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Database: UniProt
Entry: A0A1U7IX24_9NOSO
LinkDB: A0A1U7IX24_9NOSO
Original site: A0A1U7IX24_9NOSO 
ID   A0A1U7IX24_9NOSO        Unreviewed;       239 AA.
AC   A0A1U7IX24;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   13-FEB-2019, entry version 12.
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=FACHB389_01665 {ECO:0000313|EMBL:OKH42387.1};
OS   Nostoc calcicola FACHB-389.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1357508 {ECO:0000313|EMBL:OKH42387.1, ECO:0000313|Proteomes:UP000186138};
RN   [1] {ECO:0000313|EMBL:OKH42387.1, ECO:0000313|Proteomes:UP000186138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FACHB-389 {ECO:0000313|EMBL:OKH42387.1,
RC   ECO:0000313|Proteomes:UP000186138};
RA   Zhu T., Hou S., Lu X., Hess W.R.;
RT   "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT   Habitats.";
RL   Submitted (NOV-2016) 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   -!- 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:OKH42387.1}.
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DR   EMBL; MRBZ01000003; OKH42387.1; -; Genomic_DNA.
DR   RefSeq; WP_073639131.1; NZ_MRBZ01000003.1.
DR   BioCyc; GCF_001904715:FACHB389_RS01665-MONOMER; -.
DR   Proteomes; UP000186138; 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:UP000186138};
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   239 AA;  26873 MW;  5EFA2C575F89B40F CRC64;
     MTLAYPRRQR QLESLVKKFG LPTEAPIKWQ LLDLALTHPT VSESANYEQL EFVGDAVVRL
     VSAVVLWEHY PDCPVGDFAA IRSVLVSDRI LAQLARVYGL ELYLLVAGSA TADKVGQESR
     LADAFEAVLG ALYLSTQNLE LIRPWLDPHF QQLATEIRLD PARLNYKAAL QEWTQAQFKV
     LPEYRVVEVN QPHRNQERFV AEVWLHGNML GLGKGRSIKT AEQAAAKVAF LAITNQEKP
//
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