GenomeNet

Database: UniProt
Entry: Q3IDL2
LinkDB: Q3IDL2
Original site: Q3IDL2 
ID   RNC_PSEHT               Reviewed;         225 AA.
AC   Q3IDL2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   01-OCT-2014, entry version 58.
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};
GN   OrderedLocusNames=PSHAa0732;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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: Mg(2+). {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI85815.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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; CR954246; CAI85815.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_339258.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDL2; -.
DR   STRING; 326442.PSHAa0732; -.
DR   EnsemblBacteria; CAI85815; CAI85815; PSHAa0732.
DR   GeneID; 3710610; -.
DR   KEGG; pha:PSHAa0732; -.
DR   PATRIC; 32294991; VBIPseHal105694_0695.
DR   eggNOG; COG0571; -.
DR   HOGENOM; HOG000246809; -.
DR   KO; K03685; -.
DR   OrthoDB; EOG6T1WVS; -.
DR   BioCyc; PHAL326442:GJIU-741-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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    225       Ribonuclease 3.
FT                                /FTId=PRO_0000228565.
FT   DOMAIN        5    127       RNase III. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   DOMAIN      154    223       DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     44     44       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    116    116       {ECO:0000255|HAMAP-Rule:MF_00104}.
FT   METAL        40     40       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       113    113       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
FT   METAL       116    116       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00104}.
SQ   SEQUENCE   225 AA;  25072 MW;  E2E7B195B90A8220 CRC64;
     MKKNVTELYK TIDYIFADQG LLEQAMTHRS HKGQHNERLE FLGDSILSFV IANALYAKFP
     KAREGDLSRM RSTLVRGQTL AEFGLEFGLG DYLRLGPGEL KSGGFRREST LADAVEAIIG
     AVFLDSDIER CGELILSWYE ERLNAISPGL NQKDPKTLLQ EHLQARKLSL PGYTVVDTKG
     QAHNQTFTVE CIVDGMDSII SVGSSRRKAE QKAAEKALKI LKNEP
//
DBGET integrated database retrieval system