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_003112737 201 aa linear BCT 23-DEC-2024 ACCESSION WP_003112737 VERSION WP_003112737.1 KEYWORDS RefSeq. SOURCE Pseudomonas aeruginosa ORGANISM Pseudomonas aeruginosa Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. REFERENCE 1 (residues 1 to 201) AUTHORS Tchigvintsev,A., Tchigvintsev,D., Flick,R., Popovic,A., Dong,A., Xu,X., Brown,G., Lu,W., Wu,H., Cui,H., Dombrowski,L., Joo,J.C., Beloglazova,N., Min,J., Savchenko,A., Caudy,A.A., Rabinowitz,J.D., Murzin,A.G. and Yakunin,A.F. TITLE Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides JOURNAL Chem Biol 20 (11), 1386-1398 (2013) PUBMED 24210219 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 10785471 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..201 /organism="Pseudomonas aeruginosa" /db_xref="taxon:287" Protein 1..201 /product="Maf family protein" /EC_number="3.6.1.-" /GO_function="GO:0000166 - nucleotide binding [Evidence IEA]" /GO_function="GO:0047429 - nucleoside triphosphate diphosphatase activity [Evidence IEA]" /GO_process="GO:0009117 - nucleotide metabolic process [Evidence IEA]" /GO_process="GO:0009146 - purine nucleoside triphosphate catabolic process [Evidence IEA]" /calculated_mol_wt=20843 Region 2..193 /region_name="Maf" /note="7-methyl-GTP pyrophosphatase and related NTP pyrophosphatases, Maf/HAM1 superfamily [Secondary metabolites biosynthesis, transport and catabolism]; COG0424" /db_xref="CDD:440193" ORIGIN 1 mpslylasas prrrelltqi gvplsvlvta idesplpnea paayverlar gkaaaglaml 61 egrgedgcvl gadtsvvidg rilgkpvdqa dglamlaals grehqvltav alaaaggvea 121 rvvecrvrfr qvapeealry wqsgepadka ggyaiqglga ifvsriegsy savvglplce 181 taellrefgi pcwqpvggnp p