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Database: UniProt
Entry: A0A1X2LX86_9MYCO
LinkDB: A0A1X2LX86_9MYCO
Original site: A0A1X2LX86_9MYCO 
ID   A0A1X2LX86_9MYCO        Unreviewed;       167 AA.
AC   A0A1X2LX86;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=3'-5' exoribonuclease {ECO:0000256|HAMAP-Rule:MF_00977};
DE            EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_00977};
GN   ORFNames=B8W66_06615 {ECO:0000313|EMBL:OSC41791.1};
OS   Mycobacterium decipiens.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC41791.1, ECO:0000313|Proteomes:UP000193247};
RN   [1] {ECO:0000313|EMBL:OSC41791.1, ECO:0000313|Proteomes:UP000193247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC41791.1,
RC   ECO:0000313|Proteomes:UP000193247};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exonuclease that cleaves single-stranded 3' overhangs of
CC       double-stranded RNA. {ECO:0000256|HAMAP-Rule:MF_00977}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00977};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00977};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00977}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSC41791.1}.
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DR   EMBL; NCXP01000005; OSC41791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2LX86; -.
DR   STRING; 1430326.B8W66_06615; -.
DR   OrthoDB; 4640719at2; -.
DR   Proteomes; UP000193247; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004532; F:RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   HAMAP; MF_00977; 3_5_Exoribonuc_actinobact; 1.
DR   InterPro; IPR030853; 3_5_Exoribonuc_actinobac.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR033390; Rv2179c-like.
DR   NCBIfam; NF033638; RNase_AS; 1.
DR   Pfam; PF16473; Rv2179c-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00977};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00977};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00977};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00977};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00977}.
FT   DOMAIN          2..154
FT                   /note="3'-5' exoribonuclease Rv2179c-like"
FT                   /evidence="ECO:0000259|Pfam:PF16473"
FT   REGION          6..9
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00977"
FT   BINDING         6
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00977"
SQ   SEQUENCE   167 AA;  19267 MW;  3D31E202996E0412 CRC64;
     MRYFYDTEFI EDGRTIELIS IGVVAEDGRE YYAVSTEFDP ERAGSWVRAH VLPKLPPPAS
     QLWRSRQQIR LGLEEFLRVD GKDPIELWAW VGAYDHVALC QLWGPMTALP PAVPRFTREL
     RQLWEDRGSP RMPPRPRDAH DALVDARDQL RRFRLITSVD DADGGAH
//
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