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Database: UniProt
Entry: A0A1L7D2B1_9CORY
LinkDB: A0A1L7D2B1_9CORY
Original site: A0A1L7D2B1_9CORY 
ID   A0A1L7D2B1_9CORY        Unreviewed;       169 AA.
AC   A0A1L7D2B1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=CPHO_04150 {ECO:0000313|EMBL:APT92213.1};
OS   Corynebacterium phocae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161895 {ECO:0000313|EMBL:APT92213.1, ECO:0000313|Proteomes:UP000185491};
RN   [1] {ECO:0000313|EMBL:APT92213.1, ECO:0000313|Proteomes:UP000185491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M408/89/1 {ECO:0000313|EMBL:APT92213.1,
RC   ECO:0000313|Proteomes:UP000185491};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT   44612(T)), isolated from the common seal (Phoca vitulina).";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009249; APT92213.1; -; Genomic_DNA.
DR   RefSeq; WP_075733464.1; NZ_VXKJ01000034.1.
DR   AlphaFoldDB; A0A1L7D2B1; -.
DR   STRING; 161895.CPHO_04150; -.
DR   KEGG; cpho:CPHO_04150; -.
DR   OrthoDB; 4640719at2; -.
DR   Proteomes; UP000185491; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185491}.
FT   DOMAIN          2..155
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   169 AA;  19185 MW;  1BAC6145637C8153 CRC64;
     MRYFYDTEFI EDGQTIELVS IGIVAEDGRE YYAVSTDFDA AKANAWVREN VLNQLPSPSS
     KAWKPLDTIR AEVLEFLCRP TSQVQLWAWV GAYDHVVLAQ LWGDMTGLPR TLPRYTRELR
     QYWEFAGRPA LPPVPDGNHD ALVDARHNLA KFRACQAVLP LSASNKAIF
//
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