ID A0A1V3JY18_9PAST Unreviewed; 659 AA.
AC A0A1V3JY18;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BKL51_03885 {ECO:0000313|EMBL:OOF65779.1};
OS Rodentibacter sp. Ppn85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1908525 {ECO:0000313|EMBL:OOF65779.1, ECO:0000313|Proteomes:UP000189325};
RN [1] {ECO:0000313|EMBL:OOF65779.1, ECO:0000313|Proteomes:UP000189325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppn85 {ECO:0000313|EMBL:OOF65779.1,
RC ECO:0000313|Proteomes:UP000189325};
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:OOF65779.1}.
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DR EMBL; MLHS01000019; OOF65779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3JY18; -.
DR STRING; 1908525.BKL51_03885; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000189325; 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..658
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 659 AA; 75972 MW; B1C2A576D20096AA CRC64;
MFQDNPLLAQ LKQQIHETKE RVEGVVKSTD KAYGFLECDK KTYFLAPPAM KKVMHGDKIT
ATIEKQGDKE QAEPESLIEP MLTRFIAKVR FNKDKKLQVL VDHPSINQPI GAQQAKSVKE
ELQEGDWVVA NLKTHPLRDD RFFYATINQF ICRADDEFAP WWVTLARHEQ SRYPVQGAEH
YEMLDQQMRE DLTALHFVTI DSESTQDMDD ALYIEPVEQN GEQIGWKLVV AIADPTAYIA
LDSQIEKDAK QRCFTNYLPG FNIPMLPREL SDELCSLMAN ETRPALVCYI ETDLQGNIAT
KPHFVSAYVQ SKAKLAYNKV SDYLEQVANA WQPETEEISE QIRRLYQFTQ SRINWRKTHS
LLFKEKPDYS FVLAENGKVQ DIKAEHRRIA NQIVEESMII ANICAAQFLN EQTKTGIFNT
HSGFDKKFLE NAHHFLMANL ANEENQAELN ERYSTENLST LNGYCQMRHD IEPIDGDYLE
LRLRRYLTFA EFKAELAPHF GLGLEGYATW TSPIRKYSDM VNHRLIKAVL TQQPYEKPQD
EVLARLQEAR RQNRLVERDI ADWLYCRYLV DKVAENAEFD AEVQDVTRGG LRVQLLENGA
SMFVPASTLH NNKEEIQVNT DELALYIKGE RAYKIGDIVR VKLTEVKEAT RSIVGSVII
//
