ID J6H4E1_9PORP Unreviewed; 251 AA.
AC J6H4E1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN ORFNames=HMPREF1323_0408 {ECO:0000313|EMBL:EJU17933.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU17933.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU17933.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU17933.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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}.
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:EJU17933.1}.
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DR EMBL; ALKJ01000009; EJU17933.1; -; Genomic_DNA.
DR AlphaFoldDB; J6H4E1; -.
DR PATRIC; fig|1125723.3.peg.212; -.
DR Proteomes; UP000004156; 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 Pfam; PF00075; RNase_H; 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:UP000004156}.
FT DOMAIN 115..251
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ SEQUENCE 251 AA; 28081 MW; FCA61C87C8AA91C5 CRC64;
MPSVATSLID VEAVARGIVV LLGTAPTTGD GSKRLHPRAS KPMAKQQKWY VVWAGHEPGV
YETWAECQRQ TQGYPKALFK SFESRSEALR AYEEGFQGFS RRHRAPSGME SSTEAPIEEA
LAVDAACSGN PGVMEYRGVY LPSRRVIFEM GPFPKGTNNI GEFLAIVHAL ALIEKQGLSQ
LVIYSDSQTA LGWVRKKRCK TLLERTAETA PLFDLIERAE RWLQTHTYTT PLYKWDTVRW
GEIPADYGRK G
//
