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LOCUS WP_004184155 396 aa linear BCT 25-JUL-2024 ACCESSION WP_004184155 VERSION WP_004184155.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 396) AUTHORS Qi,Y. and Grishin,N.V. TITLE Structural classification of thioredoxin-like fold proteins JOURNAL Proteins 58 (2), 376-388 (2005) PUBMED 15558583 REFERENCE 2 (residues 1 to 396) AUTHORS Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J. TITLE Thioredoxin superfamily and thioredoxin-inducing agents JOURNAL Ann N Y Acad Sci 957, 189-199 (2002) PUBMED 12074972 REFERENCE 3 (residues 1 to 396) AUTHORS Aslund,F. and Beckwith,J. TITLE The thioredoxin superfamily: redundancy, specificity, and gray-area genomics JOURNAL J Bacteriol 181 (5), 1375-1379 (1999) PUBMED 10049365 REFERENCE 4 (residues 1 to 396) AUTHORS Chivers,P.T., Prehoda,K.E. and Raines,R.T. TITLE The CXXC motif: a rheostat in the active site JOURNAL Biochemistry 36 (14), 4061-4066 (1997) PUBMED 9099998 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 10002702 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..396 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..396 /product="cytochrome c biogenesis protein/redoxin" /GO_function="GO:0015036 - disulfide oxidoreductase activity [Evidence IEA]" /GO_process="GO:0017004 - cytochrome complex assembly [Evidence IEA]" /calculated_mol_wt=42368 Region 1..183 /region_name="CcdA" /note="Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; COG0785" /db_xref="CDD:440548" Region 254..378 /region_name="Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold" /note="The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox...; cl00388" /db_xref="CDD:469754" ORIGIN 1 msiliaflgg mltllspctl pvipllfasv rgrrgqlaim lagmalmfga vswlvtvasg 61 wvvnltlagr glalaffalv glsllsqrva qrltsplval gnqlndassr qrgwigslla 121 glavgllwap cagpvlgail slgfvhpgqa ttgglllayg sggalmlfll gwcgaaliar 181 lrrgqafger lrrlaggaml asvaliasgg drylqsaggl sqaleqrlaa rlpqpeqkts 241 lqpiaapqps sampslaggs awinspaltp erlkgkvvlv dfwtrecinc qhtlpyvrdw 301 ankyraaglv vigvhtpeyp werslpllrq avkdwrityp vvadneyaiw nafgnqywpa 361 hyifdargql rytafgegdy arqeqviqql lqeska