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LOCUS WP_003085816 161 aa linear BCT 20-JAN-2025 [Pseudomonas]. ACCESSION WP_003085816 VERSION WP_003085816.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 161) AUTHORS Quistgaard,E.M., Weininger,U., Ural-Blimke,Y., Modig,K., Nordlund,P., Akke,M. and Low,C. TITLE Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD JOURNAL BMC Biol 14 (1), 82 (2016) PUBMED 27664121 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 161) AUTHORS Gothel,S.F. and Marahiel,M.A. TITLE Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts JOURNAL Cell Mol Life Sci 55 (3), 423-436 (1999) PUBMED 10228556 REFERENCE 3 (residues 1 to 161) AUTHORS Trandinh,C.C., Pao,G.M. and Saier,M.H. Jr. TITLE Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases JOURNAL FASEB J 6 (15), 3410-3420 (1992) PUBMED 1464374 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 11437275 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..161 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..161 /product="FKBP-type peptidyl-prolyl cis-trans isomerase" /EC_number="5.2.1.8" /GO_function="GO:0003755 - peptidyl-prolyl cis-trans isomerase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0006457 - protein folding [Evidence IEA]" /calculated_mol_wt=16879 Region 3..140 /region_name="SlpA" /note="Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones]; COG1047" /db_xref="CDD:440668" ORIGIN 1 mqiaankavs idytltndag dvidssagga plvylhgagn iivglekale gknvgdelsv 61 aiepedayge ysaelvatlt remfegvdel evgmqfhasa pdggmqivti rdidgddvtv 121 dgnhplagqr lnfkvkvvdv reanaeeiah ghihgegghh h