ID A0A0S2SHN0_9GAMM Unreviewed; 154 AA.
AC A0A0S2SHN0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ECO:0000313|EMBL:ALP41196.1};
GN ORFNames=ATO46_12355 {ECO:0000313|EMBL:KUE81284.1}, WL1483_1777
GN {ECO:0000313|EMBL:ALP41196.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:ALP41196.1, ECO:0000313|Proteomes:UP000058114};
RN [1] {ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|Proteomes:UP000058114};
RA Liu L.;
RT "Complete Genome Sequence of Aeromonas schubertii strain WL1483.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KUE81284.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE81284.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALP41196.1, ECO:0000313|Proteomes:UP000058114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WL1483 {ECO:0000313|EMBL:ALP41196.1,
RC ECO:0000313|Proteomes:UP000058114};
RX PubMed=26798095;
RA Liu L., Li N., Zhang D., Fu X., Shi C., Lin Q., Hao G.;
RT "Complete Genome Sequence of the Highly Virulent Aeromonas schubertii
RT Strain WL1483, Isolated from Diseased Snakehead Fish (Channa argus) in
RT China.";
RL Genome Announc. 4:e01567-15(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}.
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DR EMBL; CP013067; ALP41196.1; -; Genomic_DNA.
DR EMBL; LPUO01000002; KUE81284.1; -; Genomic_DNA.
DR RefSeq; WP_050666137.1; NZ_LPUO01000002.1.
DR STRING; 652.WL1483_1777; -.
DR KEGG; asr:WL1483_1777; -.
DR PATRIC; fig|652.5.peg.2825; -.
DR OrthoDB; 7845843at2; -.
DR Proteomes; UP000054876; Unassembled WGS sequence.
DR Proteomes; UP000058114; 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; 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}.
FT DOMAIN 1..142
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 125..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ SEQUENCE 154 AA; 17256 MW; 434246F598E8FDAB CRC64;
MLKQIDLYTD GSCLGNPGPG GYGAVLIYGK HRKELSAGYR LTTNNRMELM AAIAGLRTLS
ESCQVRLTTD SQYVKQGITQ WITGWKRKGW LTANREPVKN VDLWQQLDAE VARHQVEWLW
VKGHSGHPEN ERCDELAREA ASGPSLADDT GYRP
//
