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Database: UniProt
Entry: A0A0W7W6I7_9MICO
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ID   A0A0W7W6I7_9MICO        Unreviewed;       176 AA.
AC   A0A0W7W6I7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Ribonuclease H {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|HAMAP-Rule:MF_00042};
DE            Short=RNase H {ECO:0000256|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|HAMAP-Rule:MF_00042};
GN   Name=rnhA {ECO:0000256|HAMAP-Rule:MF_00042};
GN   ORFNames=AUL38_02885 {ECO:0000313|EMBL:KUF06224.1};
OS   Leucobacter sp. G161.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06224.1, ECO:0000313|Proteomes:UP000053012};
RN   [1] {ECO:0000313|EMBL:KUF06224.1, ECO:0000313|Proteomes:UP000053012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G161 {ECO:0000313|EMBL:KUF06224.1,
RC   ECO:0000313|Proteomes:UP000053012};
RA   Ge S., Dong X.;
RT   "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT   effective chromium reducer.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|HAMAP-Rule:MF_00042}.
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_00042};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC       Rule:MF_00042}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042}.
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300, ECO:0000256|HAMAP-Rule:MF_00042}.
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:KUF06224.1}.
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DR   EMBL; LOHP01000075; KUF06224.1; -; Genomic_DNA.
DR   RefSeq; WP_059062809.1; NZ_LOHP01000075.1.
DR   AlphaFoldDB; A0A0W7W6I7; -.
DR   STRING; 663704.AUL38_02885; -.
DR   OrthoDB; 7845843at2; -.
DR   Proteomes; UP000053012; Unassembled WGS sequence.
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; Ribonuclease H-like superfamily/Ribonuclease H; 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   PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR   PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00042};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00042};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00042};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00042};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT   DOMAIN          1..138
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          131..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ   SEQUENCE   176 AA;  18945 MW;  84A384D3D683EAF0 CRC64;
     MTLTAAADGS ALGNPGPAGW AWVIDKEQWR AGGWPRATNN QGELMAVLDL LHATAARDEP
     LHILCDSQYV INSVTQWMPG WKRRGWRKAD GKPVLNRELL ESIDTALVGR TVTFEWVKGH
     AGHPLNEAAD DRARAAAEAF QRQAQPNHGP GLAGAAASPE VPLESASTQQ APPTLF
//
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