RNC_ROSHA
ID RNC_ROSHA Reviewed; 357 AA.
AC G2SYN4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=RHOM_15125;
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Roseburia.
OX NCBI_TaxID=585394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183;
RX PubMed=26543119; DOI=10.1128/genomea.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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 (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; CP003040; AEN98131.1; -; Genomic_DNA.
DR RefSeq; WP_014081094.1; NC_015977.1.
DR AlphaFoldDB; G2SYN4; -.
DR SMR; G2SYN4; -.
DR STRING; 585394.RHOM_15125; -.
DR EnsemblBacteria; AEN98131; AEN98131; RHOM_15125.
DR KEGG; rho:RHOM_15125; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_775860_0_0_9; -.
DR OMA; EECEYEW; -.
DR Proteomes; UP000008178; 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; 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; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; Reference proteome; Repeat; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..357
FT /note="Ribonuclease 3"
FT /id="PRO_0000416613"
FT DOMAIN 6..155
FT /note="RNase III"
FT DOMAIN 198..267
FT /note="DRBM 1"
FT DOMAIN 285..355
FT /note="DRBM 2"
FT ACT_SITE 49
FT /evidence="ECO:0000255"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 41045 MW; 9D9FE4E68BD9B326 CRC64;
MDEKEIKFIQ DQIGYTFKNQ ELLVQAFTRR SYSMENGGQD NEVLEFIGDK ALDFVVVKQL
SEEFGHYSKK YQNWEKWGKT EETGTFISDL DEGELTEIKK QLVQKNTLAD AIDNLGIAYY
LIMGKGDVEK NIQDSLSVKE DLFEAILGAI ALDSNWDIEA LQDSMNVMLN PGELMFDEDV
NYVAEIQAWS SANSGNIPLH CFYPTSMQGT WYMPRHHMCI YGKAEQDTHF ACEVLIPGID
YHFVGYGRSK NLARMDASRL AYEYLKDEDM LFSIRDEIDD PNYNDSIGQL EILARRGYFS
IPQYDFKETH DEDGNPVWNC KCSIKEKDTV TNGRSSSKKD AKKQAAYDML TFVLEEE