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Database: UniProt
Entry: A0A5R9GNK1_9PROT
LinkDB: A0A5R9GNK1_9PROT
Original site: A0A5R9GNK1_9PROT 
ID   A0A5R9GNK1_9PROT        Unreviewed;       259 AA.
AC   A0A5R9GNK1;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN   ORFNames=FEF65_07250 {ECO:0000313|EMBL:TLS67228.1};
OS   Mariprofundus erugo.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=2528639 {ECO:0000313|EMBL:TLS67228.1, ECO:0000313|Proteomes:UP000306585};
RN   [1] {ECO:0000313|EMBL:TLS67228.1, ECO:0000313|Proteomes:UP000306585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3 {ECO:0000313|EMBL:TLS67228.1,
RC   ECO:0000313|Proteomes:UP000306585};
RX   PubMed=31076431;
RA   Garrison C.E., Price K.A., Field E.K.;
RT   "Environmental Evidence and Genomic Insight of Iron-oxidizing Bacteria
RT   Preference Towards More Corrosion Resistant Stainless Steel at Higher
RT   Salinities.";
RL   Appl. Environ. Microbiol. 0:0-0(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300}.
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:TLS67228.1}.
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DR   EMBL; VBRY01000006; TLS67228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5R9GNK1; -.
DR   Proteomes; UP000306585; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   CDD; cd09278; RNase_HI_prokaryote_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; IPR017067; RNase_H1_euk.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_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; PF01693; Cauli_VI; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   PIRSF; PIRSF036852; Ribonuclease_H1_euk; 2.
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   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000306585}.
FT   DOMAIN          87..235
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          47..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  28589 MW;  FEABC7201EFE00CE CRC64;
     MAQKFYVVWH GRETGIFTDW ATCKKQVDQF TGARYKSFPT RAEAEAAFHG KPAGTGRASD
     PATTTPARKR TTAQTVKTYD AAEIAAMRID TKIFTDGGCE PNPGKAGSGV AVYRDGIVAE
     LWYGLFNPKG TNNTAELNAL HQALLMARKE LEQGRSVAIF CDSKYAIQCI TQWAIGWQKK
     GWKKAGGEIK NLELIKEMFA LHQQLKEKVQ VLHVNGHVGV EGNELADRMS ILTIETKTAE
     FKRYSETLDV SALLAMRAG
//
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