UniProt: A0A346NSL2

Database: UniProt
Entry: A0A346NSL2_9ALTE

LinkDB:  A0A346NSL2_9ALTE 
Original site:  A0A346NSL2_9ALTE

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
All databases (23)   

Download RDF

ID   A0A346NSL2_9ALTE        Unreviewed;       383 AA.
AC   A0A346NSL2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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:AXR08519.1};
GN   ORFNames=D0Y50_12435 {ECO:0000313|EMBL:AXR08519.1};
OS   Salinimonas sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX   NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR08519.1, ECO:0000313|Proteomes:UP000262073};
RN   [1] {ECO:0000313|EMBL:AXR08519.1, ECO:0000313|Proteomes:UP000262073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N102 {ECO:0000313|EMBL:AXR08519.1,
RC   ECO:0000313|Proteomes:UP000262073};
RA   Cao J.;
RT   "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT   deep-sea sediment sample from the New Britain Trench.";
RL   Submitted (AUG-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}.
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; CP031769; AXR08519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346NSL2; -.
DR   KEGG; salm:D0Y50_12435; -.
DR   OrthoDB; 9800549at2; -.
DR   Proteomes; UP000262073; 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; 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|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01899};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899, ECO:0000313|EMBL:AXR08519.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01899};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          210..290
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   383 AA;  42850 MW;  62132422D5CD1586 CRC64;
     MDYELVTTYR DLKAVCDAAS QCEAIALDTE FVRTRTLTPQ LGLLQLYDGK QLVLIDPLAI
     DDMTPFVRLL ENPAVIKVLH SCSEDLEAFL AAFDTLPEPV FDTQFAAAVL GLGPSLGYAR
     LVEELSGVAL DKGESRTDWL ARPLSANQLV YAANDVLYLL PVYHQLNERM AECGKTQWVF
     DEIAALGLKK KSQLPLAFAY LPVKNNWKLN SQQLTVLQHL AAWRLGTARQ KDIALNFVVK
     ESVMLDIALR LPQSRNALSA IDGMIGPTMR RHGDTLLAVV QKALEEYDDI PATEQLARVR
     RLVEFPEYKK MLGKLKTLAD DIAAQQQVPV EVVASKKQMN QVLKWYWLTL DETRVQGLKP
     DLLSSWRAPL FSSHLDTLLG TTS
//

DBGET integrated database retrieval system