.1.
DR GeneID; 102168824; -.
DR KEGG; chx:102168824; -.
DR CTD; 83594; -.
DR GeneTree; ENSGT00940000157592; -.
DR OMA; EARWFPR; -.
DR OrthoDB; 3024612at2759; -.
DR Proteomes; UP000291000; Chromosome 7.
DR Bgee; ENSCHIG00000023629; Expressed in liver and 18 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; IEA:Ensembl.
DR GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0110156; P:methylguanosine-cap decapping; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0019677; P:NAD catabolic process; IEA:Ensembl.
DR GO; GO:0110155; P:NAD-cap decapping; IEA:Ensembl.
DR GO; GO:0006742; P:NADP catabolic process; IEA:Ensembl.
DR CDD; cd03429; NADH_pyrophosphatase; 1.
DR Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR049734; NudC-like_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015376; Znr_NADH_PPase.
DR PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1.
DR PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT REPEAT 45..77
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 319..453
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 462 AA; 52134 MW; 5507FDF3B0D81EAE CRC64;
MSSVKRSLNQ EIISQFHYSA AEGDIAKLTA ILSHSPSLLN ETSENGWTAL MYAARNGHPD
VVQFLLEKGC DRSIVNKSRQ TALDIAKFWG YKHIANLLAN AKGGKKPWFL TNEVEECENY
FSKTLLDRKS EKRNNSDWLL AKESHPATVY ILFSDLNPLV TLGGNKESFQ QPEVRLCQLN
YTDIKDYLAQ PEKITLIFLG VELEMKKEFF NYAGEVSKEE EDGLVAWFAL GIDTVAAEEF
KQRHENCYFL HPPMPALLQL KEKEAGVVAQ ARSVLAWHSR YKFCPTCGNA TKIEEGGYKR
VCLKEDCPSL HGVHNTSYPR VDPVVIMQVI HPDGTKCLLG RQKRFPPGMF TCLAGFIEPG
ETIEDAVRRE VEEESGVKVG HVQYVSCQPW PMPSSLMIGC LAVAVSTEIK VDKNEIEDAR
WFTREQVVDV LTKGKQQAFF VPPSRAIAHQ LIKHWIGMNP NL
//
