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Database: UniProt
Entry: D2SUE3_9BACT
LinkDB: D2SUE3_9BACT
Original site: D2SUE3_9BACT 
ID   D2SUE3_9BACT            Unreviewed;       497 AA.
AC   D2SUE3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Phosphoesterase {ECO:0000313|EMBL:ADA82587.1};
OS   uncultured bacterium psy1.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=693111 {ECO:0000313|EMBL:ADA82587.1};
RN   [1] {ECO:0000313|EMBL:ADA82587.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19448639; DOI=10.1038/nchembio.176;
RA   Fisch K.M., Gurgui C., Heycke N., van der Sar S.A., Anderson S.A.,
RA   Webb V.L., Taudien S., Platzer M., Rubio B.K., Robinson S.J., Crews P.,
RA   Piel J.;
RT   "Polyketide assembly lines of uncultivated sponge symbionts from structure-
RT   based gene targeting.";
RL   Nat. Chem. Biol. 5:494-501(2009).
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; FJ823461; ADA82587.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2SUE3; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362119};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119}.
FT   DOMAIN          44..251
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          331..465
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   497 AA;  55278 MW;  0FD8F1DE7E73EAF3 CRC64;
     MKEKRSMTRQ SEWMVWLITC VLAWSLGAGA QVGWANENDE VRVTILHVND LYQIASLRNG
     KLGGFARLTT LRKQLEKENP NTFVLFSGDL YEPSALGNAV VDGRPLLGRH AVGVLNEVGV
     DYMTFGDHEF NMSADQFYDR LGESRFRMLS SNLFEEDGQP FPGVVANGLL SALDEQGRDV
     TIGVLGVTKP FRTKIPMKYV DHYEAIAQQL AKLEKRADMI IALTHFPRKE DMAIAQRYPA
     INLILGADDH EHMKLEQEGM ATVYKSDSNA RSVYVLDLYI NRQAKSWRIE DRLVALDESI
     EQDPTTLAKV EKWIEIGFRG FEAAGLEPRR VLGQTPVDLD GLESSIRNRP TRLTQLIGEG
     MLRAGQDAGA QVAYYPAGLV RLDDILPTDY VVREFDVMRT IPFEVDIATV TMAGEALLKV
     LESGHGKIGT GRYIIPQGAE RDDQGRWTVQ GQALDPSGTY KVVTLAGPTT ANVVAKHGSM
     KDALRNELGR LLKKVAN
//
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