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Database: UniProt
Entry: A0A1W6SSU2_9PROT
LinkDB: A0A1W6SSU2_9PROT
Original site: A0A1W6SSU2_9PROT 
ID   A0A1W6SSU2_9PROT        Unreviewed;       168 AA.
AC   A0A1W6SSU2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Phosphatase NudJ {ECO:0000256|ARBA:ARBA00015552, ECO:0000256|RuleBase:RU364043};
DE            EC=3.6.1.- {ECO:0000256|RuleBase:RU364043};
GN   Name=nudJ {ECO:0000256|RuleBase:RU364043};
GN   ORFNames=EBAPG3_014340 {ECO:0000313|EMBL:ARO88853.1};
OS   Nitrosospira lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO88853.1, ECO:0000313|Proteomes:UP000012179};
RN   [1] {ECO:0000313|EMBL:ARO88853.1, ECO:0000313|Proteomes:UP000012179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APG3 {ECO:0000313|EMBL:ARO88853.1,
RC   ECO:0000313|Proteomes:UP000012179};
RX   PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA   Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA   Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT   "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT   bacterium from sandy lake sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364043};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU364043}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudJ subfamily.
CC       {ECO:0000256|ARBA:ARBA00007608, ECO:0000256|RuleBase:RU364043}.
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DR   EMBL; CP021106; ARO88853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6SSU2; -.
DR   KEGG; nlc:EBAPG3_014340; -.
DR   eggNOG; COG1051; Bacteria.
DR   Proteomes; UP000012179; Chromosome.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR   GO; GO:0004787; F:thiamine diphosphate phosphatase activity; IEA:InterPro.
DR   CDD; cd03675; Nudix_Hydrolase_2; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR033713; NudJ.
DR   PANTHER; PTHR43222; NUDIX HYDROLASE 23; 1.
DR   PANTHER; PTHR43222:SF11; PHOSPHATASE NUDJ; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364043};
KW   Magnesium {ECO:0000256|RuleBase:RU364043};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012179}.
FT   DOMAIN          22..151
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   168 AA;  19255 MW;  7A054E37F5CFD36D CRC64;
     MRVGKHAFFF FTIFEDDQEI MIWKPNVTVA AVVEQDGKYL LVEEQTSSGV LFNQPAGHLE
     PDESIIQGAV RETLEETGYT FAPQWVLGIY RWHSCADNVT YLRFAFAGCV TGHDPDRPLD
     AGILRAGWFC VDEIREMTNR HRSPLVMRCV EDHLAGKRYS LDILTHYD
//
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