Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_000786582 475 aa linear BCT 01-JAN-2025 ACCESSION WP_000786582 VERSION WP_000786582.1 KEYWORDS RefSeq. SOURCE Shigella ORGANISM Shigella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 475) AUTHORS Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B. TITLE J-domain protein chaperone circuits in proteostasis and disease JOURNAL Trends Cell Biol 33 (1), 30-47 (2023) PUBMED 35729039 REFERENCE 2 (residues 1 to 475) AUTHORS Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T. TITLE The J-protein family: modulating protein assembly, disassembly and translocation JOURNAL EMBO Rep 5 (6), 567-571 (2004) PUBMED 15170475 REFERENCE 3 (residues 1 to 475) AUTHORS Kelley,W.L. TITLE The J-domain family and the recruitment of chaperone power JOURNAL Trends Biochem Sci 23 (6), 222-227 (1998) PUBMED 9644977 REFERENCE 4 (residues 1 to 475) AUTHORS Cyr,D.M., Langer,T. and Douglas,M.G. TITLE DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70 JOURNAL Trends Biochem Sci 19 (4), 176-181 (1994) PUBMED 8016869 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10644999 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..475 /organism="Shigella" /db_xref="taxon:620" Protein 1..475 /product="J domain-containing protein" /GO_process="GO:0006457 - protein folding [Evidence IEA]" /calculated_mol_wt=55148 Region 2..47 /region_name="DnaJ" /note="DnaJ molecular chaperone homology domain; smart00271" /db_xref="CDD:197617" Site order(31..32,36,39..40,43..44) /site_type="other" /note="HSP70 interaction site [polypeptide binding]" /db_xref="CDD:99751" ORIGIN 1 mkncwkildi eettdvdiir raylallpsf hpetdpqgfk qlrqayeeal riaqspaksv 61 wqpeeyevae heillafral lasdserflp sawqrfiqql nycsmeeide lrwslctiam 121 ntahlsfecv vllaerlrwl qeenvgeide eelesflyai akgnvfnfqt ilhlpvavqn 181 dtidfyqmfa riwsshpewl tlylaqhrav iipddaklhr nllrwysasr lgipelldya 241 rswreaepdn edaryyeyaq rvycgegesl laelcyywre ypstqadalm lqwcrqhrvy 301 yyplvvmmie ardlvndqgk pllyvpgdsa rtrfhlyeil sdeklsalgr slvemvlhkg 361 rkprisltrd tehplwplyl vakqlvqasq pteeslmpiv srldaedrcp lealiirrll 421 iqaanftgqe tvepepqpqp mpvddgglgc lgvikiifyi fifagligki lhlfg