ID A9BY84_DELAS Unreviewed; 152 AA.
AC A9BY84;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Putative pre-16S rRNA nuclease {ECO:0000256|HAMAP-Rule:MF_00651};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00651};
GN OrderedLocusNames=Daci_1579 {ECO:0000313|EMBL:ABX34223.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX34223.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX34223.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could be a nuclease involved in processing of the 5'-end of
CC pre-16S rRNA. {ECO:0000256|HAMAP-Rule:MF_00651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00651}.
CC -!- SIMILARITY: Belongs to the YqgF HJR family. {ECO:0000256|HAMAP-
CC Rule:MF_00651}.
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DR EMBL; CP000884; ABX34223.1; -; Genomic_DNA.
DR RefSeq; WP_012203508.1; NC_010002.1.
DR AlphaFoldDB; A9BY84; -.
DR STRING; 398578.Daci_1579; -.
DR GeneID; 24118037; -.
DR KEGG; dac:Daci_1579; -.
DR eggNOG; COG0816; Bacteria.
DR HOGENOM; CLU_098240_3_2_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000967; P:rRNA 5'-end processing; IEA:UniProtKB-UniRule.
DR CDD; cd16964; YqgF; 1.
DR Gene3D; 3.30.420.140; YqgF/RNase H-like domain; 1.
DR HAMAP; MF_00651; Nuclease_YqgF; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR005227; YqgF.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR NCBIfam; TIGR00250; RNAse_H_YqgF; 1.
DR PANTHER; PTHR33317; POLYNUCLEOTIDYL TRANSFERASE, RIBONUCLEASE H-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR33317:SF4; POLYNUCLEOTIDYL TRANSFERASE, RIBONUCLEASE H-LIKE SUPERFAMILY PROTEIN; 1.
DR Pfam; PF03652; RuvX; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00651};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00651};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00651}.
FT DOMAIN 27..127
FT /note="YqgF/RNase H-like"
FT /evidence="ECO:0000259|SMART:SM00732"
SQ SEQUENCE 152 AA; 16177 MW; D22605601D6206C3 CRC64;
MSLPAPESQA AAAAGTAVPP TVPSHFQSFV AFDFGAKRTG CAVGTRMLRS ANPLPTIRAE
AGEARLAQAG ERIKEWQPDA LVIGVPYHPD GNAHENTARA KKFGRQLKSR FGLPVYEVDE
RYSTTEALAG GARDADAASA CIILEQFLRS LP
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