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Database: UniProt
Entry: F5YXL7_MYCSD
LinkDB: F5YXL7_MYCSD
Original site: F5YXL7_MYCSD 
ID   F5YXL7_MYCSD            Unreviewed;       233 AA.
AC   F5YXL7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   ECO:0000313|EMBL:AEF36657.1};
GN   OrderedLocusNames=JDM601_2657 {ECO:0000313|EMBL:AEF36657.1};
OS   Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF36657.1, ECO:0000313|Proteomes:UP000009224};
RN   [1] {ECO:0000313|EMBL:AEF36657.1, ECO:0000313|Proteomes:UP000009224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM601 {ECO:0000313|EMBL:AEF36657.1,
RC   ECO:0000313|Proteomes:UP000009224};
RX   PubMed=21685274; DOI=10.1128/JB.05291-11;
RA   Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA   Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT   "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT   Mycobacterium strain JDM601.";
RL   J. Bacteriol. 193:4300-4301(2011).
CC   -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC       primary rRNA transcript to yield the immediate precursors to the large
CC       and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when
CC       they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA
CC       of type II CRISPR loci if present in the organism. {ECO:0000256|HAMAP-
CC       Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000109, ECO:0000256|HAMAP-
CC         Rule:MF_00104};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00104};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family.
CC       {ECO:0000256|ARBA:ARBA00010183}.
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DR   EMBL; CP002329; AEF36657.1; -; Genomic_DNA.
DR   RefSeq; WP_013829586.1; NC_015576.1.
DR   AlphaFoldDB; F5YXL7; -.
DR   STRING; 875328.JDM601_2657; -.
DR   KEGG; mjd:JDM601_2657; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_2_11; -.
DR   OrthoDB; 9805026at2; -.
DR   Proteomes; UP000009224; 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:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd10845; DSRM_RNAse_III_family; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 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   NCBIfam; TIGR02191; RNaseIII; 1.
DR   PANTHER; PTHR14950; DICER-RELATED; 1.
DR   PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 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; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00104};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00104};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009224};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00104}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00104};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   DOMAIN          19..134
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          161..229
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   233 AA;  24560 MW;  23ECDD8E7FE6D7E8 CRC64;
     MSRPRQAVLE ALGVDLPDDL LTLAVTHRSY AYENGGLPTN ERLEFLGDAV LGLTITDELF
     HRHPDRPEGD LAKLRSSVVN TAALADVARG LTEDGLGAHL LLGRGEINTG GADKSSILAD
     SMESLLGAVY LQHGIDTARE VILRLFGPLL DTAATLGAGL DWKTSLQELT AARGIGVPCY
     QVSSTGPDHD REFTAIVVVS DTEYGSGVGR SKKEAEQKAA AAAWTALDAL DAG
//
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