RNH3_LEUCK
ID RNH3_LEUCK Reviewed; 308 AA.
AC B1MXB1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ribonuclease HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE Short=RNase HIII {ECO:0000255|HAMAP-Rule:MF_00053};
DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00053};
GN Name=rnhC {ECO:0000255|HAMAP-Rule:MF_00053}; OrderedLocusNames=LCK_00330;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000255|HAMAP-Rule:MF_00053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00053};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000255|HAMAP-Rule:MF_00053};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00053}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00053}.
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DR EMBL; DQ489736; ACA82163.1; -; Genomic_DNA.
DR RefSeq; WP_004907416.1; NC_010471.1.
DR AlphaFoldDB; B1MXB1; -.
DR SMR; B1MXB1; -.
DR STRING; 349519.LCK_00330; -.
DR EnsemblBacteria; ACA82163; ACA82163; LCK_00330.
DR KEGG; lci:LCK_00330; -.
DR eggNOG; COG1039; Bacteria.
DR HOGENOM; CLU_059546_1_0_9; -.
DR OMA; TGDYFGP; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000002166; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00716; rnhC; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..308
FT /note="Ribonuclease HIII"
FT /id="PRO_1000091678"
FT DOMAIN 93..308
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 99
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT BINDING 100
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
FT BINDING 203
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00053"
SQ SEQUENCE 308 AA; 33403 MW; 107AFCBE69CC8E94 CRC64;
MQIVLQVSIP QLKKMAAYYA PYAVSKAPKG AVFVAKLSQA TVTAYKSGKV LFQGSGFKVE
AARWQDNANQ PTQKMNASHV TPGATIPTDF ANWSVIGSDE VGAGAYFGPL TTAAVFVSKN
DLDWVKALGI ADSKTLTDAK MRDIAPEIIQ RLPHHVVNLL PEKYNALQPH NNVNQLKAIS
HNFALHKVLE KIAPITPDAI LIDQFAQATT YFNYLSKAQQ SPVIRQNVYF TTKGEQYHLS
VAAASILARV VELDTMVALS HEAGMTLPIG AGKAVDLVAA KLIRQGQDLN HFAKLHFANT
AKAKSLVN