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Database: UniProt
Entry: M7N2A6_9FLAO
LinkDB: M7N2A6_9FLAO
Original site: M7N2A6_9FLAO 
ID   M7N2A6_9FLAO            Unreviewed;       213 AA.
AC   M7N2A6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Ribonuclease H {ECO:0000256|PIRNR:PIRNR037839};
DE            EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR037839};
GN   ORFNames=D778_01759 {ECO:0000313|EMBL:EMQ95869.1}, DHV22_16765
GN   {ECO:0000313|EMBL:HCY83129.1};
OS   Xanthomarina gelatinilytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Xanthomarina.
OX   NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ95869.1, ECO:0000313|Proteomes:UP000012024};
RN   [1] {ECO:0000313|EMBL:EMQ95869.1, ECO:0000313|Proteomes:UP000012024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK20 {ECO:0000313|EMBL:EMQ95869.1,
RC   ECO:0000313|Proteomes:UP000012024};
RA   Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Formosa sp. AK20.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HCY83129.1, ECO:0000313|Proteomes:UP000263268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBA10227 {ECO:0000313|EMBL:HCY83129.1};
RX   PubMed=30148503; DOI=.1038/nbt.4229;
RA   Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA   Chaumeil P.A., Hugenholtz P.;
RT   "A standardized bacterial taxonomy based on genome phylogeny substantially
RT   revises the tree of life.";
RL   Nat. Biotechnol. 36:996-1004(2018).
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:EMQ95869.1}.
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DR   EMBL; ANLA01000004; EMQ95869.1; -; Genomic_DNA.
DR   EMBL; DPRK01000269; HCY83129.1; -; Genomic_DNA.
DR   RefSeq; WP_007647139.1; NZ_ANLA01000004.1.
DR   AlphaFoldDB; M7N2A6; -.
DR   PATRIC; fig|1137281.3.peg.359; -.
DR   eggNOG; COG0328; Bacteria.
DR   eggNOG; COG3341; Bacteria.
DR   OrthoDB; 9811552at2; -.
DR   Proteomes; UP000012024; Unassembled WGS sequence.
DR   Proteomes; UP000263268; 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:UP000012024}.
FT   DOMAIN          79..213
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037839-1"
SQ   SEQUENCE   213 AA;  24500 MW;  DD2EB7A05A6468D9 CRC64;
     MSKKKKKYYT VWKGHKTGVF ESWHDCKAQI KDFEGAQYKS FETFDAAKKA LNGNYKDYIG
     KNKKFSSSLT EDQLKKIGQP NYHSISVDAA SSGNPGKMEY RGVDTKTKKQ LFIQGPFEEG
     TNNIGEFLAI VHGLAFLKQH NSDRIIYTDS KTAMSWVKKK SCNTKLERNQ KNKTLFELVD
     RAVNWLKENN YTTTIVKWET KAWGEIPADF GRK
//
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