Comparing 4 sequences
STET_BACSU / O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168)
TC 2.A.3.8.12 / O34739 The Ser/Thr exchange transporter (SteT) (also transports aromatic amino acids with lower efficiency) (Reig et al., 2007). The substrate-bound state of SteT shows increased conformational flexibility and kinetic stability, enabling transport of substrate across the cell membrane (Bippes et al. 2009). TMS8 sculpts the substrate-binding site and undergoes conformational changes during the transport cycle of SteT (Bartoccioni et al., 2010). Mutations allow substrate binding but not translocation. Other mutations stabilize the protein and result in higher production levels from Bacillus subtilis
438 amino acids: PaperBLAST, CDD
LAT2_RAT / Q9WVR6 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; Solute carrier family 7 member 8 from Rattus norvegicus (Rat) (heteromeric)
TC 2.A.3.8.6 / Q9WVR6 L-type neutral amino acid transporter, LAT2 (Na+-independent with broad specificity for all L-isomers of neutral amino acids; preferred substrate: Phe, His, Trp, Ile, Val, Leu, Gln, Cys, Ser; catalyzes obligatory exchange with μM affinities on the outside and mM affinities on the inside [1000x difference]). Both LAT2 and LAT1 (2.A.3.8.1) catalyze uptake of S-nitro-L-cysteine (Li and Whorton, 2005). Also transports thyroid hormones from Rattus norvegicus (Rat) (heteromeric)
533 amino acids: PaperBLAST, CDD
31% identical to query, 80% coverage
TC 2.A.3.8.3 / Q26594 The schistosome neutral and cationic amino acid transporter, SPRM1lc (Na+-independent), (takes up phe, arg, lys, ala, gln, his, trp and leu; functions with SPRM1hc (TC# 8.A.9.3.1) from Schistosoma mansoni (Blood fluke)
503 amino acids: PaperBLAST, CDD
28% identical to query, 86% coverage
TC 2.A.3.8.10 / Q9NA91 Aromatic amino acid exchanger, AAT-9 (Veljkovic et al., 2004b) from Caenorhabditis elegans
541 amino acids: PaperBLAST, CDD
26% identical to query, 71% coverage
None