Skip to main content
. 1998 Aug 4;95(16):9140–9145. doi: 10.1073/pnas.95.16.9140

Table 2.

Alignment of the four domains conserved in all CMP–Neu5Ac synthetases

Species aa motif I aa motif II aa motif III aa motif IV Acc. no.
mouse 45 ALVLARGGSKGIPLKN 83 FQSVWVSTD 140 IQATSPCL 209 LYENGSFYF AJ006215
Haemophilus influenzae 9 AIIPARAGSKGIKDKN 47 FDQIVVTSD 105 LQPTSPLR 173 YRANGAIYI U32807
N. meningitidis 7 AVILARQNSKGLPLKN 45 FDRIIVSTD 103 LQPTSPLR 172 FRPNGAIYI X78068
E. coli 7 AIIPARSGSKGLRNKN 45 FEKVIVTTD 102 LQPTSPFR 170 YHPNGAIFI P13266*
Streptococcus agalactiae 5 CIIPARSGSKGLPDKN 45 KKDIFVSTD 102 LQVTSPLR 170 YYPNGAIFI U19899
Haemophilus ducreyi 5 AIIPARAGSKGIKDKN 43 FDHIIVSSD 100 IQPTSPLR 169 YRANGAIYI U54496
Helicobacter pylori 5 AIVLARSSSKRIKNKN 43 FEKVFISSD 170 YHDAGLLYM AE000550
Consensus sequence AIIpAR-GSKGi--KN F--i-VStD LQPTSPLR Y--NGAIYI

The table aligns the four amino acid stretches of high conservation contained in the murine and bacterial enzymes. Numbers indicate the amino acid residue, with which the motifs start. In the consensus sequence, amino acid residues identical in at least five of seven sequences are shown as capital letters; those conserved in at least four sequences are shown in small letters. Boxed residues are identical for all species. Abbreviations: aa, amino acids; acc. no., accession number. 

*

SwissProt database. 

European Molecular Biology Laboratory database. 

GenBank database.