ID A0A089ILW4_9BACL Unreviewed; 220 AA.
AC A0A089ILW4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN ORFNames=H70737_22375 {ECO:0000313|EMBL:AIQ25366.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ25366.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ25366.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ25366.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP009279; AIQ25366.1; -; Genomic_DNA.
DR RefSeq; WP_042190614.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089ILW4; -.
DR KEGG; paej:H70737_22375; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG3341; Bacteria.
DR HOGENOM; CLU_080985_1_0_9; -.
DR Proteomes; UP000029519; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029519}.
FT DOMAIN 82..220
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
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; 24235 MW; 7CD7199C312A597E CRC64;
MAKQKYYVVW EGKQPGVYST WAECQAQTDH YTGAKYKSYE SKAAADAAYT AGWKGNWGTG
SSASGAAKSK GTSSFKRSAT VETSAEIDYN SISVDVGTRG NPGPVEYKGV DTQTGDIIFS
CGPIKKGTNN LGEFLAIVHA LALLKKEGST KTVYSDSVNA MKWVKQKKVA TTLPRDASTE
EIWVLIDRAE RWLQTNTYDN KVLKWQTKEW GEIKADYGRK
//
