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Database: UniProt
Entry: A0A0S2JGU4_9GAMM
LinkDB: A0A0S2JGU4_9GAMM
Original site: A0A0S2JGU4_9GAMM 
ID   A0A0S2JGU4_9GAMM        Unreviewed;       269 AA.
AC   A0A0S2JGU4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN   ORFNames=CMT41_11300 {ECO:0000313|EMBL:ALO35238.1};
OS   Colwellia sp. MT41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO35238.1, ECO:0000313|Proteomes:UP000065319};
RN   [1] {ECO:0000313|EMBL:ALO35238.1, ECO:0000313|Proteomes:UP000065319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT41 {ECO:0000313|EMBL:ALO35238.1,
RC   ECO:0000313|Proteomes:UP000065319};
RA   Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA   Yayanos A., Methe B.A., Bartlett D.H.;
RT   "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT   Colwellia.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP013145; ALO35238.1; -; Genomic_DNA.
DR   RefSeq; WP_058027315.1; NZ_CP013145.1.
DR   AlphaFoldDB; A0A0S2JGU4; -.
DR   STRING; 58049.CMT41_11300; -.
DR   KEGG; com:CMT41_11300; -.
DR   OrthoDB; 7845843at2; -.
DR   Proteomes; UP000065319; Chromosome.
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:UP000065319}.
FT   DOMAIN          94..245
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          63..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  29540 MW;  0CDFBE4B89D4A55D CRC64;
     MSKKFYVIWK GAKTGIFTTW PEVQQHTAGR SDAQYMGFES KGAAEQAFAA TYTKALMQRS
     LNNKGTASTA PNSSRKASSS KGTRAKTATV SPNGPSDIEI YCDGACSPNP GKSGTGIAVY
     EQGKVTSLYY GLYEKNGTNN TAELNGLLSS FQLAQHFIDK DKEQSICILS DSKYSIDCIT
     KWAKGWQAKG WTRGKGEEVK NLALVQQCYA LYKTMHTKIT IRHVKAHANI EGNELADRMA
     VLARKQHQET MIRYSEVIDI KALLALQSG
//
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