RNB_XENBS
ID RNB_XENBS Reviewed; 646 AA.
AC D3V184;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Exoribonuclease 2 {ECO:0000255|HAMAP-Rule:MF_01036};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01036};
DE AltName: Full=Exoribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
DE Short=RNase II {ECO:0000255|HAMAP-Rule:MF_01036};
DE Short=Ribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
GN Name=rnb {ECO:0000255|HAMAP-Rule:MF_01036}; OrderedLocusNames=XBJ1_2302;
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004;
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3' to 5' direction.
CC {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01036}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01036}.
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DR EMBL; FN667741; CBJ81428.1; -; Genomic_DNA.
DR RefSeq; WP_012988744.1; NC_013892.1.
DR AlphaFoldDB; D3V184; -.
DR SMR; D3V184; -.
DR STRING; 406818.XBJ1_2302; -.
DR PRIDE; D3V184; -.
DR EnsemblBacteria; CBJ81428; CBJ81428; XBJ1_2302.
DR GeneID; 8831915; -.
DR KEGG; xbo:XBJ1_2302; -.
DR PATRIC; fig|406818.4.peg.2075; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR Proteomes; UP000002045; Chromosome.
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; 2.40.50.140; -; 2.
DR HAMAP; MF_01036; RNase_II; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
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 Pfam; PF17876; CSD2; 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; SSF50249; 4.
DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR TIGRFAMs; TIGR02062; RNase_B; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..646
FT /note="Exoribonuclease 2"
FT /id="PRO_0000409537"
FT DOMAIN 563..645
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 646 AA; 73860 MW; 96A4A4256937EDBA CRC64;
MFQNNPLLAQ LKQQLYSQTL RVEGLVKGTE KGFGFLEVDG QKSYFIPPPQ MKKVMHGDRI
TAAIHTDKEK EIAEPEALIE PFLTRFVGRV QKKENDNRLW IIPDHPLLKD TILCRPANQV
THNFENGDWA VAEMRRHPLK GDRGFQAEIT GYIIKGDDHY APWWVTLTRH SLQREAPTMP
DCQLDDGSLE RIDLTALDFV TIDSATTEDM DDALHIVKNN DGSLKLSIAI ADPTAYIKAD
SELDKIAYQR SFTNYLPGFN IPMLPRELSD DLCSLRPKAR RPALVCQVSI LEDGQLGDDM
QFFAAWVESK FKLAYDDVSD WLEHQTGWKP ESEAVTTQIT LLQEMCERRN QWRHQYALVF
KERPDYRFVL DKGGNVVDIV IDQRRSANRI VEEAMITANL CAAKILRDKL GFGIYNVHTG
FEPTQIDQVV DVLKENGIEA EANALLELDG FCQLRRELDQ QPTQFLDSRI RRFQTFAEIR
PEPGPHFGLG FDAYATWTSP IRKYSDIINH RLLKAIIQQT EEEKPSEEVC LQLTERRRAN
RMAERDVGDW LYARFLHPHA GTDKTFSAEI VDITRGGLRI RLVDNGAIAF VPGSFLHAVR
DELQCSQETG SVLIKGEAVH RLNDIINVRI EEVRMETRNI VARPVA