RND_DESPS
ID RND_DESPS Reviewed; 374 AA.
AC Q6AJF4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=DP2797;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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}.
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DR EMBL; CR522870; CAG37526.1; -; Genomic_DNA.
DR RefSeq; WP_011190038.1; NC_006138.1.
DR AlphaFoldDB; Q6AJF4; -.
DR SMR; Q6AJF4; -.
DR STRING; 177439.DP2797; -.
DR PRIDE; Q6AJF4; -.
DR EnsemblBacteria; CAG37526; CAG37526; DP2797.
DR KEGG; dps:DP2797; -.
DR eggNOG; COG0349; Bacteria.
DR HOGENOM; CLU_042387_0_0_7; -.
DR OMA; FMRVDTF; -.
DR OrthoDB; 1462689at2; -.
DR Proteomes; UP000000602; 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; -; 1.
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 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; Reference proteome;
KW tRNA processing.
FT CHAIN 1..374
FT /note="Ribonuclease D"
FT /id="PRO_0000411061"
FT DOMAIN 6..171
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
FT DOMAIN 213..292
FT /note="HRDC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
SQ SEQUENCE 374 AA; 42417 MW; D42604D4329F0A08 CRC64;
MKQENIISTT EDLKKIVNKA LKLDAVGLDT EFVWERTYYP QLGLIQIALS DEECYAIDPL
SIKDLSPLGE LLADRNTIKI LHDAPQDLII MSQATGATPQ NIFDTRLAAG FAGSISTISL
LQLVSEQLET ELDKSETRTN WLKRPLTEKQ LSYSLNDVRY LRATRVILLS KIIGPKIKSW
LQEELNLLNN PANYSTIADE SRYKKVKGVN KLDRKSIGVA QEIATWREQK ARELNRPRGH
VIKDDILLEI AAIRPTRPEE LANTAISTKA AERYGNDICQ ATARALNKKE VDLPHQQKRS
QLSSQEKGAL AQLKELITLK CDILGIDPAL LGNSNELKKI IQTLYKGKTT HMRQSFGWRK
EFLKDFYQIH RDTI