ID A0A365P9B7_9ACTN Unreviewed; 234 AA. AC A0A365P9B7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 02-OCT-2024, entry version 20. 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=DQ226_10705 {ECO:0000313|EMBL:RBA35277.1}; OS Dietzia maris. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae; OC Dietzia. OX NCBI_TaxID=37915 {ECO:0000313|EMBL:RBA35277.1, ECO:0000313|Proteomes:UP000252187}; RN [1] {ECO:0000313|EMBL:RBA35277.1, ECO:0000313|Proteomes:UP000252187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SST1 {ECO:0000313|EMBL:RBA35277.1, RC ECO:0000313|Proteomes:UP000252187}; RA Abdel-Mageed W.M., Lehri B., Jarmusch S.A., Miranda K., Goodfellow M., RA Jaspars M., Karlyshev A.V.; RT "Whole genome sequencing of four bacterial strains from South Shetland RT trench revealing bio-synthetic gene clusters."; RL Submitted (JUN-2018) 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:RBA35277.1}. 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; QNTT01000026; RBA35277.1; -; Genomic_DNA. DR AlphaFoldDB; A0A365P9B7; -. DR Proteomes; UP000252187; 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:UniProtKB-UniRule. 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; Ribonuclease H-like superfamily/Ribonuclease H; 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; RIBONUCLEASE H2 SUBUNIT A; 1. DR PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 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}. FT DOMAIN 39..230 FT /note="RNase H type-2" FT /evidence="ECO:0000259|PROSITE:PS51975" FT BINDING 45 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 46 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 139 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 234 AA; 24840 MW; 473218F06B8F456F CRC64; MSRARPQRPR GVALPGRVRV TRRDGRLALE AALARRGLGP VAGVDEAGRG SCAGPLVVAA CVLGDRLHPD LADLDDSKKL TAATRERLHD VILRRASAVS VVVIEPDRID MRGIHRCNLE GMRRAVAALD PAPGFVLTDG FAVDGLGCQS TSVIGGDAVV ASIAAASVLA KVTRDRIMVD LDLRYPGYGF VAHKGYSTVS HARAIEQLGP SGIHRMSYAN VRRAAQAHSR SSTR //