GenomeNet

Database: UniProt
Entry: I0YK30_COCSC
LinkDB: I0YK30_COCSC
Original site: I0YK30_COCSC 
ID   I0YK30_COCSC            Unreviewed;       551 AA.
AC   I0YK30;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   ORFNames=COCSUDRAFT_49188 {ECO:0000313|EMBL:EIE18749.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE18749.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE18749.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE18749.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
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   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009595}.
CC   -!- SIMILARITY: Belongs to the janus family.
CC       {ECO:0000256|ARBA:ARBA00010971}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIE18749.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGSI01000022; EIE18749.1; -; Genomic_DNA.
DR   RefSeq; XP_005643293.1; XM_005643236.1.
DR   AlphaFoldDB; I0YK30; -.
DR   STRING; 574566.I0YK30; -.
DR   GeneID; 17036678; -.
DR   KEGG; csl:COCSUDRAFT_49188; -.
DR   eggNOG; KOG3084; Eukaryota.
DR   OrthoDB; 3024612at2759; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
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; 3.50.20.20; Janus/Ocnus; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR007702; Janus.
DR   InterPro; IPR038596; Janus_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   PANTHER; PTHR42904:SF8; NAD(+) DIPHOSPHATASE; 1.
DR   PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF09296; NUDIX-like; 1.
DR   Pfam; PF05005; Ocnus; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   SUPFAM; SSF143724; PHP14-like; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT   DOMAIN          216..380
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   ACT_SITE        479
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR607702-1"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR607702-2"
SQ   SEQUENCE   551 AA;  60200 MW;  898F191F3ED3FF38 CRC64;
     MSDMLLRFGQ FARSTRLYIG SGSLRGTHVG CRIATSARLE RINDGDAAAL HYAGLGLDRA
     THIRNDEAKL KELAGRSDAK LVPVFEGKNL VTHSQGLSSA VLPLQNAEQY LIPDSLVFLG
     LEPGGVPVFG AACRPECEEW LSPLVAEAGA GARWVDLRKE GPKLAGDQAA LLALAQALLR
     WNENNAFCGR TGAPTAAMQG GHARVAASPR ARVVYPRIDP AVIALVYCGD YALLGRQSRW
     APGRYSCLAG FAEVGETLEL AVGREVKEES GVAVDPHSIQ YVASQPWPFP QSLMIGFMAT
     AAAPDRSHAW SLARQRLQGL HHGCTEEEVG FTLVEELCLQ QPLVDITELE DARWFHRSWL
     RRHLHHAADG SGWDTSEAES SSSTAASVSF SIPGSYALAH RLIHTFMALE QPAKGDARHW
     RQARIQTCHC VMAFDAVPDV KEVDIDESGT YKYVLLRLQS KSNSMSRLLV RGNKRAGYHQ
     DILELAQEVD ADDDSQVVPL GGGRIAFDEE KRTIDIYGFS SAYDQAPHDI TAALVRRSYP
     FHTVSVSYSG Y
//
DBGET integrated database retrieval system