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PROQ_ECODH
ID   PROQ_ECODH              Reviewed;         232 AA.
AC   B1XH99;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   OrderedLocusNames=ECDH10B_1970;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: RNA chaperone with significant RNA binding, RNA strand
CC       exchange and RNA duplexing activities. May regulate ProP activity
CC       through an RNA-based, post-transcriptional mechanism.
CC       {ECO:0000255|HAMAP-Rule:MF_00749}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00749}.
CC   -!- SIMILARITY: Belongs to the ProQ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00749}.
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DR   EMBL; CP000948; ACB03029.1; -; Genomic_DNA.
DR   RefSeq; WP_000431381.1; NC_010473.1.
DR   AlphaFoldDB; B1XH99; -.
DR   SMR; B1XH99; -.
DR   KEGG; ecd:ECDH10B_1970; -.
DR   HOGENOM; CLU_113254_0_0_6; -.
DR   OMA; WRYLKGV; -.
DR   BioCyc; ECOL316385:ECDH10B_RS10095-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033592; F:RNA strand annealing activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034057; F:RNA strand-exchange activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:InterPro.
DR   Gene3D; 1.10.1710.10; -; 1.
DR   HAMAP; MF_00749; ProQ; 1.
DR   InterPro; IPR023529; ProQ.
DR   InterPro; IPR016103; ProQ/FinO.
DR   InterPro; IPR036442; ProQ/FinO_sf.
DR   InterPro; IPR035236; ProQ_C.
DR   PANTHER; PTHR38106; PTHR38106; 1.
DR   Pfam; PF04352; ProQ; 1.
DR   Pfam; PF17516; ProQ_C; 1.
DR   SMART; SM00945; ProQ; 1.
DR   SUPFAM; SSF48657; SSF48657; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; RNA-binding.
FT   CHAIN           1..232
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_1000133293"
FT   REGION          105..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   232 AA;  25893 MW;  042BEAA345A3C739 CRC64;
     MENQPKLNSS KEVIAFLAER FPHCFSAEGE ARPLKIGIFQ DLVDRVAGEM NLSKTQLRSA
     LRLYTSSWRY LYGVKPGATR VDLDGNPCGE LDEQHVEHAR KQLEEAKARV QAQRAEQQAK
     KREAAATAGE KEDAPRRERK PRPTTPRRKE GAERKPRAQK PVEKAPKTVK APREEQHTPV
     SDISALTVGQ ALKVKAGQNA MDATVLEITK DGVRVQLNSG MSLIVRAEHL VF
 
 
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