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Database: UniProt
Entry: Q49X17
LinkDB: Q49X17
Original site: Q49X17 
ID   RNC_STAS1               Reviewed;         244 AA.
AC   Q49X17;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   26-NOV-2014, entry version 61.
DE   RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE            EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE   AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104};
DE            Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN   Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=SSP1536;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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). Processes some mRNAs, and
CC       tRNAs when they are encoded in the rRNA operon. Processes pre-
CC       crRNA and tracrRNA of type II CRISPR loci if present in the
CC       organism. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00104}.
CC   -!- SIMILARITY: Contains 1 RNase III domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00104}.
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DR   EMBL; AP008934; BAE18681.1; -; Genomic_DNA.
DR   RefSeq; WP_011303283.1; NC_007350.1.
DR   RefSeq; YP_301626.1; NC_007350.1.
DR   ProteinModelPortal; Q49X17; -.
DR   STRING; 342451.SSP1536; -.
DR   EnsemblBacteria; BAE18681; BAE18681; SSP1536.
DR   GeneID; 3615182; -.
DR   KEGG; ssp:SSP1536; -.
DR   PATRIC; 19624662; VBIStaSap90642_1538.
DR   eggNOG; COG0571; -.
DR   HOGENOM; HOG000246808; -.
DR   KO; K03685; -.
DR   OMA; NIHGNIF; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; SSAP342451:GKFA-1595-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-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; IPR014720; dsRNA-bd_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   PANTHER; PTHR11207; PTHR11207; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 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; Reference proteome;
KW   RNA-binding; rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN         1    244       Ribonuclease 3.
FT                                /FTId=PRO_0000228586.
FT   DOMAIN       17    146       RNase III. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   DOMAIN      172    241       DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     63     63       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    135    135       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   METAL        59     59       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       132    132       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       135    135       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
SQ   SEQUENCE   244 AA;  28228 MW;  7842F44C2CAF6465 CRC64;
     MTNQKKKEMV QTFQNKFEKK MQELNLDFNR VDLYQQAFSH SSFINDFNMN RLDHNERLEF
     LGDAVLELTV SRYLFDKYPE LPEGNLTKMR ATIVCEPSLV IFANKIQLND LILLGKGEEK
     TGGRTRPSLV SDAFEAFVGA LYLDQGLEAV WQFSEQIIFP YVEDDELDGV VDFKTQFQEY
     VHRQNKGDVT YRLINEEGPA HHRLFTSEVI LEEDAVAEGK GKTKKESEQK AAERAYKILK
     NKNA
//
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