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_003722138 366 aa linear BCT 04-JUN-2024 ACCESSION WP_003722138 VERSION WP_003722138.1 KEYWORDS RefSeq. SOURCE Listeria ORGANISM Listeria Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae. REFERENCE 1 (residues 1 to 366) AUTHORS Hannemann,L., Suppanz,I., Ba,Q., MacInnes,K., Drepper,F., Warscheid,B. and Koch,H.G. TITLE Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1 JOURNAL Antioxid Redox Signal 24 (3), 141-156 (2016) PUBMED 26160547 REFERENCE 2 (residues 1 to 366) AUTHORS Rosler,K.S., Mercier,E., Andrews,I.C. and Wieden,H.J. TITLE Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF JOURNAL J Biol Chem 290 (30), 18650-18661 (2015) PUBMED 26018081 REFERENCE 3 (residues 1 to 366) AUTHORS Becker,M., Gzyl,K.E., Altamirano,A.M., Vuong,A., Urban,K. and Wieden,H.J. TITLE The 70S ribosome modulates the ATPase activity of Escherichia coli YchF JOURNAL RNA Biol 9 (10), 1288-1301 (2012) PUBMED 22995830 REFERENCE 4 (residues 1 to 366) AUTHORS Teplyakov,A., Obmolova,G., Chu,S.Y., Toedt,J., Eisenstein,E., Howard,A.J. and Gilliland,G.L. TITLE Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid JOURNAL J Bacteriol 185 (14), 4031-4037 (2003) PUBMED 12837776 REFERENCE 5 (residues 1 to 366) AUTHORS Mittenhuber,G. TITLE Comparative genomics of prokaryotic GTP-binding proteins (the Era, Obg, EngA, ThdF (TrmE), YchF and YihA families) and their relationship to eukaryotic GTP-binding proteins (the DRG, ARF, RAB, RAN, RAS and RHO families) JOURNAL J Mol Microbiol Biotechnol 3 (1), 21-35 (2001) PUBMED 11200227 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 :: TIGR00092.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..366 /organism="Listeria" /db_xref="taxon:1637" gene 1..366 /gene="ychF" Protein 1..366 /product="redox-regulated ATPase YchF" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_function="GO:0005525 - GTP binding [Evidence IEA]" /GO_function="GO:0016887 - ATP hydrolysis activity [Evidence IEA]" /calculated_mol_wt=40552 Region 3..366 /region_name="GTP1" /note="Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis]; COG0012" /db_xref="CDD:439783" ORIGIN 1 maltagivgl pnvgkstlfn aitkagaeaa nypfatidpn vgivevpdhr lnkltelvkp 61 kktvpttfef tdiagivkga skgeglgnkf lshirqvdai chvtrcfdde nithvegrvd 121 plddistinl eliladletv ekrigrvekl skqkdkdava eynvlvklre afendkpara 181 iefneeeeki vrnlflltrk pvlyvanvse edvsspddnk yvqqvrefaa sensevivvc 241 araeeeiael ededklefle algieesgld qlirsaytll glatyftagv qevrawtfik 301 gmkapqcagi ihtdfergfi raevvaydal leygseqaak eagkvrlegk eyemkdgdvv 361 hfrfnv