ID S3Y1Y4_9ACTN Unreviewed; 297 AA.
AC S3Y1Y4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF1531_01696 {ECO:0000313|EMBL:EPH02390.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02390.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH02390.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02390.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EPH02390.1}.
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DR EMBL; ATFL01000014; EPH02390.1; -; Genomic_DNA.
DR RefSeq; WP_016669486.1; NZ_KE340297.1.
DR AlphaFoldDB; S3Y1Y4; -.
DR STRING; 1203605.HMPREF1531_01696; -.
DR PATRIC; fig|1203605.3.peg.1751; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_030894_1_0_11; -.
DR OrthoDB; 7845843at2; -.
DR Proteomes; UP000014567; 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; 3.10.450.50; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00042; RNase_H; 1.
DR InterPro; IPR027843; DUF4440.
DR InterPro; IPR032710; NTF2-like_dom_sf.
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; PF14534; DUF4440; 1.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF54427; NTF2-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|HAMAP-Rule:MF_00042};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00042};
KW 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|HAMAP-Rule:MF_00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000014567}.
FT DOMAIN 1..136
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 131..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00042"
SQ SEQUENCE 297 AA; 33061 MW; 7DE081DC6C95C35F CRC64;
MITASVDGSA LSNPGPAGWA WYIDEDRWDA DGWEHGTNNM GELQAIIEVL AATPPDEELH
ILCDSTYVIN SVTKWMPGWK RKGWKKADGQ PVLNQDQLKT IDEALQGRKV TFEWVKGHAG
HQMNEAADER ARNAASAYQR GTVPPRGPGY RPGKVDPAPV ADRGGDDLFS AGADEPSLPR
KPAGADPDIM TTISQEKELL SDKVRCDVSR VRTLLHADFT EFSSSGQIWT RSRLLAEIKP
LPLRIGFEPI RAQRLSDDLI LLLWRATTPT HSWLRSSLWR RGDGRWQLLF CQGTQAS
//
