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_003119646 442 aa linear BCT 01-MAR-2025 ACCESSION WP_003119646 VERSION WP_003119646.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 442) AUTHORS Stachelhaus,T., Mootz,H.D., Bergendahl,V. and Marahiel,M.A. TITLE Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain JOURNAL J Biol Chem 273 (35), 22773-22781 (1998) PUBMED 9712910 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 :: NF012873.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00668.25 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..442 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..442 /product="condensation domain-containing protein" /GO_function="GO:0003824 - catalytic activity [Evidence IEA]" /calculated_mol_wt=49004 Region 9..241 /region_name="COG4908" /note="Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only]" /db_xref="CDD:443936" ORIGIN 1 mmaeirrpls averwywlsd qfsalnvisr vrvhgrlsid dlrrgldalq arhpllrari 61 ehdagldprw vpcerpiplr evrgggeeqw lreinerelp eridpdsgpl irtvaiatda 121 gahdllvvvp hiiadgttvl tlaeqwltla adpaaqpwta salppaedlr prrftgdega 181 arlaeqtaqd ealvgrhrpg riepsnpvpl earrtrllhr eldgaqleql qrrarehgtt 241 vhgaltaala iaaghdhqrr pshiaigspi dfrdeleppv rpdevgtyva tvpvvldiar 301 pfwevaralt ddlgerrrqg hhfnlvtlva saaprcmada rpfmafmeae gpinlcssni 361 grypfperig alrlsdaqfl tgisvngyfv aainsshgrl fwnftyidea vpgeraerla 421 edclgtllsa ihapqrsale eq