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Database: UniProt
Entry: M2TNC5_9SPHN
LinkDB: M2TNC5_9SPHN
Original site: M2TNC5_9SPHN 
ID   M2TNC5_9SPHN            Unreviewed;       154 AA.
AC   M2TNC5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=C725_1137 {ECO:0000313|EMBL:EMD83236.1};
OS   Pacificimonas flava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingosinicellaceae; Pacificimonas.
OX   NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD83236.1, ECO:0000313|Proteomes:UP000011717};
RN   [1] {ECO:0000313|EMBL:EMD83236.1, ECO:0000313|Proteomes:UP000011717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2015 {ECO:0000313|EMBL:EMD83236.1,
RC   ECO:0000313|Proteomes:UP000011717};
RX   PubMed=23661488;
RA   Tang K., Liu K., Li S., Jiao N.;
RT   "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family
RT   Sphingomonadaceae of the Alphaproteobacteria.";
RL   Genome Announc. 1:E00226-13(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:EMD83236.1}.
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DR   EMBL; AMRV01000003; EMD83236.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2TNC5; -.
DR   PATRIC; fig|1234595.3.peg.1139; -.
DR   OrthoDB; 7845843at2; -.
DR   Proteomes; UP000011717; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042};
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:UP000011717}.
FT   DOMAIN          3..144
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ   SEQUENCE   154 AA;  17408 MW;  F80E015C0464A78E CRC64;
     MMDSDIVEIA TDGACKGNPG RGGWGAVLRY RGQERELYGY EAETTNNRME LMAAIAALSE
     LKRPCQVRLS TDSVYVRDGI TKWVHGWQKK GWKTAARKDV KNRDLWQALL QAARPHRVEW
     KWVKGHAGDP DNERADALAN RAIEERFEAA VKVA
//
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