ID B6IN01_RHOCS Unreviewed; 236 AA.
AC B6IN01;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:ACI98898.1};
GN OrderedLocusNames=RC1_1494 {ECO:0000313|EMBL:ACI98898.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98898.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI98898.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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; CP000613; ACI98898.1; -; Genomic_DNA.
DR RefSeq; WP_012566684.1; NC_011420.2.
DR AlphaFoldDB; B6IN01; -.
DR STRING; 414684.RC1_1494; -.
DR KEGG; rce:RC1_1494; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_1_5; -.
DR OrthoDB; 9805026at2; -.
DR Proteomes; UP000001591; 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:UP000001591};
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 11..139
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 164..233
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT ACT_SITE 56
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 128
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 236 AA; 25436 MW; 82046725C309DB27 CRC64;
MTTHDCGGPP LSELETGLGY HFRHRDLLVQ ALTHPSLGGV ERNAGRGYER LEFLGDRVLG
LVIAEWLLER FPAEAEGALA RRHTALVRAE ALTVVAETIG LGPFLRLAPS ERDSGGQAKP
AILADACEAV IGAIFQDGGL EPARTLIRTR WTPLIEADLS PPQDPKTALQ EWALGRGRPL
PAYETLSREG PDHAPVFRVR VRVEGAEPAT ATGPSKRAAE KAAAEALLRQ IRTVKG
//
