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Database: UniProt/TrEMBL
Entry: D0R4F1_LACJF
LinkDB: D0R4F1_LACJF
Original site: D0R4F1_LACJF 
ID   D0R4F1_LACJF            Unreviewed;       250 AA.
AC   D0R4F1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   01-MAY-2013, entry version 25.
DE   RecName: Full=Ribonuclease HII;
DE            Short=RNase HII;
DE            EC=3.1.26.4;
GN   Name=rnhB; OrderedLocusNames=FI9785_1100;
OS   Lactobacillus johnsonii (strain FI9785).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=633699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FI9785;
RX   PubMed=19767436; DOI=10.1128/JB.01182-09;
RA   Wegmann U., Overweg K., Horn N., Goesmann A., Narbad A., Gasson M.J.,
RA   Shearman C.;
RT   "Complete genome sequence of Lactobacillus johnsonii FI9785, a
RT   competitive exclusion agent against pathogens in poultry.";
RL   J. Bacteriol. 191:7142-7143(2009).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
CC   -!- COFACTOR: Manganese or magnesium. Binds 1 divalent metal ion per
CC       monomer in the absence of substrate. May bind a second metal ion
CC       after substrate binding (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the RNase HII family.
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DR   EMBL; FN298497; CAX66964.1; -; Genomic_DNA.
DR   RefSeq; YP_003293231.1; NC_013504.1.
DR   STRING; 633699.FI9785_1100; -.
DR   EnsemblBacteria; CAX66964; CAX66964; FI9785_1100.
DR   GeneID; 8570867; -.
DR   KEGG; ljf:FI9785_1100; -.
DR   PATRIC; 32246789; VBILacJoh137736_1025.
DR   eggNOG; COG0164; -.
DR   HOGENOM; HOG000100288; -.
DR   KO; K03470; -.
DR   BioCyc; LJOH633699:GJ95-1033-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0004523; F:ribonuclease H activity; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:HAMAP.
DR   HAMAP; MF_00052_B; RNase_HII_B; 1; -.
DR   InterPro; IPR022898; RNase_HII.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; RNaseH_fold; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Manganese;
KW   Metal-binding; Nuclease.
FT   METAL        72     72       Divalent metal cation (By similarity).
FT   METAL        73     73       Divalent metal cation (By similarity).
FT   METAL       164    164       Divalent metal cation (By similarity).
SQ   SEQUENCE   250 AA;  27948 MW;  9D8A0E00E8901CE9 CRC64;
     MTITEIKNLL QGEVSKEQLE ELKADERKGV QKLLISYEKR QAKYAKALAQ FQSRFSYEKE
     FWQKDQLVAG VDEVGRGPLA GPVVTAAVIL PHDFDLIDVN DSKKLSPKKR QALFPKILEK
     AVSVSVGLAN NDLIDQINIY EADRVAMAHA VQGLKVKPDA LLVDAMNVPL NIPQVKLIHG
     DAKSNSIAAA SIVAKVFRDN LMDAYGELYP EYDFKHNAGY GTREHMEALK KYGPTPIHRR
     SFAPVSEYEK
//
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