ID I7GT96_9HELI Unreviewed; 239 AA.
AC I7GT96;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN Name=rnhB {ECO:0000313|EMBL:EFR46631.1};
GN ORFNames=HCBAA847_0855 {ECO:0000313|EMBL:BAM32093.1}, HCCG_01178
GN {ECO:0000313|EMBL:EFR46631.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM32093.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:EFR46631.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 18818 {ECO:0000313|EMBL:EFR46631.1};
RG The Broad Institute Genome Sequencing Platform;
RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Helicobacter cinaedi strain CCUG 18818.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAM32093.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM32093.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
RN [3] {ECO:0000313|EMBL:BAM32093.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM32093.1};
RA Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000005755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 18818 {ECO:0000313|Proteomes:UP000005755};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|ARBA:ARBA00004065,
CC ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
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|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={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|PROSITE-ProRule:PRU01319};
CC -!- SIMILARITY: Belongs to the RNase HII family.
CC {ECO:0000256|ARBA:ARBA00007383, ECO:0000256|RuleBase:RU003515}.
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DR EMBL; AP012492; BAM32093.1; -; Genomic_DNA.
DR EMBL; DS990392; EFR46631.1; -; Genomic_DNA.
DR AlphaFoldDB; I7GT96; -.
DR KEGG; hcb:HCBAA847_0855; -.
DR PATRIC; fig|1206745.3.peg.889; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_3_1_7; -.
DR OrthoDB; 9803420at2; -.
DR Proteomes; UP000005755; Unassembled WGS sequence.
DR Proteomes; UP000006036; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR022898; RNase_HII.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 1.
DR Pfam; PF01351; RNase_HII; 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};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319}.
FT DOMAIN 1..239
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 239 AA; 26655 MW; 2F74A9161BD70357 CRC64;
MWLAGIDEAG RGCICGALFV AGVIGREENI AHFGAKDSKK LSPKQRERIY QTLLESQHKG
EIGLFVAQIE AWEIDKFGLS IAMKNGIEQI LCRIADFATL QNLIGQNVEQ NTAKHNLLEQ
DVEQNPTDST DSKNALQEII MDGNTTFQAK IPHILTQSGV GVQTLVKADD IMPIVSCASI
VAKVSKDRQM HELDKLYPQY FLAKNKGYGT LQHKKAIAKN GYCPHHRKSF KILMQECLF
//
