位置:首页 > 蛋白库 > RNB_XENBS
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024