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Database: UniProt
Entry: A0A090IJ69_9GAMM
LinkDB: A0A090IJ69_9GAMM
Original site: A0A090IJ69_9GAMM 
ID   A0A090IJ69_9GAMM        Unreviewed;       362 AA.
AC   A0A090IJ69;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:CED60219.1};
GN   ORFNames=MVIS_2271 {ECO:0000313|EMBL:CED60219.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED60219.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) 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; LN554852; CED60219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090IJ69; -.
DR   STRING; 80854.MVIS_2271; -.
DR   KEGG; mvs:MVIS_2271; -.
DR   PATRIC; fig|80854.5.peg.2422; -.
DR   HOGENOM; CLU_042387_0_1_6; -.
DR   Proteomes; UP000032438; Chromosome complete 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; IPR048579; RNAseD_HRDC_C.
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   Pfam; PF21293; RNAseD_HRDC_C; 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|HAMAP-Rule:MF_01899};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899, ECO:0000313|EMBL:CED60219.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01899};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032438};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          194..273
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   362 AA;  41122 MW;  9160237546769321 CRC64;
     MIAQCAEVEI LAIDTEFIRQ RTYYPILGLF QLYNGTETYL VDPLAIDDLS ALWQLLDRQP
     VVLHACSEDL DVFMTVANKF PDFFHDTQIA AAFCGLGSSL GFGGLVSEFQ NITLDKGESR
     SNWLARPLTT KQLSYAAADV YHLLPCWHEL KSKLDELGYY DFYLQELDNL RRRKMVNKNP
     KTVYKQFKNA SFLSPRELAT LQALAEWRED NAVNRDMAVN FVVKEAHLLE VAKQQPKSLR
     DLNQLGLLPI EIKRHGKQII DLVKQAQSLS DEALPEPLTR ISDYPGYKKI VLGIRNKIAV
     VAEKTNIPAE LIGSKKIINE LLNWVWKLTE AERAVGSKPI LLSNWRAELI GNSLFEGLMA
     NK
//
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