GenomeNet

Database: UniProt
Entry: K9YYW4_DACSA
LinkDB: K9YYW4_DACSA
Original site: K9YYW4_DACSA 
ID   K9YYW4_DACSA            Unreviewed;       264 AA.
AC   K9YYW4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   31-JUL-2019, entry version 49.
DE   RecName: Full=Ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE            EC=3.1.26.3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE   AltName: Full=Ribonuclease III {ECO:0000256|HAMAP-Rule:MF_00104};
DE            Short=RNase III {ECO:0000256|HAMAP-Rule:MF_00104};
GN   Name=rnc {ECO:0000256|HAMAP-Rule:MF_00104};
GN   ORFNames=Dacsa_3634 {ECO:0000313|EMBL:AFZ52114.1};
OS   Dactylococcopsis salina PCC 8305.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Dactylococcopsis.
OX   NCBI_TaxID=13035 {ECO:0000313|EMBL:AFZ52114.1, ECO:0000313|Proteomes:UP000010482};
RN   [1] {ECO:0000313|EMBL:AFZ52114.1, ECO:0000313|Proteomes:UP000010482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8305 {ECO:0000313|EMBL:AFZ52114.1,
RC   ECO:0000313|Proteomes:UP000010482};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Daligault H.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Dactylococcopsis salina PCC 8305.";
RL   Submitted (APR-2012) 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). 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:0000256|HAMAP-Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00104,
CC         ECO:0000256|SAAS:SAAS01115986};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00104, ECO:0000256|SAAS:SAAS00751453};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00104,
CC       ECO:0000256|SAAS:SAAS00751513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104,
CC       ECO:0000256|SAAS:SAAS00751438}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family.
CC       {ECO:0000256|SAAS:SAAS00809456}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003944; AFZ52114.1; -; Genomic_DNA.
DR   STRING; 13035.Dacsa_3634; -.
DR   EnsemblBacteria; AFZ52114; AFZ52114; Dacsa_3634.
DR   KEGG; dsl:Dacsa_3634; -.
DR   PATRIC; fig|13035.3.peg.4116; -.
DR   KO; K03685; -.
DR   BioCyc; DSAL13035:G1HCV-3641-MONOMER; -.
DR   Proteomes; UP000010482; Chromosome.
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-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF00636; Ribonuclease_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 {ECO:0000313|Proteomes:UP000010482};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751501};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751464};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751448};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751488};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751459};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751469};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010482};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00104, ECO:0000256|PROSITE-
KW   ProRule:PRU00266, ECO:0000256|SAAS:SAAS00880466};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751509};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00745773};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751473}.
FT   DOMAIN       40    165       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   DOMAIN      193    263       DRBM. {ECO:0000259|PROSITE:PS50137}.
FT   REGION        1     37       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     14     37       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE     83     83       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    154    154       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   METAL        79     79       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL       151    151       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL       154    154       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
SQ   SEQUENCE   264 AA;  29785 MW;  444FFD56712A5A75 CRC64;
     MRAESSSELA IETSRSRSKT RSEELRSRNR QGGSRRGREL RKMVERLGLT DTTTIDWNLL
     DLALTHPSAS SLANYQQLEF VGDAVVRLAA SELLLETYPE APVGDFAAIR SILVSDRVLA
     EFAESYGMDR FLLMAGSAAK NKAGARSRLA DTFEAVLGAL YLSTYSMNLI RPWLDPILKQ
     KADQIRQDPA RQNYKDALQE WTQAHYKVLP HYQVEETGRG YDDPERFTAY VWLKDRFLSQ
     GKGRSKKAAQ QAAAQSAYQN LTQK
//
DBGET integrated database retrieval system