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LOCUS WP_002892937 132 aa linear BCT 24-DEC-2024 ACCESSION WP_002892937 VERSION WP_002892937.1 KEYWORDS RefSeq. SOURCE Gammaproteobacteria ORGANISM Gammaproteobacteria Bacteria; Pseudomonadati; Pseudomonadota. REFERENCE 1 (residues 1 to 132) AUTHORS Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E. TITLE The evolution of function within the Nudix homology clan JOURNAL Proteins 85 (5), 775-811 (2017) PUBMED 27936487 REFERENCE 2 (residues 1 to 132) AUTHORS McLennan,A.G. TITLE The Nudix hydrolase superfamily JOURNAL Cell Mol Life Sci 63 (2), 123-143 (2006) PUBMED 16378245 REFERENCE 3 (residues 1 to 132) AUTHORS Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M., Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M. TITLE Structures and mechanisms of Nudix hydrolases JOURNAL Arch Biochem Biophys 433 (1), 129-143 (2005) PUBMED 15581572 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 10140390 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..132 /organism="Gammaproteobacteria" /db_xref="taxon:1236" Protein 1..132 /product="NUDIX hydrolase" /EC_number="3.6.1.-" /GO_function="GO:0016817 - hydrolase activity, acting on acid anhydrides [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0009132 - nucleoside diphosphate metabolic process [Evidence IEA]" /calculated_mol_wt=14503 Region 12..128 /region_name="NUDIX_Hydrolase" /note="uncharacterized NUDIX hydrolase subfamily; cd04690" /db_xref="CDD:467572" ORIGIN 1 mkmiiiaaai itdsqgrcll vrkrgteyfm qpggkpeige tphaalirel eeelnfsvsp 61 eelvqvgrft daaanepghl vsadvfliat nrvsftptme ieeviwftpg qdrhiklapl 121 tenhllpllk gv