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Database: UniProt
Entry: A0A0F7JTL7_9GAMM
LinkDB: A0A0F7JTL7_9GAMM
Original site: A0A0F7JTL7_9GAMM 
ID   A0A0F7JTL7_9GAMM        Unreviewed;       186 AA.
AC   A0A0F7JTL7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Oligoribonuclease {ECO:0000256|HAMAP-Rule:MF_00045};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00045};
GN   Name=orn {ECO:0000256|HAMAP-Rule:MF_00045};
GN   ORFNames=AAY24_05255 {ECO:0000313|EMBL:AKH19856.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19856.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH19856.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19856.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
CC   -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC       oligoribonucleotides. {ECO:0000256|HAMAP-Rule:MF_00045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00045}.
CC   -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC       {ECO:0000256|ARBA:ARBA00009921, ECO:0000256|HAMAP-Rule:MF_00045}.
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DR   EMBL; CP011412; AKH19856.1; -; Genomic_DNA.
DR   RefSeq; WP_046858792.1; NZ_CP011412.1.
DR   AlphaFoldDB; A0A0F7JTL7; -.
DR   KEGG; seds:AAY24_05255; -.
DR   PATRIC; fig|1543721.4.peg.1088; -.
DR   OrthoDB; 9801329at2; -.
DR   Proteomes; UP000034410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006259; P:DNA metabolic process; IEA:UniProt.
DR   CDD; cd06135; Orn; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   HAMAP; MF_00045; Oligoribonuclease; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR022894; Oligoribonuclease.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11046; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11046:SF0; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00045};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00045}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00045};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT   DOMAIN          7..180
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00045"
SQ   SEQUENCE   186 AA;  21016 MW;  071B9BADBA4A6D07 CRC64;
     MAQESTNLIW IDLEMTGLDP ENDRIIEIAT IVTDGDLNVL AEGPMIAIHQ APEVMAAMDE
     WNTNQHGKSG LTERVLASEV SEAQAEQETL AFLRQYVPQG VSPICGNSIC QDRRFLARYM
     PELEAYFHYR NLDVSTLKEL AKRWAPAIAK GVVKSGRHLA MDDIVDSINE LRHYRDHFLR
     LPEEPA
//
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