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Database: UniProt
Entry: A0A0B4EAU5_9RHOB
LinkDB: A0A0B4EAU5_9RHOB
Original site: A0A0B4EAU5_9RHOB 
ID   A0A0B4EAU5_9RHOB        Unreviewed;       555 AA.
AC   A0A0B4EAU5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Metallo-beta-lactamase {ECO:0000313|EMBL:KID08113.1};
GN   ORFNames=GC1_13005 {ECO:0000313|EMBL:KID08113.1};
OS   Leisingera sp. ANG1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID08113.1, ECO:0000313|Proteomes:UP000031201};
RN   [1] {ECO:0000313|EMBL:KID08113.1, ECO:0000313|Proteomes:UP000031201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG1 {ECO:0000313|EMBL:KID08113.1,
RC   ECO:0000313|Proteomes:UP000031201};
RX   PubMed=21551313; DOI=10.1128/JB.05139-11;
RA   Collins A.J., Nyholm S.V.;
RT   "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   J. Bacteriol. 193:3397-3398(2011).
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:KID08113.1}.
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DR   EMBL; AFCF02000008; KID08113.1; -; Genomic_DNA.
DR   RefSeq; WP_019295976.1; NZ_AFCF02000008.1.
DR   AlphaFoldDB; A0A0B4EAU5; -.
DR   STRING; 1002340.GC1_13005; -.
DR   eggNOG; COG0595; Bacteria.
DR   OrthoDB; 9770211at2; -.
DR   Proteomes; UP000031201; Unassembled WGS sequence.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          18..206
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   555 AA;  60500 MW;  539BE3478A02EF38 CRC64;
     MSSDRLIYLP LGGAGEIGMN AYVYGYGPQG KERLILVDLG VTFPDMDTTP GVDLIMPDIT
     WLKERADRLE GIFITHGHED HIGAIAHLYA HLNVPVYARA FTANLARRKM EEAGHDPANV
     HTVQAWPETT KLGPFTIGVA PMSHSIPESG ALVIDSPAGR VVHTGDFKLD SNPLVGEPFD
     PEMWAEIAKD GIQALVCDST NVFSQHPGRS ESELPEEITK LFSEAKGLVA ATTFASNVAR
     VKTLAEAGVK AGRSVVLLGR AMRRMIEAAV ETGVLVDFPK VISPEDAANV PRDNLMLITT
     GSQGERRAAT AQLARGKYRG LELKEGDLFL FSSKTIPGNE KGVIRIINQF SEMGVDVVDD
     SSGLYHVSGH ANGPDLEVVH NLLKPKMLIP MHGEHRHLRQ HARLGEEKGI ASAVAVNGMM
     MDLTGDAPAV TEWIETGRTY LDGSVKYGAM DGIVRDRIRM ALNGHVLVTV ILDEEDEPLG
     EPWCDLKGLP ETGTSNAALV EVLEEDLNQF LMRAGAKTLR DDDRLEQELR RITRQTAQAE
     IGKKPEVTVV VSRMR
//
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