ID X8H1Y0_9FIRM Unreviewed; 220 AA.
AC X8H1Y0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ribonuclease H {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|PIRNR:PIRNR037839};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|PIRNR:PIRNR037839};
GN ORFNames=HMPREF1504_1696 {ECO:0000313|EMBL:EUB20765.1};
OS Veillonella sp. ICM51a.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=936591 {ECO:0000313|EMBL:EUB20765.1, ECO:0000313|Proteomes:UP000020651};
RN [1] {ECO:0000313|EMBL:EUB20765.1, ECO:0000313|Proteomes:UP000020651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM51a {ECO:0000313|EMBL:EUB20765.1,
RC ECO:0000313|Proteomes:UP000020651};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037839}.
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|ARBA:ARBA00005300, 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:EUB20765.1}.
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DR EMBL; JAPX01000048; EUB20765.1; -; Genomic_DNA.
DR RefSeq; WP_038125184.1; NZ_JAPX01000048.1.
DR AlphaFoldDB; X8H1Y0; -.
DR PATRIC; fig|936591.3.peg.1756; -.
DR Proteomes; UP000020651; 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 GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd09277; RNase_HI_bacteria_like; 1.
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 PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
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, ECO:0000313|EMBL:EUB20765.1};
KW Magnesium {ECO:0000256|PIRNR:PIRNR037839};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037839};
KW Nuclease {ECO:0000256|PIRNR:PIRNR037839}.
FT DOMAIN 80..217
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
SQ SEQUENCE 220 AA; 24620 MW; 5277BF63AEEB85CE CRC64;
MAKKFYAVKA GRTPGIYETW SDCEKQVKGF GGAIYKSFPT KSEAQAFIGD EGVSIGDYLA
SSKTSKTNHT KKSIAPDFSE TNHLIAYIDG SYDKYNQSVG SGGIMFLNGN KETFSFGTKD
EKYTEFWNVS GELLAAMHVM EYALTHGISK CSLYYDYMGI EMWATKKWKR NNVLTNEYAA
FCERIFSHVK VYFHKVHAHT GDTYNEMADQ LAKAGAAIGK
//
