位置:首页 > 蛋白库 > RBN_SHIB3
RBN_SHIB3
ID   RBN_SHIB3               Reviewed;         305 AA.
AC   B2TW54;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SbBS512_E2647;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD09128.1; -; Genomic_DNA.
DR   RefSeq; WP_001424321.1; NC_010658.1.
DR   AlphaFoldDB; B2TW54; -.
DR   SMR; B2TW54; -.
DR   STRING; 344609.SbBS512_E2647; -.
DR   EnsemblBacteria; ACD09128; ACD09128; SbBS512_E2647.
DR   KEGG; sbc:SbBS512_E2647; -.
DR   HOGENOM; CLU_031317_2_0_6; -.
DR   OMA; GTQRQMM; -.
DR   Proteomes; UP000001030; 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; IPR013469; Rnase_BN.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF12706; Lactamase_B_2; 2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
DR   TIGRFAMs; TIGR02649; true_RNase_BN; 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_1000187987"
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;  32960 MW;  679547AE8BDDF668 CRC64;
     MELIFLGTSA GVPTRTRNVT AILLNLQHPT QSGLWLFDCG EGTQHQLLHT AFNPGKLDKI
     FISHLHGDHL FGLPGLLCSR SMSGIIQPLT IYGPQGIREF VETALRISGS WTDYPLEIVE
     IGAGEILDDG LRKVTAYPLE HPLECYGYRI EEHDKPGALN AQALKAAGVP PGPLFQELKA
     GKTIMLEDGR QINGADYLAA PVPGKALAIF GDTGPCDAAL DLAKGVDVMV HEATLDITME
     AKANSRGHSS TRQAATLARE AGVGKLIITH VSSRYDDKGC QHLLRECRSI FPATELANDF
     TVFNV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024