RNH_WOLWR
ID RNH_WOLWR Reviewed; 145 AA.
AC C0R2X2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_00042};
DE Short=RNase H {ECO:0000255|HAMAP-Rule:MF_00042};
DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00042};
GN Name=rnhA {ECO:0000255|HAMAP-Rule:MF_00042}; OrderedLocusNames=WRi_004800;
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=66084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wRi;
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00042};
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding. {ECO:0000255|HAMAP-
CC Rule:MF_00042};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00042}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000255|HAMAP-
CC Rule:MF_00042}.
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DR EMBL; CP001391; ACN95264.1; -; Genomic_DNA.
DR RefSeq; WP_007548952.1; NZ_MKIF01000200.1.
DR AlphaFoldDB; C0R2X2; -.
DR SMR; C0R2X2; -.
DR STRING; 66084.WRi_004800; -.
DR EnsemblBacteria; ACN95264; ACN95264; WRi_004800.
DR KEGG; wri:WRi_004800; -.
DR HOGENOM; CLU_030894_6_0_5; -.
DR OMA; MQEIEIF; -.
DR Proteomes; UP000001293; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid 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; cd09278; RNase_HI_prokaryote_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00042; RNase_H; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR022892; RNaseHI.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..145
FT /note="Ribonuclease H"
FT /id="PRO_1000194439"
FT DOMAIN 2..143
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00042"
SQ SEQUENCE 145 AA; 16549 MW; FB35E9C252E106B1 CRC64;
MSKKEVAIYT DGACSGNPGA GGWAAIILFQ DYRKDIYGRE ENTTNNKMEL TAVINGLKVL
KFSCNINLYT DSLYVKHGIT EWINKWKMNG WKTSNKKSVK NMELWKELDN VASQHEIDWK
WVKAHSGDKY NEEADSLARK AIIDA
