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Database: UniProt
Entry: D4TRN2_9CYAN
LinkDB: D4TRN2_9CYAN
Original site: D4TRN2_9CYAN 
ID   D4TRN2_9CYAN            Unreviewed;       240 AA.
AC   D4TRN2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
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=CRD_02283 {ECO:0000313|EMBL:EFA72905.1};
OS   Raphidiopsis brookii D9.
OC   Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Raphidiopsis.
OX   NCBI_TaxID=533247 {ECO:0000313|EMBL:EFA72905.1, ECO:0000313|Proteomes:UP000052137};
RN   [1] {ECO:0000313|EMBL:EFA72905.1, ECO:0000313|Proteomes:UP000052137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D9 {ECO:0000313|EMBL:EFA72905.1,
RC   ECO:0000313|Proteomes:UP000052137};
RX   PubMed=20169071; DOI=10.1371/journal.pone.0009235;
RA   Stucken K., John U., Cembella A., Murillo A.A., Soto-Liebe K.,
RA   Fuentes-Valdes J.J., Friedel M., Plominsky A.M., Vasquez M.,
RA   Glockner G.;
RT   "The smallest known genomes of multicellular and toxic cyanobacteria:
RT   comparison, minimal gene sets for linked traits and the evolutionary
RT   implications.";
RL   PLoS ONE 5:E9235-E9235(2010).
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFA72905.1}.
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DR   EMBL; ACYB01000035; EFA72905.1; -; Genomic_DNA.
DR   RefSeq; WP_009343439.1; NZ_ACYB01000035.1.
DR   STRING; 533247.CRD_02283; -.
DR   EnsemblBacteria; EFA72905; EFA72905; CRD_02283.
DR   eggNOG; ENOG4107Z8V; Bacteria.
DR   eggNOG; COG0571; LUCA.
DR   OrthoDB; 1890943at2; -.
DR   Proteomes; UP000052137; Unassembled WGS sequence.
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:UP000052137};
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:UP000052137};
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       12    137       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   DOMAIN      165    235       DRBM. {ECO:0000259|PROSITE:PS50137}.
FT   ACT_SITE     55     55       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   ACT_SITE    126    126       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   METAL        51     51       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL       123    123       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL       126    126       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
SQ   SEQUENCE   240 AA;  26960 MW;  DA95BC5E6BB33FD5 CRC64;
     MSRVYPRRQR QLESLIQKLG LSANSPIKWP LLDLALTHPT VSESANYEQL EFVGDAVVRL
     VAAVVLWESY PDCCVGDFAA IRSVLVSDRI LARLAREYDL ELYLLVAGSA TADNVGQESR
     LADAFEALLG ALYLSTQNLI LIRPWLDPHF QELAEQIRLD PARLNYKAAL QEWTQAGYKV
     LPEYRVVEVN QSQNAHERFL AQVWLHEKIL GQGKGRSIKA AEQEAAKVAY LAITQTQSIT
//
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