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Database: UniProt
Entry: A0A1Z4V815_9CYAN
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Original site: A0A1Z4V815_9CYAN 
ID   A0A1Z4V815_9CYAN        Unreviewed;       240 AA.
AC   A0A1Z4V815;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
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=NIES806_39230 {ECO:0000313|EMBL:BAZ87692.1};
OS   Dolichospermum compactum NIES-806.
OC   Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae;
OC   Dolichospermum; Dolichospermum compactum.
OX   NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ87692.1, ECO:0000313|Proteomes:UP000218702};
RN   [1] {ECO:0000313|EMBL:BAZ87692.1, ECO:0000313|Proteomes:UP000218702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ87692.1,
RC   ECO:0000313|Proteomes:UP000218702};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; AP018316; BAZ87692.1; -; Genomic_DNA.
DR   Proteomes; UP000218702; 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:UP000218702};
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   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;  27087 MW;  358426FCBF1221B9 CRC64;
     MSSVYPRRQR QLESLVQKFG LSINAPIKWQ LLDLALTHPT VSDTANYEQL EFVGDAVVRL
     VAAEILWEHY ADCSVGDFAA IRSVLVSDRI LAQLAREYGL ELYLLVAGSA TADHVGQESR
     LADSFEAVLG ALYLSTNNLN LIRPWLDPHF QQLTTEIRLD PARLNYKAAL QEWTQAQFKV
     LPEYRVLEVS QPHRTHERFF AEVWLHEKML GQGKGRSIKA AEQAAAKVAY LAISTPLKDE
//
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