GenomeNet

Database: UniProt
Entry: E0TC26_PARBH
LinkDB: E0TC26_PARBH
Original site: E0TC26_PARBH 
ID   E0TC26_PARBH            Unreviewed;       383 AA.
AC   E0TC26;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   OrderedLocusNames=PB2503_08819 {ECO:0000313|EMBL:ADM09819.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM09819.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM09819.1, ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RX   PubMed=21037002; DOI=10.1128/JB.01205-10;
RA   Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT   the type species of the order "Parvularculales" in the class
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM09819.1; -; Genomic_DNA.
DR   RefSeq; WP_013300793.1; NC_014414.1.
DR   AlphaFoldDB; E0TC26; -.
DR   STRING; 314260.PB2503_08819; -.
DR   KEGG; pbr:PB2503_08819; -.
DR   eggNOG; COG0349; Bacteria.
DR   HOGENOM; CLU_042387_0_0_5; -.
DR   OrthoDB; 9800549at2; -.
DR   Proteomes; UP000001302; 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; 1.
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; 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   SMART; SM00474; 35EXOc; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01899};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001302};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          208..289
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   383 AA;  42811 MW;  1290D99448EFBB47 CRC64;
     MHIVTQTQDL TALCGRLAKH DFVTVDTEFM RERTYYPKLC LIQVASTEEA AIIDPLAAAL
     DLAPFLELLA DPSVLKVFHA ARQDLEIFYK LMGKVPAPLF DTQIAAMACG HGDQVGYEAL
     IREVTGAQVD KGSRFTDWAK RPLSDKQLTY ALGDVTHLVD AYQALITELE EKGRLEWIHA
     EMTQLNDPTL YYTDPDEAWR RIKVRNLKQR DRALLKAVAA WREREAIARD TPRNRVMKDD
     GLMEIVRTKP KDAQELAALR AIPSGFERSR AATALFDALA AADRMDEGAI PPAQKRDDRS
     APADVLELLR VLLKRQSEMH RVAPKLLASA ADLEAIALND EADVPALSGW RREVFGEMAL
     KLKHGRIALA LDRGSVRLID VQG
//
DBGET integrated database retrieval system