ID E6SJD7_THEM7 Unreviewed; 329 AA.
AC E6SJD7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 79.
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 OrderedLocusNames=Tmar_0952 {ECO:0000313|EMBL:ADU51065.1};
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS 7p75a).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51065.1, ECO:0000313|Proteomes:UP000008915};
RN [1] {ECO:0000313|EMBL:ADU51065.1, ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX PubMed=21304738;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75a).";
RL Stand. Genomic Sci. 3:337-345(2010).
RN [2] {ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(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; CP002344; ADU51065.1; -; Genomic_DNA.
DR RefSeq; WP_013495370.1; NC_014831.1.
DR AlphaFoldDB; E6SJD7; -.
DR STRING; 644966.Tmar_0952; -.
DR KEGG; tmr:Tmar_0952; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_1_9; -.
DR Proteomes; UP000008915; 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; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR PANTHER; PTHR11207; RIBONUCLEASE III; 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:UP000008915};
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 74..203
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 231..300
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 192
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 329 AA; 33637 MW; E606AB344D6E4F4F CRC64;
MGLDGQQRDA AAGAGTGAAT AASTAAGPGG PGDGTAGTVP PDTAAAGTAP QRAGPGGGGA
GPSRPPRAGE PGWLQRVAEL TGTEPRRPEL FLEALTHASY RAEHPDTAGA DNERLEFLGD
AVLNLCVTDH IFRTYPQRPE GELSKLRAAT VRAETLAVTA QRLGLGELLR LGRGEEATGG
RQRPSVLADA FEAVVAAVYL QEGLEGARAF ILRTLGDEIR RLAESSGACD DPKTALQELS
RRLGLGEPSY RVIDASGPEH DPRYTVEVRV GGRPLGQAVG RSKKVAEREA ARIALADLEE
PAAGAARPAG DAGAAGSGAS RAGEEPAGR
//
