ID U2E713_9GAMM Unreviewed; 146 AA.
AC U2E713;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:ERJ19526.1};
GN ORFNames=SSPSH_001599 {ECO:0000313|EMBL:ERJ19526.1};
OS Salinisphaera shabanensis E1L3A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ19526.1, ECO:0000313|Proteomes:UP000006242};
RN [1] {ECO:0000313|EMBL:ERJ19526.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ19526.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=21705588; DOI=10.1128/JB.05459-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT the harsh, variable environment of the brine-seawater interface of the
RT Shaban Deep in the Red Sea.";
RL J. Bacteriol. 193:4555-4556(2011).
RN [2] {ECO:0000313|EMBL:ERJ19526.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ19526.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
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:ERJ19526.1}.
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DR EMBL; AFNV02000009; ERJ19526.1; -; Genomic_DNA.
DR RefSeq; WP_006915482.1; NZ_AFNV02000009.1.
DR AlphaFoldDB; U2E713; -.
DR STRING; 1033802.SSPSH_001599; -.
DR eggNOG; COG0328; Bacteria.
DR OrthoDB; 7845843at2; -.
DR Proteomes; UP000006242; 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000313|EMBL:ERJ19526.1};
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:UP000006242}.
FT DOMAIN 1..142
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
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 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 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 146 AA; 16341 MW; 883D47B804F74D50 CRC64;
MSEPVVIYTD GACRGNPGPG GWGALLRHGE NTRELCGGEA NTTNNRMELM AAIEALNALK
RACRVELHTD SNYVRQGITS WMHNWKRNGW KTAAKKPVKN DDLWRALDEA TQRHEIEWHW
VKGHSGDPGN EAADALANRG IDELKR
//
