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LOCUS WP_001281825 334 aa linear BCT 18-JUL-2020 ACCESSION WP_001281825 VERSION WP_001281825.1 KEYWORDS RefSeq. SOURCE Escherichia ORGANISM Escherichia Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 334) AUTHORS Villeret,V., Clantin,B., Tricot,C., Legrain,C., Roovers,M., Stalon,V., Glansdorff,N. and Van Beeumen,J. TITLE The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures JOURNAL Proc. Natl. Acad. Sci. U.S.A. 95 (6), 2801-2806 (1998) PUBMED 9501170 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 :: TIGR00658.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..334 /organism="Escherichia" /db_xref="taxon:561" gene 1..334 /gene="argF" Protein 1..334 /product="ornithine carbamoyltransferase" /EC_number="2.1.3.3" /GO_function="GO:0004585 - ornithine carbamoyltransferase activity [Evidence IEA]" /GO_process="GO:0042450 - arginine biosynthetic process via ornithine [Evidence IEA]" /calculated_mol_wt=36696 Region 1..332 /region_name="PRK03515" /note="ornithine carbamoyltransferase subunit I; Provisional" /db_xref="CDD:179587" ORIGIN 1 msdlykkhfl klldftpaqf tslltlaaql kadkkngkev qkltgknial ifekdstrtr 61 csfevaafdq garvtylgps gsqighkesi kdtarvlgrm ydgiqyrghg qevvetlaqy 121 agvpvwnglt nefhptqlla dlmtmqehlp gkafnemtlv yagdarnnmg nsmleaaalt 181 gldlrllapk acwpeeslva ecsalaekhg gkitltedva agvkgadfiy tdvwvsmgea 241 kekwaerial lrgyqvnaqm maltdnpnvk flhclpafhd dqttlgkqma kefdlhggme 301 vtdevfesaa sivfdqaenr mhtikavmma tlge