ID A0A1V3LBZ0_9PAST Unreviewed; 659 AA.
AC A0A1V3LBZ0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Exoribonuclease 2 {ECO:0000256|HAMAP-Rule:MF_01036};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01036};
DE AltName: Full=Exoribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
DE Short=RNase II {ECO:0000256|HAMAP-Rule:MF_01036};
DE Short=Ribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
GN Name=rnb {ECO:0000256|HAMAP-Rule:MF_01036};
GN ORFNames=BKG88_02320 {ECO:0000313|EMBL:OOF87165.1};
OS Rodentibacter ratti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1906745 {ECO:0000313|EMBL:OOF87165.1, ECO:0000313|Proteomes:UP000189353};
RN [1] {ECO:0000313|EMBL:OOF87165.1, ECO:0000313|Proteomes:UP000189353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppn158 {ECO:0000313|EMBL:OOF87165.1,
RC ECO:0000313|Proteomes:UP000189353};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3' to 5' direction.
CC {ECO:0000256|HAMAP-Rule:MF_01036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01036}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000256|ARBA:ARBA00009925, ECO:0000256|HAMAP-Rule:MF_01036}.
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:OOF87165.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLAI01000010; OOF87165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3LBZ0; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000189353; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.640; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01036; RNase_II; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR011804; RNase_II.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02062; RNase_B; 1.
DR PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01036};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01036};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01036};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01036};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01036}.
FT DOMAIN 576..659
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 659 AA; 75672 MW; F38B24C35CCA03BD CRC64;
MFQDNPLLAQ LKQQIHESKE RVEGVVKSTD KAYGFLECDK KTYFIAPPAM KKVMHGDKIT
ATIEKQGDKE QAEPESLIEP MLTRFIAKVR FNKDKKLQVL VDHPSINQPI GAQQAKSVKE
ELQEGDWVVA NLKTHPLRDD RFFYATINQF ICRAEDEFAP WWVTLARHEQ SRYPVQGADH
YEMLDQQTRE DLTALHFVTI DSESTQDMDD ALYIEPVAQN GEQTGWKLVV AIADPTAYIA
LDSQIEKDAK QRCFTNYLPG FNIPMLPREL SDELCSLMAN EPRPALVCYI ETDLQGNITA
KPHFVSAYVQ SKAKLAYNKV SDYLEQAADA WQPETSEINE QIQRLHQFTL ARINWRKTHS
LLFKEKPDYS FVLAENGKVQ EIKAEYRRIA NQIVEESMII ANICAAQFLN EQAHTGIFNT
HSGFDKKFVG NAHQFLMANL ANEENQAELN ERYSVENLST LSGYCQMRHD IEPIEGDYLE
LRLRRYLTFA EFKSELAPHF GLGLEGYATW TSPIRKYSDM VNHRLIKAVL TQQPCEKPQD
EVLARLQEAR RQNRLVERDI ADWLYCRYLA DKVAENAEFD AEVQDVMRGG LRVQLLENGA
SMFVPASALH NNKEEIQVNY DELALYIKGE RTYKIGDIVR VKLTEVKEST RSIVGSVIL
//
