ID G8PDH1_PEDCP Unreviewed; 232 AA.
AC G8PDH1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:AEV95306.1};
GN OrderedLocusNames=PECL_1038 {ECO:0000313|EMBL:AEV95306.1};
OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS 3811 / P06).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95306.1, ECO:0000313|Proteomes:UP000005444};
RN [1] {ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV95306.1, ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RX PubMed=22328764; DOI=10.1128/JB.06759-11;
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL J. Bacteriol. 194:1271-1272(2012).
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; CP003137; AEV95306.1; -; Genomic_DNA.
DR RefSeq; WP_014215503.1; NC_016605.1.
DR AlphaFoldDB; G8PDH1; -.
DR STRING; 701521.PECL_1038; -.
DR KEGG; pce:PECL_1038; -.
DR PATRIC; fig|701521.8.peg.985; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_3_9; -.
DR Proteomes; UP000005444; 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; 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:UP000005444};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00104};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00104}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00104}.
FT DOMAIN 2..135
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 161..230
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 206..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 232 AA; 26550 MW; CD0BB87CA5C0FC1B CRC64;
MIKALEDDLA QNFNIHFNNH DLLDEAFTQA SYVNEHPNQG LKFYERIEFL GDAVLQIVVS
EYLFKRYPEM PQGKLTRLRA AMVKEDSFSD FAKECHFDRY IRLGKGEELS GARQRSSLLC
DIFESFTGAL YLDQGRDAVE EFVQKVIFPK LDEGRFDHVI DHKSELQEVL QVHGDVDIDY
QLIAETGGEN DRVFEVELIA DGKKLSRGKG TSKKLAEQNA ANKALQQIKS KK
//
