(data stored in ACNUC7421 zone)

SWISSPROT: C3MHK3_SINFN

ID   C3MHK3_SINFN            Unreviewed;       153 AA.
AC   C3MHK3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=Ribonuclease H {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000256|SAAS:SAAS00728424};
DE            Short=RNase H {ECO:0000256|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000256|SAAS:SAAS00728424};
GN   Name=rnhA {ECO:0000256|HAMAP-Rule:MF_00042,
GN   ECO:0000313|EMBL:ACP24331.1};
GN   OrderedLocusNames=NGR_c05350 {ECO:0000313|EMBL:ACP24331.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24331.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24331.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00728421}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00728447}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00042};
CC       Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion
CC       at a regulatory site, or after substrate binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00728487}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS00821850}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000256|HAMAP-
CC       Rule:MF_00042, ECO:0000256|SAAS:SAAS00728416}.
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DR   EMBL; CP001389; ACP24331.1; -; Genomic_DNA.
DR   RefSeq; WP_012707116.1; NC_012587.1.
DR   RefSeq; YP_002825084.1; NC_012587.1.
DR   ProteinModelPortal; C3MHK3; -.
DR   STRING; 394.NGR_c05350; -.
DR   EnsemblBacteria; ACP24331; ACP24331; NGR_c05350.
DR   GeneID; 7791761; -.
DR   KEGG; rhi:NGR_c05350; -.
DR   PATRIC; fig|394.7.peg.3348; -.
DR   eggNOG; ENOG4108UMW; Bacteria.
DR   eggNOG; COG0328; LUCA.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   OMA; MQEIEIF; -.
DR   OrthoDB; POG091H04XT; -.
DR   Proteomes; UP000001054; Chromosome.
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   CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00042; RNase_H; 1.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR022892; RNaseHI.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHK3.
DR   SWISS-2DPAGE; C3MHK3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00821852};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00728460};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00728437, ECO:0000313|EMBL:ACP24331.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00728497};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00728473};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS00728430};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        1    141       RNase H. {ECO:0000259|PROSITE:PS50879}.
FT   METAL         9      9       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL         9      9       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        47     47       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        69     69       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL       133    133       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
SQ   SEQUENCE   153 AA;  17294 MW;  58D25853143B455E CRC64;
     MKHVDIFTDG ACSGNPGPGG WGAVLRYGEV EKEMFGGEAE TTNNRMELMA AISALNALKQ
     PCEVDLHTDS KYVMDGISKW IHGWKRNGWK TGDRKPVKNG ELWQALDEAR DRHQVTWHWV
     KGHAGHPENE RADELARKGM EPFKKVRRTD AVK
//

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