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LOCUS WP_003123219 209 aa linear BCT 24-DEC-2024 ACCESSION WP_003123219 VERSION WP_003123219.1 KEYWORDS RefSeq. SOURCE Pseudomonas aeruginosa ORGANISM Pseudomonas aeruginosa Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. REFERENCE 1 (residues 1 to 209) AUTHORS Martin,J.L. and McMillan,F.M. TITLE SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold JOURNAL Curr Opin Struct Biol 12 (6), 783-793 (2002) PUBMED 12504684 REMARK Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142] REFERENCE 2 (residues 1 to 209) AUTHORS Brenner,C. TITLE Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases JOURNAL Biochemistry 41 (29), 9003-9014 (2002) PUBMED 12119013 REFERENCE 3 (residues 1 to 209) AUTHORS Lima,C.D., Klein,M.G. and Hendrickson,W.A. TITLE Structure-based analysis of catalysis and substrate definition in the HIT protein family JOURNAL Science 278 (5336), 286-290 (1997) PUBMED 9323207 REFERENCE 4 (residues 1 to 209) AUTHORS Seraphin,B. TITLE The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals JOURNAL DNA Seq 3 (3), 177-179 (1992) PUBMED 1472710 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 10472213 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..209 /organism="Pseudomonas aeruginosa" /db_xref="taxon:287" Protein 1..209 /product="HIT family protein" /GO_function="GO:1904047 - S-adenosyl-L-methionine binding [Evidence IEA]" /calculated_mol_wt=22938 Region <17..>66 /region_name="Adenylate forming domain, Class I superfamily" /note="This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate...; cl17068" /db_xref="CDD:473059" Region 74..166 /region_name="HIT" /note="HIT domain; pfam01230" /db_xref="CDD:395984" Site order(92,94,102,148,153,157,159) /site_type="active" /note="nucleotide binding site/active site [active]" /db_xref="CDD:238606" Site order(155,157,159..161) /site_type="active" /note="HIT family signature motif [active]" /db_xref="CDD:238606" Site 157 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:238606" ORIGIN 1 mfgvalysfg rhlmgrsage arqagaggcv gllwpggevs caavtagpfp eggaklsmnd 61 grtgevsmfa ldprleqdtl llgdfplsrl llmndarypw filvprredv telfqldvdd 121 rqalwreatl laevlkdtfr adkmnvanlg nvvsqlhmhv ivrrrgddaw pgpvwgrhpa 181 rpysseqvea irgklrmvlt dgfrfagea