ID A0A1Y2K969_9PROT Unreviewed; 180 AA.
AC A0A1Y2K969;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=MAIT1_03389 {ECO:0000313|EMBL:OSM05226.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM05226.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM05226.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM05226.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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:OSM05226.1}.
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DR EMBL; LVJN01000018; OSM05226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K969; -.
DR STRING; 1434232.MAIT1_03389; -.
DR OrthoDB; 7845843at2; -.
DR Proteomes; UP000194003; 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|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00042}; Hydrolase {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:UP000194003}.
FT DOMAIN 24..165
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ SEQUENCE 180 AA; 19175 MW; 087D190287AF51BC CRC64;
MASLDDTPSL FSNLEADEPE ASGCLSTTII HTDGACSGNP GPGGWGYVWE RDGLAGQAAG
FSPRTTNNRM ELLAAIRALE SLPRGSQAEV ITDSAYVKNG ITEWIHGWKR RNWRKSGGGA
VLNADLWKRL DALAAQRSVE WRWIKGHAGH PGNEAADALA RRAISDGLNG LADADPEGAL
//
