ID H1LQS2_9PAST Unreviewed; 141 AA.
AC H1LQS2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ORFNames=HMPREF9096_01648 {ECO:0000313|EMBL:EHO45793.1};
OS Haemophilus sp. oral taxon 851 str. F0397.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=762965 {ECO:0000313|EMBL:EHO45793.1, ECO:0000313|Proteomes:UP000005305};
RN [1] {ECO:0000313|EMBL:EHO45793.1, ECO:0000313|Proteomes:UP000005305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0397 {ECO:0000313|EMBL:EHO45793.1,
RC ECO:0000313|Proteomes:UP000005305};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHO45793.1}.
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DR EMBL; AGRK01000033; EHO45793.1; -; Genomic_DNA.
DR RefSeq; WP_009500893.1; NZ_JH591082.1.
DR AlphaFoldDB; H1LQS2; -.
DR PATRIC; fig|762965.3.peg.1563; -.
DR HOGENOM; CLU_098240_3_0_6; -.
DR Proteomes; UP000005305; Unassembled WGS sequence.
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 Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00651}.
FT DOMAIN 3..103
FT /note="YqgF/RNase H-like"
FT /evidence="ECO:0000259|SMART:SM00732"
SQ SEQUENCE 141 AA; 15484 MW; DDC9A5996ACFE103 CRC64;
MGITALAFDF GTKSIGCAVG QSITGTAQAL PAFKAQDGIP NWDVIEKCLK EWKPDVVVVG
LPLNMDGTEQ DLTLRARKFA NRLQGRFGVN VQLQDERLTT TEARSEIFDR GGFRALKKGK
VDGISACLIL ESWFEVAEYS E
//