ID A0A1Y2SMB1_9GAMM Unreviewed; 646 AA.
AC A0A1Y2SMB1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=Xbed_01799 {ECO:0000313|EMBL:OTA20083.1};
OS Xenorhabdus beddingii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=40578 {ECO:0000313|EMBL:OTA20083.1, ECO:0000313|Proteomes:UP000194204};
RN [1] {ECO:0000313|EMBL:OTA20083.1, ECO:0000313|Proteomes:UP000194204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4764 {ECO:0000313|EMBL:OTA20083.1,
RC ECO:0000313|Proteomes:UP000194204};
RA Tobias N.J., Wolff H., Djahanschiri B., Ebersberger I., Bode H.B.;
RT "Deconstructing symbiosis and pathogenesis requirements using a combined
RT genomic-metabolomic approach.";
RL Submitted (JAN-2017) 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:OTA20083.1}.
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DR EMBL; MUBK01000012; OTA20083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2SMB1; -.
DR STRING; 40578.Xbed_01799; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000194204; 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 SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 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 23..79
FT /note="Cold shock"
FT /evidence="ECO:0000259|SMART:SM00357"
FT DOMAIN 191..519
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
SQ SEQUENCE 646 AA; 73726 MW; 4527E6ECCE15E2F1 CRC64;
MFQNNPLLAQ LKQQLHAKTT RVEGLVKGTE KGFGFLEVDG QKSYFIPPPY MKKVMHGDRI
TAAIHTDKEK EIADPETLVE PFLTRFVGRI QKKENDNRLW IIPDHPLLKD TIPCRPASQV
THTFQHGDWA VAEMRRHPLK GDRGFQAEVT GYITQGDDHY APWWVTLTRH SLGREAPVMT
DCQLDNESIE RTDLTALDFV TIDSATTEDM DDALYITQND DGSLKLSIAI ADPTAYIKAD
SELDKIAYQR SFTNYLPGFN IPMLPRELSD DLCSLRPNVR RPALVCQVSI LENGQLGDDI
QFFAAWVESK FKLVYDEVSD WLEGQEGWEP KSEAVKTQIT LLKEMCERRN NWRHQHALVF
KERPDYRFML DEGGHVVDIV IEQRRSANRI VEEAMIAANL CAAMVLRDKL GFGIYNVHTG
FDSTHIEQVV EVLKEYGIDA NAEALLGLDG FCKLRRELDK QPTQFLDSRI RRFQTFAEIK
TEPGPHFGLG FDAYATWTSP IRKYSDIINH RLLKAIIQQT DVEKPTEEIC LQLTDRRRAN
RLAERDVGDW LYARFLHPHA GTDKTFPAEI IDITRGGLRV RLVDNGAIAF VPGPFLHAVR
DELQCSQETG SVLIKGEAAY RLNDIIDVRI EEVRMETRNI VARPVG
//
