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Database: UniProt/TrEMBL
Entry: B4RNJ6_NEIG2
LinkDB: B4RNJ6_NEIG2
Original site: B4RNJ6_NEIG2 
ID   B4RNJ6_NEIG2            Unreviewed;       174 AA.
AC   B4RNJ6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   26-NOV-2014, entry version 39.
DE   RecName: Full=Ribonuclease H {ECO:0000256|HAMAP-Rule:MF_00042};
DE            Short=RNase H {ECO:0000256|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00042};
GN   Name=rnhA {ECO:0000256|HAMAP-Rule:MF_00042};
GN   OrderedLocusNames=NGK_2020 {ECO:0000313|EMBL:ACF30635.1};
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=521006 {ECO:0000313|EMBL:ACF30635.1, ECO:0000313|Proteomes:UP000002564};
RN   [1] {ECO:0000313|EMBL:ACF30635.1, ECO:0000313|Proteomes:UP000002564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945 {ECO:0000313|EMBL:ACF30635.1,
RC   ECO:0000313|Proteomes:UP000002564};
RX   PubMed=18586945; DOI=10.1128/JB.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00016438}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00016435}.
CC   -!- COFACTOR:
CC       Note=Binds 1 magnesium ion per subunit. May bind a second metal
CC       ion at a regulatory site, or after substrate binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000256|SAAS:SAAS00016447};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00016404}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00016421}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000256|HAMAP-
CC       Rule:MF_00042}.
CC   -!- SIMILARITY: Contains 1 RNase H domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00042}.
CC   -!- SIMILARITY: Contains RNase H domain.
CC       {ECO:0000256|SAAS:SAAS00016450}.
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DR   EMBL; CP001050; ACF30635.1; -; Genomic_DNA.
DR   RefSeq; YP_002002645.1; NC_011035.1.
DR   ProteinModelPortal; B4RNJ6; -.
DR   STRING; 521006.NGK_2020; -.
DR   EnsemblBacteria; ACF30635; ACF30635; NGK_2020.
DR   GeneID; 6449275; -.
DR   KEGG; ngk:NGK_2020; -.
DR   eggNOG; COG0328; -.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   OMA; DSAYVKN; -.
DR   OrthoDB; EOG696BTR; -.
DR   BioCyc; NGON521006:GJ73-2062-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00042; RNase_H; 1.
DR   InterPro; IPR022892; RNaseH.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   InterPro; IPR002156; RNaseH_domain.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002564};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016445};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016426};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016425};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016427};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016420};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00016416}.
FT   DOMAIN       30    171       RNase H. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        39     39       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        39     39       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        77     77       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        99     99       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL       163    163       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
SQ   SEQUENCE   174 AA;  19493 MW;  66017872D99CBD2E CRC64;
     MPISIRRNLS DGTTHKPLII TPDTTQRHDM DTPVYLYTDG ACKGNPGAGG WGVLMRYGSR
     EKELFGGEAQ TTNNRMELTA VIEGLKSLKR RCTVIICTDS QYVKNGMENW IHGWKRNGWK
     TAAKQPVKND DLWQELDALV GQHQVSWTWV KGHAGHAENE RADDLANRGA AQFS
//
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