RND_ZYMMO
ID RND_ZYMMO Reviewed; 390 AA.
AC Q5NPM2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=ZMO0714;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV89338.1; -; Genomic_DNA.
DR RefSeq; WP_011240601.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NPM2; -.
DR SMR; Q5NPM2; -.
DR STRING; 264203.ZMO0714; -.
DR EnsemblBacteria; AAV89338; AAV89338; ZMO0714.
DR GeneID; 58026535; -.
DR KEGG; zmo:ZMO0714; -.
DR eggNOG; COG0349; Bacteria.
DR HOGENOM; CLU_042387_0_0_5; -.
DR OMA; FMRVDTF; -.
DR OrthoDB; 1462689at2; -.
DR Proteomes; UP000001173; 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..390
FT /note="Ribonuclease D"
FT /id="PRO_0000411075"
FT DOMAIN 7..173
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
FT DOMAIN 212..293
FT /note="HRDC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01899"
SQ SEQUENCE 390 AA; 43855 MW; D39C9EF2C9A4698E CRC64;
MQIHPLITDS ATLAALCSRL SRADFIAIDT EFIRENSYWP ELCLIQIADD KEAAAIDPLA
PGLDMTPLTD LLVNNEDILK VFHAGGQDLE IILHHTGKMP FPLFDTQIAA MALGVGEQVG
YSNLVERYLS IKLDKGARFT DWSHRPLDRR QLDYAIADVT HLATLFPMLL KELRDKGRGA
WLDQEMERLA DPSQYINDPE KSWLRIRMPN RKADILGRLK ALAAWREIEA QNRNIPRGRI
AKDETLADLA IHPPRRQSDL VKVRGLSGSW GSNDIGQRLM EAIENAEALR PEEIPQRNDR
KLCIGKDGAM IADLLKLLLK MRARDAEVAA RLIAKSDDIE GIIAGERENN PVLTGWRYDI
FGKEAIALIE GKMAFSVQKG KIAMTLIEKE