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Database: UniProt
Entry: A0A078LJR1_9PSED
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ID   A0A078LJR1_9PSED        Unreviewed;       374 AA.
AC   A0A078LJR1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ECO:0000313|EMBL:CDZ92953.1};
GN   ORFNames=BN1079_00228 {ECO:0000313|EMBL:CDZ92953.1}, EGJ00_01115
GN   {ECO:0000313|EMBL:RRV17963.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ92953.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ92953.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ92953.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RRV17963.1, ECO:0000313|Proteomes:UP000271179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS_399 {ECO:0000313|EMBL:RRV17963.1,
RC   ECO:0000313|Proteomes:UP000271179};
RA   D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA   Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT   "Transmission dynamics of multidrug resistant bacteria on intensive care
RT   unit surfaces.";
RL   Submitted (OCT-2018) 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: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}.
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DR   EMBL; CCSF01000001; CDZ92953.1; -; Genomic_DNA.
DR   EMBL; RHQU01000001; RRV17963.1; -; Genomic_DNA.
DR   RefSeq; WP_037021704.1; NZ_RHQU01000001.1.
DR   AlphaFoldDB; A0A078LJR1; -.
DR   STRING; 1499686.BN1079_00228; -.
DR   eggNOG; COG0349; Bacteria.
DR   HOGENOM; CLU_042387_0_0_6; -.
DR   OrthoDB; 9800549at2; -.
DR   Proteomes; UP000053902; Unassembled WGS sequence.
DR   Proteomes; UP000271179; Unassembled WGS sequence.
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; 2.
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   SMART; SM00341; HRDC; 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};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899, ECO:0000313|EMBL:RRV17963.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01899};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          211..291
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   374 AA;  42506 MW;  9E7704F62A13C1E4 CRC64;
     MAITTQWVLD DEHLARLCTE WRQLPFVALD TEFMRVDTFY PIAALLQVGD GRCAYLIDPL
     QISDWSAFAG LLEDQAVVKV LHACSEDLEV FLRLTGSLPV PLFDTQLAAG YLNIGFSMGY
     SRLVQSVLNI ELPKGETRSD WLQRPLSEMQ VQYAAEDAQH LAELYQALLP KLSEEKFAWI
     LEDGAELVAN QRRETDPAEA YRDVKQAWRL KPRQLAVLRA LACWRETQAR KRNQPRNRVL
     REASLWPLAR TQPGDLVSLA RIEDMHPRTV RQDGETLLEL IRAAAATPEQ EWPAVLPEPL
     PLEASKLLKK LRAVGQRAAI DLDIAPELVL RKKVLEALLK TGYPDGPYQL PDSFRGWRRE
     RLGQSLLDAL EKKS
//
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