ID A0A143HCQ1_9BACL Unreviewed; 314 AA.
AC A0A143HCQ1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ribonuclease HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE Short=RNase HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00053};
GN Name=rnhC {ECO:0000256|HAMAP-Rule:MF_00053};
GN ORFNames=ATY39_08855 {ECO:0000313|EMBL:AMW99557.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW99557.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMW99557.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMW99557.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|ARBA:ARBA00004065, ECO:0000256|HAMAP-
CC Rule:MF_00053}.
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_00053, ECO:0000256|PROSITE-ProRule:PRU01319};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00053,
CC ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00053,
CC ECO:0000256|PROSITE-ProRule:PRU01319};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000256|HAMAP-Rule:MF_00053, ECO:0000256|PROSITE-
CC ProRule:PRU01319};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00053}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000256|ARBA:ARBA00008378, ECO:0000256|HAMAP-Rule:MF_00053}.
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DR EMBL; CP014806; AMW99557.1; -; Genomic_DNA.
DR RefSeq; WP_066788718.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HCQ1; -.
DR STRING; 241244.ATY39_08855; -.
DR KEGG; rst:ATY39_08855; -.
DR OrthoDB; 9777935at2; -.
DR Proteomes; UP000076021; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; cd06590; RNase_HII_bacteria_HIII_like; 1.
DR CDD; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR HAMAP; MF_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR NCBIfam; TIGR00716; rnhC; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF25; RIBONUCLEASE HIII; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00053};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00053};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00053};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00053};
KW Reference proteome {ECO:0000313|Proteomes:UP000076021}.
FT DOMAIN 93..310
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 100
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 314 AA; 34349 MW; CC5B7EC403B13E97 CRC64;
MSTIVLNLND TVQKEVMSTY SRHMVDRKAP GVIFAAKLPD CAITVYRSGK VMFQGNGGDR
EAEKWSQGGI EPASSVKKTS SKGDLLPPNF ADLSVVGSDE TGTGDYFGPI TVAAVYVPKE
RIQLVKELGV KDSKMLTDDF MRKIAPDLKA SLLHHVLILR NPKYNAMQAS GMSQGKMKAK
LHNQALLKLL QKIAPDKPDH ILIDQFAERN TYYNYLKGDK EVVRDQVLFA TKAEQLHVAV
AAASILARCA FLNEMDKLSK LVGTTLPKGA GPKVDEVAAQ ILLAQGEEAL NNITKWHFAN
TGKASRIASK SRPL
//
