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Database: UniProt
Entry: A0A139NEH6_9STRE
LinkDB: A0A139NEH6_9STRE
Original site: A0A139NEH6_9STRE 
ID   A0A139NEH6_9STRE        Unreviewed;       504 AA.
AC   A0A139NEH6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Zn-dependent hydrolase, RNA-metabolising {ECO:0000313|EMBL:KXT74171.1};
GN   ORFNames=STRDD10_01155 {ECO:0000313|EMBL:KXT74171.1};
OS   Streptococcus sp. DD10.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT74171.1, ECO:0000313|Proteomes:UP000072050};
RN   [1] {ECO:0000313|EMBL:KXT74171.1, ECO:0000313|Proteomes:UP000072050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD10 {ECO:0000313|EMBL:KXT74171.1,
RC   ECO:0000313|Proteomes:UP000072050};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXT74171.1}.
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DR   EMBL; LQRE01000091; KXT74171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139NEH6; -.
DR   STRING; 1777878.STRDD10_01155; -.
DR   PATRIC; fig|1777878.3.peg.1269; -.
DR   Proteomes; UP000072050; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; 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; IPR004613; RNase_J.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR041636; RNase_J_C.
DR   NCBIfam; TIGR00649; MG423; 1.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF4; RIBONUCLEASE J 2; 1.
DR   Pfam; PF12706; Lactamase_B_2; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXT74171.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000072050};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          16..217
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   504 AA;  55708 MW;  316BF178A42AF29C CRC64;
     MTSIKLFSLG GIRENGKNLY VAEINDSIFV LDTGLKYPEN EQLGVDVVIP NMDYLIENRD
     RIAGIFLTHG HADAIGALPY LIAGAKKTPV FGSELTIELA KLFVKNNDVV KKFNDFHVID
     HNTEIEFGDA IVSFFKTTHS IPESLGIVLK TSEGSIVYTG DFKFDQAATE SYATDFGRLA
     EIGREGVLAL LSDSANADSN IQVASESEVA DEILNTIGDC EGRVIVAAVA SNLSRIQQVF
     DAAAATGRRV VLTGYDIENI VRTAIRLKKL SLVDERLLIK PKDMNKYEDH ELIILETGRM
     GEPINGLRKM SIGRHRYVEI KEGDLIYIVT TPSIAKEAVV ARVENMIYQA GGTVKLITQN
     LRVSGHGNAR DLQLMINLIK PKFLFPIQGE YRELDAHAKA AMEVGLLPEK IFIPKRGDIM
     VYEKGDFVHS GSIPAGDVMI DGNAMGDVGH IVLRDRKVLS EDGIFIVAIT VNRKKKKLFR
     RQKSILVVLS MSRKVGIFYE KVQS
//
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