RND_PSEA7
ID RND_PSEA7 Reviewed; 376 AA.
AC A6V8R6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Ribonuclease D {ECO:0000255|HAMAP-Rule:MF_01899};
DE Short=RNase D {ECO:0000255|HAMAP-Rule:MF_01899};
DE EC=3.1.13.5 {ECO:0000255|HAMAP-Rule:MF_01899};
GN Name=rnd {ECO:0000255|HAMAP-Rule:MF_01899}; OrderedLocusNames=PSPA7_4097;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_01899};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01899};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01899}.
CC -!- SIMILARITY: Belongs to the RNase D family. {ECO:0000255|HAMAP-
CC Rule:MF_01899}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABR83083.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000744; ABR83083.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6V8R6; -.
DR SMR; A6V8R6; -.
DR PRIDE; A6V8R6; -.
DR EnsemblBacteria; ABR83083; ABR83083; PSPA7_4097.
DR KEGG; pap:PSPA7_4097; -.
DR HOGENOM; CLU_042387_0_0_6; -.
DR Proteomes; UP000001582; 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 Gene3D; 1.10.150.80; -; 2.
DR Gene3D; 3.30.420.10; -; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; SSF47819; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR01388; rnd; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; tRNA processing.
FT CHAIN 1..376
FT /note="Ribonuclease D"
FT /id="PRO_0000411069"
FT DOMAIN 8..176
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
FT DOMAIN 214..294
FT /note="HRDC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
SQ SEQUENCE 376 AA; 43331 MW; 2B6D2A2868E8AB0D CRC64;
MFVTAPEIQW IRDDASLAQQ CREWRTQPYL ALDTEFMRVD TFYPAAGLVQ VGDGRREWLI
DPLLVRDWGP FAELLEDPRV VKVLHACSED LEVFLRLTGS LPVPLFDTQL AAAYLGMAHS
MGYSKLVKEV LDIDLPKDET RSDWLQRPLT EMQMRYAADD VQHLAQVYLA LDARLSEEKR
AWLLEDGAEL VANLCRESDP REAYREVKLG WRLRPQQLAV LRELCAWREE QARLRNRPRN
HVLRERTLWP LARLLPKNKT DLAAIEDMHP RTVRQDGDFL IELIAEAARL PQSEWPEALP
EPLPPEVTPL LKSLRAIGQR EAETLGMAPE LMLRKKILEA LLKSGYPHGP YELPDSLRGW
RRERMGQALL NALESA
