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Database: UniProt
Entry: Q5GSG7_WOLTR
LinkDB: Q5GSG7_WOLTR
Original site: Q5GSG7_WOLTR 
ID   Q5GSG7_WOLTR            Unreviewed;       544 AA.
AC   Q5GSG7;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Predicted hydrolase of the metallo-beta-lactamase superfamily {ECO:0000313|EMBL:AAW71057.1};
GN   OrderedLocusNames=Wbm0469 {ECO:0000313|EMBL:AAW71057.1};
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=292805 {ECO:0000313|EMBL:AAW71057.1, ECO:0000313|Proteomes:UP000000534};
RN   [1] {ECO:0000313|EMBL:AAW71057.1, ECO:0000313|Proteomes:UP000000534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS {ECO:0000313|Proteomes:UP000000534};
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
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DR   EMBL; AE017321; AAW71057.1; -; Genomic_DNA.
DR   RefSeq; WP_011256667.1; NC_006833.1.
DR   AlphaFoldDB; Q5GSG7; -.
DR   STRING; 292805.Wbm0469; -.
DR   KEGG; wbm:Wbm0469; -.
DR   eggNOG; COG0595; Bacteria.
DR   HOGENOM; CLU_008727_3_3_5; -.
DR   Proteomes; UP000000534; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd07714; RNaseJ_MBL-fold; 1.
DR   Gene3D; 3.10.20.580; -; 1.
DR   Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR041636; RNase_J_C.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   Pfam; PF17770; RNase_J_C; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   4: Predicted;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAW71057.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000534};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          20..216
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   544 AA;  60528 MW;  1BA879D711BD45FF CRC64;
     MNINKNEFLF LPLGGVGRIG MNVNLYHYRG KWIMIDLGIG FADETMPGIE LLIADVSFIA
     QRKKDLLGII ITHAHEDHCG AVPYLWKELQ CPIYTTKFTA NFLKEKLKEF RLEGMVSVKE
     VDINGSINLS PFTVEFINVT HSIPEAHSIL VSTDVGSALH TGDWKFDQKP IVGLTSNISR
     LKEIGDKGNL LAAICDSTNV LGKHNPESES EIYNNIYNII RRSKKLVAVS LFASNVARIE
     TIGQVAKVLG RKVVLLGRSL WRIVRVAQNS GYLTDSVEFC EVKDVADLPR EKLLLICTGC
     QGEPMAAISK LANKSHHAFK MQQGDTVIFS SKIIPGNETR AHVIFNAFIE MGVEIVTEKT
     ECVHASGHPV KAELREMYSL IKPKMSIPVH GEYIHTHAHV KFAKECGVEK AIMIAPGDIV
     NLENGKKVDS INVNYFGVDG ILLRHPGSNV IRMRKKMRDA GTIVVTAIVN KRNKLLAKPK
     VFAPGVLEAV EDAAIIQRII KAVESAFNLQ STKKVRNKIE SLIFSILKEY LLKRPIIEVQ
     IEQV
//
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