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Database: UniProt
Entry: R7U2G6_CAPTE
LinkDB: R7U2G6_CAPTE
Original site: R7U2G6_CAPTE 
ID   R7U2G6_CAPTE            Unreviewed;       440 AA.
AC   R7U2G6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 53.
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   ORFNames=CAPTEDRAFT_220786 {ECO:0000313|EMBL:ELT97831.1},
GN   CAPTEDRAFT_228617 {ECO:0000313|EMBL:ELT96544.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT97831.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT97831.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT97831.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP220786}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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; AMQN01002282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMQN01027363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB308810; ELT96544.1; -; Genomic_DNA.
DR   EMBL; KB308463; ELT97831.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7U2G6; -.
DR   STRING; 283909.R7U2G6; -.
DR   EnsemblMetazoa; CapteT220786; CapteP220786; CapteG220786.
DR   EnsemblMetazoa; CapteT228617; CapteP228617; CapteG228617.
DR   HOGENOM; CLU_037162_0_2_1; -.
DR   OMA; EARWFPR; -.
DR   Proteomes; UP000014760; Unassembled WGS sequence.
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; 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; 1.
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|PROSITE-ProRule:PRU00023};
KW   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:UP000014760}.
FT   REPEAT          42..74
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          297..423
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   440 AA;  48806 MW;  72B4301D717617CD CRC64;
     MDKHDIYETY VEKFHEAAAG GDTDLLDSAV KVLPNLNVKN DKGWTALMFA ARNGHANVVK
     LLLDRGCDCE VINSTGQTAL GIAQFWNQHK VVELLEAPPS SSSSSGPVLQ TEPGVTNFLC
     GSPLDRRAEK RKDKKWLDEA LKGSSVEIIS FHNLSPVVKK LPDLTTKGLD AEYRLMTSKY
     ADLSVVFHNQ TPAVIFLGVD PSGEVPWFAV DVSHVPEEKI KDIHPYAEIM GYRSIFSFKK
     AEAAICGQAR TLLAWHDRYQ FCPTCGAKTT IEEGGYKRKC TDANCRSLKG THNTCYPRVD
     PTVIMAVVSP DGKQLLLGRG SKFPPLFFSC LAGFVEPGES IEEACRREVF EEAGVCVGHV
     QYHSCQPWPM PASLMIGCIA HATSTDITID HDELEEARWF SRQEVIQILT SQHPQRLSCP
     PEFAIAHQII RSWVNMTSNL
//
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