RNH3_STRPN
ID RNH3_STRPN Reviewed; 293 AA.
AC O07874;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribonuclease HIII;
DE Short=RNase HIII;
DE EC=3.1.26.4;
GN Name=rnhC; Synonyms=rnhB; OrderedLocusNames=SP_0403;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17.
RC STRAIN=533;
RX PubMed=9190796; DOI=10.1128/jb.179.12.3828-3836.1997;
RA Zhang Y.B., Ayalew S., Lacks S.A.;
RT "The rnhB gene encoding RNase HII of Streptococcus pneumoniae and evidence
RT of conserved motifs in eucaryotic genes.";
RL J. Bacteriol. 179:3828-3836(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally defined as a RNase HII; but belongs to the
CC RNase HIII subfamily. {ECO:0000305|PubMed:9190796}.
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DR EMBL; U93576; AAC45437.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74566.1; -; Genomic_DNA.
DR PIR; E95046; E95046.
DR PIR; E97917; E97917.
DR RefSeq; WP_000146867.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; O07874; -.
DR SMR; O07874; -.
DR STRING; 170187.SP_0403; -.
DR EnsemblBacteria; AAK74566; AAK74566; SP_0403.
DR KEGG; spn:SP_0403; -.
DR eggNOG; COG1039; Bacteria.
DR OMA; TGDYFGP; -.
DR BioCyc; SPNE170187:G1FZB-419-MON; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9190796"
FT CHAIN 2..293
FT /note="Ribonuclease HIII"
FT /id="PRO_0000111701"
FT DOMAIN 78..293
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 130
FT /note="T -> A (in Ref. 1; AAC45437)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> T (in Ref. 1; AAC45437)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> A (in Ref. 1; AAC45437)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> N (in Ref. 1; AAC45437)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..293
FT /note="KRLER -> NA (in Ref. 1; AAC45437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32347 MW; 77EB0090668E19F5 CRC64;
MASITLTPSE KDIQAFLEHY QTSLAPSKNP YIRYFLKLPQ ATVSIYTSGK ILLQGEGAEK
YASFFGYQAV EQTSGQNLPL IGTDEVGNGS YFGGLAVVAA FVTPDQHDFL RKLGVGDSKT
LTDQKIRQIT PILKEKIQHQ ALLLSPSKYN EVIGDRYNAV SVKVALHNQA IYLLLQKGVQ
PEKIVIDAFT SAKNYDKYLA QEANRFSNPI SLEEKAEGKY LSVAVSSVIA RDLFLENLEN
LGRELGYQLP SGAGTASDKV ASQILQAYGM QGLSFCAKLH FKNTEKAKKR LER
