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PROQ_PROMH
ID   PROQ_PROMH              Reviewed;         230 AA.
AC   B4ETI7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749}; OrderedLocusNames=PMI1015;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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; AM942759; CAR42220.1; -; Genomic_DNA.
DR   RefSeq; WP_004242572.1; NC_010554.1.
DR   AlphaFoldDB; B4ETI7; -.
DR   SMR; B4ETI7; -.
DR   STRING; 529507.PMI1015; -.
DR   EnsemblBacteria; CAR42220; CAR42220; PMI1015.
DR   GeneID; 6801025; -.
DR   KEGG; pmr:PMI1015; -.
DR   eggNOG; COG3109; Bacteria.
DR   HOGENOM; CLU_113254_0_0_6; -.
DR   OMA; WRYLKGV; -.
DR   Proteomes; UP000008319; Chromosome.
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; Reference proteome; RNA-binding.
FT   CHAIN           1..230
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_1000133300"
FT   REGION          104..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25837 MW;  D036EA88E517CF02 CRC64;
     MENQPKLNSS KEIIAFLAER FPKCFIAEGE ARPLKVGIFQ DLVEHLKDET QLSKTQLRSA
     LRLYTSSWRY LYGVKEGAKR VDLNGNDCGE LEAEHIAHAR TQLAEAKARV QAQRAEQRAK
     KREAEGDKET SKRPAAKKPN PRRQAPKDGE KRQPRPQKQA NQAPRKAPRQ NTEKLTPVKD
     ISVLTVGQSL KVNVGSSVMD ATVLEIAKEG VRVQLPNGLA MNVRTEHLKF
 
 
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