ID G1PQ84_MYOLU Unreviewed; 464 AA.
AC G1PQ84;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN Name=NUDT12 {ECO:0000313|Ensembl:ENSMLUP00000013221.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013221.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013221.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000013221.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Peroxisome {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; AAPE02000388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PQ84; -.
DR STRING; 59463.ENSMLUP00000013221; -.
DR Ensembl; ENSMLUT00000014533.2; ENSMLUP00000013221.2; ENSMLUG00000014521.2.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG3084; Eukaryota.
DR GeneTree; ENSGT00940000157592; -.
DR HOGENOM; CLU_037162_0_2_1; -.
DR InParanoid; G1PQ84; -.
DR OMA; EARWFPR; -.
DR TreeFam; TF106352; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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; 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; 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:UP000001074}.
FT REPEAT 45..77
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 318..455
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 464 AA; 52347 MW; 89C69FE6765E6416 CRC64;
MSSIKRNPKQ EIVSQFHYSA AEGDIARLTV ILSHSPSLLN ETSENGWTAL MYAARNGHPD
VVQFLLEKGC DRSIVNKSRQ TALDIAKFWG YKHIANLLAN NKGGKKPWFL TNEVEECENY
FGKTLLDRKS EKRNNSDWLL AKESHPATVY ILFSDLNPLV TLGGNKESSQ QPEVRLCQLN
YTDIKDYLAQ PEKITLIFLG VELEMKKELL NYPGEVPREE EDGLVAWFAL GIDPVAAEEF
KQRHENCYFL HPPMPALLQL KENEAEGVVA QARSVLAWHS RYKFCPTCGS ATKIEEGGYK
RVCLKEDCPS LHGVHNTSYP RVVDPVVIMQ VIHPDGTKCL LGRQKRFPPG MFTCLAGFIE
PGETIEDAVR REVEEESGVK VGHVQYVSCQ PWPMPSSLMI GCLAVAVSTE IKVDKNEIED
ARWFTREQVV DVLTKGKQQA FFVPPSRAIA HQLIKHWIGM NPNL
//
