GenomeNet

Database: UniProt/TrEMBL
Entry: F8F3H4_SPICH
LinkDB: F8F3H4_SPICH
Original site: F8F3H4_SPICH 
ID   F8F3H4_SPICH            Unreviewed;       249 AA.
AC   F8F3H4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-APR-2013, entry version 13.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
GN   Name=rnc; OrderedLocusNames=Spica_1404;
OS   Spirochaeta caldaria (strain ATCC 51460 / DSM 7334 / H1).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=744872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51460 / DSM 7334 / H1;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Lu M., Misra M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta caldaria DSM 7334.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002868; AEJ19550.1; -; Genomic_DNA.
DR   RefSeq; YP_004698058.1; NC_015732.1.
DR   EnsemblBacteria; AEJ19550; AEJ19550; Spica_1404.
DR   GeneID; 10946819; -.
DR   KEGG; scd:Spica_1404; -.
DR   KO; K03685; -.
DR   BioCyc; SCAL744872:GHIK-1447-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   DOMAIN       24    151       RNase III (By similarity).
FT   DOMAIN      178    247       DRBM (By similarity).
FT   ACT_SITE     68     68       By similarity.
FT   ACT_SITE    140    140       By similarity.
FT   METAL        64     64       Magnesium (By similarity).
FT   METAL       137    137       Magnesium (By similarity).
FT   METAL       140    140       Magnesium (By similarity).
SQ   SEQUENCE   249 AA;  27880 MW;  10CFF4DC88C54012 CRC64;
     MKDRSIQAVP AGSNTVNSAR KQVLIDFQKT AAIRFRSLEL LNLSFIHRSA SNEFPQKINN
     ERLEFLGDAI LGACTATILY EKLSAQPEGE LAKIKSVVVS EDTLAGIARE LQIDVLLILG
     KGEELSGGRT KKAILADALE ALIGAYYLDS GYKAVFEFIS KYLEVEIERV VTNQHHRDYK
     TLLQEKCQQL YKNYPTYTLL KRTGPDHERM FWVEVHVNGV AYGPGIGKNK KEAEQEAAKL
     AYKAITDIM
//
DBGET integrated database retrieval system