ID RND_JANSC Reviewed; 386 AA.
AC Q28RA7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 01-MAY-2013, entry version 41.
DE RecName: Full=Ribonuclease D;
DE Short=RNase D;
DE EC=3.1.13.5;
GN Name=rnd; OrderedLocusNames=Jann_1838;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage that removes extra
CC residues from the 3'-terminus of tRNA to produce 5'-
CC mononucleotides.
CC -!- COFACTOR: Divalent cation (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the RNase D family.
CC -!- SIMILARITY: Contains 1 3'-5' exonuclease domain.
CC -!- SIMILARITY: Contains 1 HRDC domain.
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DR EMBL; CP000264; ABD54755.1; -; Genomic_DNA.
DR RefSeq; YP_509780.1; NC_007802.1.
DR ProteinModelPortal; Q28RA7; -.
DR STRING; 290400.Jann_1838; -.
DR EnsemblBacteria; ABD54755; ABD54755; Jann_1838.
DR GeneID; 3934289; -.
DR KEGG; jan:Jann_1838; -.
DR PATRIC; 22147408; VBIJanSp43325_1971.
DR eggNOG; COG0349; -.
DR HOGENOM; HOG000277561; -.
DR KO; K03684; -.
DR OMA; SRTGTEI; -.
DR ProtClustDB; CLSK864964; -.
DR BioCyc; JSP290400:GI1R-1891-MONOMER; -.
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:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0042780; P:tRNA 3'-end processing; IEA:HAMAP.
DR HAMAP; MF_01899; RNase_D; 1; -.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR010997; HRDC-like.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR006292; RNase_D.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF47819; HRDC_like; 2.
DR SUPFAM; SSF53098; RNaseH_fold; 1.
DR TIGRFAMs; TIGR01388; rnd; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW tRNA processing.
FT CHAIN 1 386 Ribonuclease D.
FT /FTId=PRO_0000411065.
FT DOMAIN 3 174 3'-5' exonuclease.
FT DOMAIN 213 294 HRDC.
SQ SEQUENCE 386 AA; 42398 MW; 89E9EF4C81B863BD CRC64;
MPHTITTTDE LAAYCARAAT QPYVTVDTEF LRERTYFAQL CLVQVAMPGT DDTDAVLIDP
LAEGLSLEPL YELFRNVNVV KVFHAARQDL EIFFVEGGLV PTPLFDTQVA AMVCGFGDQV
GYETLVRRIA KANLDKSSRF TDWSRRPLSD AQKVYALADV TYLREIYEYL SAELARTDRT
HWLEEELAQL TNADAYVVDP ENAWKRLKLR SNSGRVVAIA QQLAAFRETY AQEKNVPRNR
VLKDDALLEL AGTKPKTVAD LGKSRLLLRD ARKGAIAEGL VAAVARGMSV PNSEIPKVQA
GRDRSNLNPA LADLLRVLLK AKAENAGVAT KLIASSSDLD DIASGFTDGV WASGWRSEVF
GADALRLLNG EVALAAKGQK VKIVEV
//