GenomeNet

Database: UniProt
Entry: Q8ZP09_SALTY
LinkDB: Q8ZP09_SALTY
Original site: Q8ZP09_SALTY 
ID   Q8ZP09_SALTY            Unreviewed;       375 AA.
AC   Q8ZP09;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Ribonuclease D {ECO:0000256|HAMAP-Rule:MF_01899};
DE            Short=RNase D {ECO:0000256|HAMAP-Rule:MF_01899};
DE            EC=3.1.13.5 {ECO:0000256|HAMAP-Rule:MF_01899};
GN   Name=rnd {ECO:0000256|HAMAP-Rule:MF_01899,
GN   ECO:0000313|EMBL:AAL20732.1};
GN   OrderedLocusNames=STM1817 {ECO:0000313|EMBL:AAL20732.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL20732.1, ECO:0000313|Proteomes:UP000001014};
RN   [1] {ECO:0000313|EMBL:AAL20732.1, ECO:0000313|Proteomes:UP000001014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720
RC   {ECO:0000313|Proteomes:UP000001014};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Exonuclease involved in the 3' processing of various
CC       precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA
CC       molecule and releases 5'-mononucleotides. {ECO:0000256|HAMAP-
CC       Rule:MF_01899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage that removes extra residues from the
CC         3'-terminus of tRNA to produce 5'-mononucleotides.; EC=3.1.13.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01899};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01899};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01899}.
CC   -!- SIMILARITY: Belongs to the RNase D family. {ECO:0000256|HAMAP-
CC       Rule:MF_01899}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006468; AAL20732.1; -; Genomic_DNA.
DR   RefSeq; NP_460773.1; NC_003197.2.
DR   RefSeq; WP_001109130.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZP09; -.
DR   STRING; 99287.STM1817; -.
DR   PaxDb; 99287-STM1817; -.
DR   GeneID; 1253336; -.
DR   KEGG; stm:STM1817; -.
DR   PATRIC; fig|99287.12.peg.1917; -.
DR   HOGENOM; CLU_042387_0_1_6; -.
DR   OMA; TSGMHKV; -.
DR   PhylomeDB; Q8ZP09; -.
DR   BioCyc; SENT99287:STM1817-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0033890; F:ribonuclease D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042780; P:tRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR   CDD; cd06142; RNaseD_exo; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   HAMAP; MF_01899; RNase_D; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR006292; RNase_D.
DR   InterPro; IPR048579; RNAseD_HRDC_C.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR01388; rnd; 1.
DR   PANTHER; PTHR47649; RIBONUCLEASE D; 1.
DR   PANTHER; PTHR47649:SF1; RIBONUCLEASE D; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF21293; RNAseD_HRDC_C; 1.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01899};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01899};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899, ECO:0000313|EMBL:AAL20732.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01899};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          210..289
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   375 AA;  42375 MW;  152B85AEC4D099DF CRC64;
     MNYQMIETDD ALASLCEAVR ACPAIALDTE FVRTRTYYPQ LGLIQLFDGA NVALIDPLGI
     SDWSPLKAVL RDTGITKFLH AGSEDLEVFL NAFGELPEPL IDTQILAAFC GRPLSWGFAS
     MVEEYTGVAL DKSESRTDWL ARPLSERQCE YAAADVWYLL PIAKKLMIET EAAGWLPAAL
     DECRLMQQRR QEIQAPEEAW RDITNAWQLR TRQLACLQLL ADWRLRKARE RDMAVNFVVR
     EENLWAVARY MPGSLGELDS LGLSGSEIRF HGKTLISLVA KAQALPEEAL PEPLLNLMDM
     PGYRKAFKAI KALVAEVSAS HHVSGELLAS RRQINQLLNW HWKLKPQNGQ PELISGWRAE
     LMEEKLTLLL QEYPL
//
DBGET integrated database retrieval system