ID K9IK57_DESRO Unreviewed; 461 AA.
AC K9IK57;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA47555.1};
RN [1] {ECO:0000313|EMBL:JAA47555.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA47555.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; GABZ01005970; JAA47555.1; -; mRNA.
DR AlphaFoldDB; K9IK57; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:JAA47555.1};
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}.
FT REPEAT 45..77
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 318..452
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 461 AA; 51894 MW; D6A90D4ED3F5E717 CRC64;
MSSINRSPKQ EIISQFHCSA AEGDIAKLTV ILSRSPSLLN EISENGWTAL MYAARNGHLD
VVQLLLEKGC DRSIVNRSKQ TALDIAEFWG YKHIANLLAN AKGQKKPWFL TNEVEECENY
FSKTLLDRKS EKRNDSDWLL AKESHPATVY VLFSDLNPLV TLGGNKESSQ QPEVRLCQLN
YTDIKDYLAQ PEKVTLIFLG VELEMKKELL NSAGEVPREE DGLIAWFALG IDPVAAEEFK
QRHENCYFLH PPMPALLQLK EREAGVVAQA RSVLAWHSRY KFCPTCGSTT KIEEGGYKRV
CLKENCPSLH GVHNTSYPRV DPVVIMQVIH PDGTKCLLGR QKRFPPGMFT CLAGFIEPGE
TIEDAVRREV EEESGVKVGQ VQYVSCQPWP MPSSLMIGCL AVAVSTEIKV DKNEIEDARW
FTREQVVDVL TKGKQQAFFV PPSRAIAHQL IKHWIGMNPN L
//
