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Database: UniProt/TrEMBL
Entry: Q31L56_SYNE7
LinkDB: Q31L56_SYNE7
Original site: Q31L56_SYNE7 
ID   Q31L56_SYNE7            Unreviewed;       259 AA.
AC   Q31L56;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   01-MAY-2013, entry version 51.
DE   RecName: Full=Ribonuclease H;
DE            Short=RNase H;
DE            EC=3.1.26.4;
GN   Name=rnhA; OrderedLocusNames=Synpcc7942_2183;
OS   Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. May bind a second
CC       metal ion at a regulatory site, or after substrate binding (By
CC       similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC   -!- SIMILARITY: Contains 1 RNase H domain.
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DR   EMBL; CP000100; ABB58213.1; -; Genomic_DNA.
DR   RefSeq; YP_401200.1; NC_007604.1.
DR   ProteinModelPortal; Q31L56; -.
DR   STRING; 1140.Synpcc7942_2183; -.
DR   EnsemblBacteria; ABB58213; ABB58213; Synpcc7942_2183.
DR   GeneID; 3773740; -.
DR   KEGG; syf:Synpcc7942_2183; -.
DR   PATRIC; 23789875; VBISynElo51371_2458.
DR   eggNOG; COG0328; -.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   ProtClustDB; CLSK895212; -.
DR   BioCyc; SELO1140:GJWQ-2215-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:ribonuclease H activity; IEA:HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:HAMAP.
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; RNaseH_fold; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease.
FT   DOMAIN        2    146       RNase H (By similarity).
FT   METAL        11     11       Magnesium 1 (By similarity).
FT   METAL        11     11       Magnesium 2 (By similarity).
FT   METAL        50     50       Magnesium 1 (By similarity).
FT   METAL        75     75       Magnesium 1 (By similarity).
FT   METAL       138    138       Magnesium 2 (By similarity).
SQ   SEQUENCE   259 AA;  29448 MW;  1CA9C8DAD87C16D9 CRC64;
     MSDAILRLYT DGACTGNPGP GGWGVQIQFA DGTVQELGGR DAATTNNRME LQAAIAALEF
     WRDHSDQQPV TLYTDSEYVI KGITQWLKGW QRKGWKTAAG KPVLNQDLWM HLDDLNSPAV
     QWQYVRGHSG DPGNERCDQI ARSFAQQRPL PLCQRSDAPL QSGQPQQEPV RMPEVVTQEW
     SSNPRDRSQR LRDVLDCLQI AAAIAEQQFL ITSSELADLM DVNASAVTSR GEEWIWRNWR
     VKRDRREGNQ ILWQLERIH
//
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