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Database: UniProt
Entry: A0A0A2UE50_9BACL
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ID   A0A0A2UE50_9BACL        Unreviewed;       220 AA.
AC   A0A0A2UE50;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE            EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN   ORFNames=P364_0102250 {ECO:0000313|EMBL:KGP85023.1};
OS   Paenibacillus sp. MAEPY2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP85023.1, ECO:0000313|Proteomes:UP000030061};
RN   [1] {ECO:0000313|EMBL:KGP85023.1, ECO:0000313|Proteomes:UP000030061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP85023.1,
RC   ECO:0000313|Proteomes:UP000030061};
RX   PubMed=24526641;
RA   Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT   "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT   MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|PIRNR:PIRNR037839}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037839};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037839-1};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037839-1};
CC       Note=Binds 2 metal ions per subunit. Manganese or magnesium.
CC       {ECO:0000256|PIRSR:PIRSR037839-1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037839}.
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|PIRNR:PIRNR037839}.
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:KGP85023.1}.
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DR   EMBL; AWUK01000004; KGP85023.1; -; Genomic_DNA.
DR   RefSeq; WP_024628557.1; NZ_AWUK01000004.1.
DR   AlphaFoldDB; A0A0A2UE50; -.
DR   eggNOG; COG0328; Bacteria.
DR   eggNOG; COG3341; Bacteria.
DR   OrthoDB; 9811552at2; -.
DR   Proteomes; UP000030061; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   InterPro; IPR017290; RNase_H_bac.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   PIRSF; PIRSF037839; Ribonuclease_H; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037839};
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR037839};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037839};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR037839, ECO:0000256|PIRSR:PIRSR037839-1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR037839-1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037839,
KW   ECO:0000256|PIRSR:PIRSR037839-1}; Nuclease {ECO:0000256|PIRNR:PIRNR037839}.
FT   DOMAIN          86..220
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          60..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ   SEQUENCE   220 AA;  24157 MW;  5A0C1D487CDBB3DC CRC64;
     MAKQKYYVVW AGKQPGIYST WAECKAQTDH FTGAKYKSYE SKAAAEEAYR AGWKGNWGTG
     ASGSGSASKT KSGSSGRSAG METSAEIDYD SISVDVGTRG NPGPVEYKGV DTRTGEIIFS
     VGPISKGTNN LGEFLAIVHA LAYLKKEGST KTVYTDSVNA MKWLKQKAVS TTLARDASTE
     EIWLMIDRAE QWLRTNTYSN KVLKWQTKQW GEIKADYGRK
//
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