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MULTISPECIES: peptidylprolyl isomerase [Vibrio].


LOCUS       WP_020332956             164 aa            linear   BCT 28-AUG-2024
ACCESSION   WP_020332956
VERSION     WP_020332956.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
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  :: HMM
            Evidence Accession :: NF012387.5
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00160.26
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..164
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=17993
     Region          1..164
                     /region_name="cyclophilin"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases. This family contains eukaryotic, bacterial and
                     archeal proteins which exhibit a peptidylprolyl cis- trans
                     isomerases activity (PPIase, Rotamase) and in addition
                     bind the immunosuppressive drug...; cl00197"
                     /db_xref="CDD:469651"
     Site            order(43,45,48..49,51,86..91,99,107..108,120)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238901"
ORIGIN      
        1 mitlhtnfgd ikiqlneeka petsanflqy crdgfydntl fhrvidgfmv qgggmesglr
       61 ekatrapikn eannglsnkv gtlamartme phsassqffi nvnnntfldf rsesldgwgy
      121 cvfgevvegm dvvnqikgvs tgsygmhqdv pledvvitgt tiee