ID G0EJJ7_BRAIP Unreviewed; 614 AA.
AC G0EJJ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=UshA, 5'-nucleotidase/2',3'-cyclic phosphodiesterase-like esterase {ECO:0000313|EMBL:AEM22393.1};
GN OrderedLocusNames=Bint_1777 {ECO:0000313|EMBL:AEM22393.1};
OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM22393.1, ECO:0000313|Proteomes:UP000008522};
RN [1] {ECO:0000313|EMBL:AEM22393.1, ECO:0000313|Proteomes:UP000008522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA Hafstrom T., Jansson D.S., Segerman B.;
RT "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT features in Brachyspira species and phage-mediated horizontal gene
RT transfer.";
RL BMC Genomics 12:395-395(2011).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP002874; AEM22393.1; -; Genomic_DNA.
DR RefSeq; WP_014488216.1; NC_017243.1.
DR AlphaFoldDB; G0EJJ7; -.
DR KEGG; bip:Bint_1777; -.
DR PATRIC; fig|1045858.4.peg.1779; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_3_12; -.
DR OMA; EKAQYPM; -.
DR OrthoDB; 9800780at2; -.
DR Proteomes; UP000008522; Chromosome.
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:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE/3'-NUCLEOTIDASE; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119}.
FT DOMAIN 38..265
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 372..543
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 614 AA; 69688 MW; 7A759DB85EC98F93 CRC64;
MKRGYIVMSI FLSALLTNVS CNSKDKNRVY PEGEVNFTIV QTTDIHGMIF PYNFITDKEE
DTSMAHVSSY LKQLKNEGKT ILLLENGDSL QGQPTVYYYN FVAINEPHIW SEVLNYMDYD
AVAVGNHDIE AGHSVYDKLA KELKAPLLAA NLIDEKSKEP YFKPYTVVEK NGVKIAVLGL
IEPAIDRQLP KVLYEGLATE DMVESAKKWI KVIKDKEKPD MIIGLFHAGA DHTDDKETYK
NENASQLVAE QVDGFDIIFV GHDHQGWSGL GYDQTSKQKT KEVKSPSGKI VPIYGGVNSA
RYIASVDVSM SYNKNNKTWN MKFDGNLLDP SQFESDKEFL EKFADARANI EKWVSRDIGN
LNTKLVSDEA IFGDSYFLSF IHKLQFTIAE KELGEKADIS FAAPLSKDAV LNNGVIKVKD
MFNLYPYENF FYVMKLTGKQ IKDAMEYSYG RWFNTMNNIN DHLIAFKKDS SGKLIFNKRY
NSYDTITPSY NYESVAGLNY TVDVTKPNGE KIIIESLSDG RSFELDKEYK VAINSYRGSG
GGGHLTQGAG IDLETLQNMD LVLKSTDKDL RYYIINWFEE QNGPITVEKL NNWKVVPENY
VKAGKQRDYK LLYP
//