ID RNC_MYCS5 Reviewed; 231 AA.
AC Q4A589;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=MS53_0675;
OS Mycoplasma synoviae (strain 53).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=262723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53;
RX PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R.,
RA Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S.,
RA Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A.,
RA Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W.,
RA Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C.,
RA Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R.,
RA Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C.,
RA Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P.,
RA Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P.,
RA Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M.,
RA Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M.,
RA Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M.,
RA Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S.,
RA Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C.,
RA Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R.,
RA Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W.,
RA Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two
RT strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma
RT synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing
CC of primary rRNA transcript to yield the immediate precursors to
CC the large and small rRNAs (23S and 16S). Also processes some
CC mRNAs, and tRNAs when they are encoded in the rRNA operon (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC phosphomonoester.
CC -!- COFACTOR: Mg(2+) (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 RNase III domain.
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DR EMBL; AE017245; AAZ44082.1; -; Genomic_DNA.
DR RefSeq; YP_278793.1; NC_007294.1.
DR ProteinModelPortal; Q4A589; -.
DR STRING; 262723.MS53_0675; -.
DR EnsemblBacteria; AAZ44082; AAZ44082; MS53_0675.
DR GeneID; 3564469; -.
DR KEGG; msy:MS53_0675; -.
DR PATRIC; 20026032; VBIMycSyn118523_0717.
DR eggNOG; COG0571; -.
DR HOGENOM; HOG000246808; -.
DR KO; K03685; -.
DR OMA; KHEAEEN; -.
DR BioCyc; MSYN262723:GH37-703-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:HAMAP.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:HAMAP.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1520.10; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR HAMAP; MF_00104; RNase_III; 1; -.
DR InterPro; IPR001159; Ds-RNA-bd.
DR InterPro; IPR014720; dsRNA-bd-like_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; RNase_III; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; mRNA processing; Nuclease; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1 231 Ribonuclease 3.
FT /FTId=PRO_0000228552.
FT DOMAIN 12 139 RNase III.
FT DOMAIN 165 231 DRBM.
FT ACT_SITE 56 56 Potential.
FT ACT_SITE 128 128 By similarity.
FT METAL 52 52 Magnesium (By similarity).
FT METAL 125 125 Magnesium (By similarity).
FT METAL 128 128 Magnesium (By similarity).
SQ SEQUENCE 231 AA; 26235 MW; BF47EE3F88964D7F CRC64;
MEKDNQPSIE ELKAFLQKNN IEYKNIDLFI EATTHKTYSK VNKNSKDYER LEFLGDSLVG
FLISDYCVRE FSSLEPGELS RLRSKLVDKL ALFKIAQKLK VEQIIKTGPK KARNEVLSSS
NVLSDVVEAL IAAIYLDQGM QSAKDFIKSH FYEIANKAQN KPNKDPKSEL QEYFQTISAE
TVKYETIEIP NKRSFESKAW HLNKIYGTGV GLSKKDAEKN AAANALSKLK T
//
