ID A0A2M9HRX8_9BIFI Unreviewed; 216 AA.
AC A0A2M9HRX8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=CUU80_04830 {ECO:0000313|EMBL:PJM79563.1};
OS Bifidobacterium scaligerum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM79563.1, ECO:0000313|Proteomes:UP000228755};
RN [1] {ECO:0000313|EMBL:PJM79563.1, ECO:0000313|Proteomes:UP000228755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (NOV-2017) 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:PJM79563.1}.
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DR EMBL; PGLQ01000002; PJM79563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9HRX8; -.
DR OrthoDB; 9801329at2; -.
DR Proteomes; UP000228755; 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:UP000228755}.
FT DOMAIN 16..191
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00045"
SQ SEQUENCE 216 AA; 24412 MW; 6B4385E5F439EE66 CRC64;
MVDSHDAETY SAKDSRLIWI DCEMTGLDIF GGDELVEVSV VPTDFDLNVL DEGVDFIIKP
SQKAVDHMND FVRNMHTRSG LINEWEHGLS LEEAEQKVTE YVLRFTPEGV KPLLAGNTIG
SDKKFLDHYM PNLMSHLHYR SVDVSTFKEL ARRWYPAVYE NRPPKNGGHR ALADIIESLD
ELRYYRKAFM APVPGPSEAE AKAISAQIVA SSLLNK
//
