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Database: UniProt
Entry: A0A066TUT8_9NEIS
LinkDB: A0A066TUT8_9NEIS
Original site: A0A066TUT8_9NEIS 
ID   A0A066TUT8_9NEIS        Unreviewed;       144 AA.
AC   A0A066TUT8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   ORFNames=BHC48_03555 {ECO:0000313|EMBL:PIT51762.1}, SALWKB29_0182
GN   {ECO:0000313|EMBL:KDN15763.1};
OS   Snodgrassella alvi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196083 {ECO:0000313|EMBL:KDN15763.1, ECO:0000313|Proteomes:UP000027170};
RN   [1] {ECO:0000313|EMBL:KDN15763.1, ECO:0000313|Proteomes:UP000027170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wkB29 {ECO:0000313|Proteomes:UP000027170}, and WkB29
RC   {ECO:0000313|EMBL:KDN15763.1};
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "The genomes of two eusocial bee gut symbionts.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PIT51762.1, ECO:0000313|Proteomes:UP000231484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Occ4-2 {ECO:0000313|EMBL:PIT51762.1,
RC   ECO:0000313|Proteomes:UP000231484};
RA   Steele M.I., Kwong W.K., Powell J.E., Whiteley M., Moran N.A.;
RT   "Type VI secretion-mediated competition in the bee gut microbiome.";
RL   MBio 0:0-0(2017).
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:KDN15763.1}.
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DR   EMBL; JFZV01000001; KDN15763.1; -; Genomic_DNA.
DR   EMBL; MEIQ01000027; PIT51762.1; -; Genomic_DNA.
DR   RefSeq; WP_037405035.1; NZ_CAJZCD010000003.1.
DR   AlphaFoldDB; A0A066TUT8; -.
DR   GeneID; 75157075; -.
DR   eggNOG; COG0328; Bacteria.
DR   OrthoDB; 7845843at2; -.
DR   Proteomes; UP000027170; Unassembled WGS sequence.
DR   Proteomes; UP000231484; 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:KDN15763.1};
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   144 AA;  16035 MW;  DF6D9A7A7A5CDB7C CRC64;
     MSEVTLYTDG ACKGNPGVGG WGAFLQSGRH SKELFGGEAN TTNNRMELTA VIQGLAALKR
     PCIVNIYTDS QYVKNGMQEW IHNWKARGWK TASKQPVKNV ELWQALDAEV NKHQVHWHWI
     KGHAGNPGNE KADELANRGV ELIK
//
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