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RNH2_COLP3
ID   RNH2_COLP3              Reviewed;         217 AA.
AC   Q485F4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ribonuclease HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE            Short=RNase HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00052};
GN   Name=rnhB {ECO:0000255|HAMAP-Rule:MF_00052}; OrderedLocusNames=CPS_1569;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
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_00052};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000255|HAMAP-
CC       Rule:MF_00052}.
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DR   EMBL; CP000083; AAZ25408.1; -; Genomic_DNA.
DR   RefSeq; WP_011042405.1; NC_003910.7.
DR   AlphaFoldDB; Q485F4; -.
DR   SMR; Q485F4; -.
DR   STRING; 167879.CPS_1569; -.
DR   EnsemblBacteria; AAZ25408; AAZ25408; CPS_1569.
DR   KEGG; cps:CPS_1569; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_3_2_6; -.
DR   OMA; YPTKLHL; -.
DR   OrthoDB; 1685277at2; -.
DR   Proteomes; UP000000547; 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..217
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000235713"
FT   DOMAIN          16..217
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:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         23
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT   BINDING         114
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ   SEQUENCE   217 AA;  23901 MW;  6AD3AD1D133B540B CRC64;
     MASKQIFPDF EYPIAYCIAG VDEVGRGPLV GDVVTAAVIL DPDNPIEGLM DSKKLSEKKR
     NLLSLEIKEK AISWSLGRAS PQEIDTLNIL HATMLAMQRA VEGLNVEPDF VLVDGNRCPT
     FLCNASESNQ QNLKIASQAV VKGDARVTEI SAASIIAKVA RDNEMIALDK LHPEYGFAKH
     KGYPTKLHLE KIIEHGVLDC YRQSFKPVAR VLGTYHD
 
 
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