RNH2_CHLAD
ID RNH2_CHLAD Reviewed; 212 AA.
AC B8GBB1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Cagg_1844;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001337; ACL24739.1; -; Genomic_DNA.
DR RefSeq; WP_015940598.1; NC_011831.1.
DR AlphaFoldDB; B8GBB1; -.
DR SMR; B8GBB1; -.
DR STRING; 326427.Cagg_1844; -.
DR EnsemblBacteria; ACL24739; ACL24739; Cagg_1844.
DR KEGG; cag:Cagg_1844; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_3_2_0; -.
DR OMA; YPTKLHL; -.
DR OrthoDB; 1685277at2; -.
DR Proteomes; UP000002508; 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.
FT CHAIN 1..212
FT /note="Ribonuclease HII"
FT /id="PRO_1000194445"
FT DOMAIN 17..211
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
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 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
SQ SEQUENCE 212 AA; 22970 MW; 5707CA0477E535C8 CRC64;
MSPDLSIEQT LLARGYRVLA GIDEAGRGCW AGPVVAAAVV LAPIVYERPG LLDAVDDSKQ
LTAVARERAY TLVQRYARGI GVGTVPAFLV DAYGILPATR LAMTLALLSL PCSVDALLID
AERLPGIRVP QESLVRGDAR SLSIAAASII AKVTRDRLMQ TADRCYPQYG FALHKGYGTP
VHRRALRQYG PSPFHRRTFQ PVLELLDLTD SS