ID A0A4T2A8Y9_9RHOB Unreviewed; 213 AA. AC A0A4T2A8Y9; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 12-OCT-2022, entry version 11. DE RecName: Full=Ribonuclease HII {ECO:0000256|HAMAP-Rule:MF_00052}; DE Short=RNase HII {ECO:0000256|HAMAP-Rule:MF_00052}; DE EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00052}; GN Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052}; GN ORFNames=ELI80_16560 {ECO:0000313|EMBL:TIH11891.1}; OS Paracoccus aeridis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=1966466 {ECO:0000313|EMBL:TIH11891.1, ECO:0000313|Proteomes:UP000309864}; RN [1] {ECO:0000313|EMBL:TIH11891.1, ECO:0000313|Proteomes:UP000309864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JC 501 {ECO:0000313|EMBL:TIH11891.1, RC ECO:0000313|Proteomes:UP000309864}; RA Rai A., Venkata Ramana C., Sasikala C.; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA CC hybrids. {ECO:0000256|ARBA:ARBA00004065, ECO:0000256|HAMAP- CC Rule:MF_00052, ECO:0000256|RuleBase:RU003515}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|HAMAP- CC Rule:MF_00052, ECO:0000256|PROSITE-ProRule:PRU01319, CC ECO:0000256|RuleBase:RU003515}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00052, CC ECO:0000256|PROSITE-ProRule:PRU01319}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00052, CC ECO:0000256|PROSITE-ProRule:PRU01319}; 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:0000256|HAMAP-Rule:MF_00052, ECO:0000256|PROSITE- CC ProRule:PRU01319}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052}. CC -!- SIMILARITY: Belongs to the RNase HII family. CC {ECO:0000256|ARBA:ARBA00007383, ECO:0000256|HAMAP-Rule:MF_00052, CC ECO:0000256|RuleBase:RU003515}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TIH11891.1}. 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; SELD01000055; TIH11891.1; -; Genomic_DNA. DR Proteomes; UP000309864; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00052}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_00052}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00052}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00052}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00052}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00052}; KW Reference proteome {ECO:0000313|Proteomes:UP000309864}. FT DOMAIN 20..211 FT /note="RNase H type-2" FT /evidence="ECO:0000259|PROSITE:PS51975" FT BINDING 26 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052, FT ECO:0000256|PROSITE-ProRule:PRU01319" FT BINDING 27 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052, FT ECO:0000256|PROSITE-ProRule:PRU01319" FT BINDING 120 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052, FT ECO:0000256|PROSITE-ProRule:PRU01319" SQ SEQUENCE 213 AA; 22949 MW; EAC0EBC2709A6B47 CRC64; MRRLKHLRTY EVALDKAGLG PVAGVDEAGR GACFGPVTIA ACVLPPRPIA QLDRLTDSKQ LAPSTRASLY DAICDVAESF AVVHISAAEI DRRGIQVANV DGARRAVAKL DARPGYVLVD ALRVPGLTAP QLPIIGGDYT ARCIAAASVL AKVSRDRLVT EMAQRYADYG IAGHKGYGTQ AHMAAVRRHG ASPEHRYSYA NVRQAHEYFM RSQ //