位置:首页 > 蛋白库 > RBN_ENT38
RBN_ENT38
ID   RBN_ENT38               Reviewed;         305 AA.
AC   A4WCQ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ribonuclease BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase BN {ECO:0000255|HAMAP-Rule:MF_01818};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01818};
DE   AltName: Full=Ribonuclease Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
DE            Short=RNase Z homolog {ECO:0000255|HAMAP-Rule:MF_01818};
GN   Name=rbn {ECO:0000255|HAMAP-Rule:MF_01818}; Synonyms=rnz;
GN   OrderedLocusNames=Ent638_2818;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
CC   -!- FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and
CC       endoribonuclease activities. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01818};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_01818};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01818}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. RNase BN subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01818}.
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; CP000653; ABP61483.1; -; Genomic_DNA.
DR   RefSeq; WP_015959816.1; NC_009436.1.
DR   AlphaFoldDB; A4WCQ3; -.
DR   SMR; A4WCQ3; -.
DR   STRING; 399742.Ent638_2818; -.
DR   EnsemblBacteria; ABP61483; ABP61483; Ent638_2818.
DR   KEGG; ent:Ent638_2818; -.
DR   eggNOG; COG1234; Bacteria.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1712770at2; -.
DR   Proteomes; UP000000230; Chromosome.
DR   GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042779; P:tRNA 3'-trailer cleavage; IEA:InterPro.
DR   CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01818; RNase_Z_BN; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF12706; Lactamase_B_2; 2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   tRNA processing; Zinc.
FT   CHAIN           1..305
FT                   /note="Ribonuclease BN"
FT                   /id="PRO_1000070280"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01818"
SQ   SEQUENCE   305 AA;  33064 MW;  BDEF556BFDF44495 CRC64;
     MELIFLGTSA GVPTRSRNVT AILLDLQHPT RAGLWLFDCG EGTQHQLLHT AYHPGKLDKI
     FITHLHGDHV FGLPGLLCSR SMAGNVNPLT IFGPAGIREF TETALRLSGS WTDYPLEIVE
     VSEGVVFKDE QYTVTAGALN HPVECYGYRI EEHDKPGALD AAALIADGIK PGPLFQRLKH
     GDTVTLEDGR IVNGQDYLSA PQPGKKLVIF GDTAPCPAAL ALARNADVLV HEVTLEAAME
     EKANSRGHSS TRQAAQLARD ASVGKLLVTH ISSRYDAQGC ESLLKECRAV FPECELAQDF
     MQVCV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024