RNH2_CAUVN
ID RNH2_CAUVN Reviewed; 211 AA.
AC B8GZ34; P52975;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=CCNA_00383;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7896686; DOI=10.1128/jb.177.7.1662-1669.1995;
RA Stephens C.M., Zweiger G., Shapiro L.;
RT "Coordinate cell cycle control of a Caulobacter DNA methyltransferase and
RT the flagellar genetic hierarchy.";
RL J. Bacteriol. 177:1662-1669(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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. {ECO:0000305}.
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DR EMBL; S76857; AAB33869.2; -; Genomic_DNA.
DR EMBL; CP001340; ACL93850.1; -; Genomic_DNA.
DR PIR; A56141; A56141.
DR RefSeq; WP_012639945.1; NC_011916.1.
DR RefSeq; YP_002515758.1; NC_011916.1.
DR AlphaFoldDB; B8GZ34; -.
DR SMR; B8GZ34; -.
DR PRIDE; B8GZ34; -.
DR EnsemblBacteria; ACL93850; ACL93850; CCNA_00383.
DR GeneID; 7331082; -.
DR KEGG; ccs:CCNA_00383; -.
DR PATRIC; fig|565050.3.peg.382; -.
DR HOGENOM; CLU_036532_3_2_5; -.
DR OMA; YPTKLHL; -.
DR OrthoDB; 1685277at2; -.
DR PhylomeDB; B8GZ34; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese 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; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
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_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..211
FT /note="Ribonuclease HII"
FT /id="PRO_0000378307"
FT DOMAIN 16..205
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 22
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 1..24
FT /note="MPPGPDMTLELACGQAPVCGVDEA -> MCVEKN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="G -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Missing (in Ref. 1; AAB33869)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> T (in Ref. 1; AAB33869)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> S (in Ref. 1; AAB33869)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="N -> S (in Ref. 1; AAB33869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 21931 MW; D27A6FF06FF1A108 CRC64;
MPPGPDMTLE LACGQAPVCG VDEAGRGPWA GPVSAGAVIL DPDRIPKGLN DSKKLSAKAR
AALEEEIKDV AISWCVGLAS IEEIAQLNIL HAAGLAMRRA VEGLAVTPAF ALVDGNYAFK
LPCPVKTVIK GDSLSCSIAA ASILAKEARD RIMIEADALY PGYGFAGHKG YHAKVHVEGL
RRLGPSPIHR LGWAPVKAAL AAAAVNGELD L
