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Database: UniProt
Entry: A0A0A8DV91_9XANT
LinkDB: A0A0A8DV91_9XANT
Original site: A0A0A8DV91_9XANT 
ID   A0A0A8DV91_9XANT        Unreviewed;       152 AA.
AC   A0A0A8DV91;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:UYK89804.1};
GN   ORFNames=FHR56_002191 {ECO:0000313|EMBL:MBB6367078.1}, NG824_05065
GN   {ECO:0000313|EMBL:UYK89804.1};
OS   Xanthomonas sacchari.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=56458 {ECO:0000313|EMBL:MBB6367078.1, ECO:0000313|Proteomes:UP000535971};
RN   [1] {ECO:0000313|EMBL:MBB6367078.1, ECO:0000313|Proteomes:UP000535971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F10 {ECO:0000313|EMBL:MBB6367078.1,
RC   ECO:0000313|Proteomes:UP000535971};
RA   Potnis N.;
RT   "Studying the diversity of plant-associated saprophytic bacteria and their
RT   role in host health and plant-pathogen interactions.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:UYK89804.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JR3-14 {ECO:0000313|EMBL:UYK89804.1};
RA   Liao K., Zhang X.;
RT   "Dynamics of rice microbiomes reveals core vertical transmitted seed
RT   endophytes.";
RL   Submitted (JUN-2022) 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}.
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DR   EMBL; JACHNP010000001; MBB6367078.1; -; Genomic_DNA.
DR   EMBL; CP099534; UYK89804.1; -; Genomic_DNA.
DR   RefSeq; WP_017907823.1; NZ_JANFXE010000008.1.
DR   KEGG; xsa:SB85_07675; -.
DR   HOGENOM; CLU_030894_6_0_6; -.
DR   Proteomes; UP000535971; Unassembled WGS sequence.
DR   Proteomes; UP001164392; 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};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000313|EMBL:MBB6367078.1};
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}.
FT   DOMAIN          1..141
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ   SEQUENCE   152 AA;  16951 MW;  C30F8F0F17DF5096 CRC64;
     MKTVDIHTDG ACLGNPGPGG WAALLRYKGL EREVAGAEAH TTNNRMELMA AIMALETLNE
     PCQIVLHTDS QYVRQGITEW MPGWVRRQWK TAGGDPVKNR DLWERLHAAA QRHTIDWRWV
     KGHNGDPDNE RVDQLARNQA LHVRAGGAAV AT
//
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