ID A0A0J6XYC1_9ACTN Unreviewed; 200 AA.
AC A0A0J6XYC1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=ACS04_03320 {ECO:0000313|EMBL:KMO99242.1};
OS Streptomyces roseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO99242.1, ECO:0000313|Proteomes:UP000035932};
RN [1] {ECO:0000313|EMBL:KMO99242.1, ECO:0000313|Proteomes:UP000035932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO99242.1,
RC ECO:0000313|Proteomes:UP000035932};
RA Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA Barona-Gomez F.;
RT "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT hidden chemical diversity on bacterial genomes.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KMO99242.1}.
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DR EMBL; LFML01000013; KMO99242.1; -; Genomic_DNA.
DR RefSeq; WP_048474947.1; NZ_LFML01000013.1.
DR AlphaFoldDB; A0A0J6XYC1; -.
DR STRING; 66430.ACS04_03320; -.
DR PATRIC; fig|66430.4.peg.1994; -.
DR OrthoDB; 9801329at2; -.
DR Proteomes; UP000035932; Unassembled WGS sequence.
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:0090304; P:nucleic acid 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|HAMAP-Rule:MF_00045};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00045};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00045};
KW Reference proteome {ECO:0000313|Proteomes:UP000035932}.
FT DOMAIN 4..178
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 126
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00045"
SQ SEQUENCE 200 AA; 22120 MW; 8EBFB10433FE9085 CRC64;
MNDRMVWIDC EMTGLSLTDD ALIEVAALVT DSELNVLGEG VDLVIRPPDA ALETMPDVVR
EMHTASGLLD ELADGITLAD AEAQVLAYVR EHVKEPRKAP LCGNSVGTDR GFLLRDMPAL
ESHLHYRIVD VSSVKELARR WYPRAYFNSP PKNGNHRALA DIRESIAELR YYREAVFVPQ
PGPDSDTARA IAAKHTLSAE
//
