SitesBLAST
Comparing CCNA_02495 FitnessBrowser__Caulo:CCNA_02495 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
42% identity, 95% coverage: 15:400/405 of query aligns to 14:393/403 of P77589
- E27 (= E28) mutation to A: Lack of 3HPP transport activity.; mutation to D: Slight decrease in 3HPP transport activity.
- D75 (= D76) mutation D->A,E: Lack of 3HPP transport activity.
- A272 (≠ W277) mutation to H: 30% increase in 3HPP transport activity.
- K276 (≠ H281) mutation to D: Lack of 3HPP transport activity.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
34% identity, 95% coverage: 18:400/405 of query aligns to 23:435/452 of Q5EXK5
- D82 (= D76) mutation to A: Loss of activity.
- V311 (≠ W277) mutation to W: Loss of activity.
- D314 (= D280) mutation to A: Loss of activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
34% identity, 91% coverage: 18:384/405 of query aligns to 31:426/448 of Q51955
- D41 (≠ E28) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D31) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G72) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D76) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G79) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
- R124 (= R111) mutation to A: Abolishes 4-HBA transport.
- E144 (= E131) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ R170) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (= D280) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- H328 (≠ L287) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
- R386 (= R344) mutation to A: Strong decrease in 4-HBA transport.
- R398 (= R356) mutation to A: Abolishes 4-HBA transport.
Sites not aligning to the query:
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
30% identity, 94% coverage: 1:381/405 of query aligns to 26:413/444 of Q8NLB7
- D54 (≠ E28) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (= D31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R77) mutation to A: Loss of transport activity.
- W309 (= W277) mutation to V: Loss of transport activity.
- D312 (= D280) mutation to A: Loss of transport activity.
- R313 (= R282) mutation to A: Loss of transport activity.
- I317 (≠ T286) mutation I->H,Y: Loss of transport activity.
- R386 (= R356) mutation to A: Loss of transport activity.
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
28% identity, 39% coverage: 40:195/405 of query aligns to 177:344/727 of Q9Z2I6
Sites not aligning to the query:
- 1:57 Interaction with SYT1
- 529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
- 559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.
Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
28% identity, 39% coverage: 40:195/405 of query aligns to 177:344/727 of Q496J9
Sites not aligning to the query:
- 519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
- 534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
- 561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
- 563 F→A: No longer interacts with BoNT/A HC.
- 565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
23% identity, 95% coverage: 15:397/405 of query aligns to 22:421/430 of P0AA76
- Y29 (≠ C22) binding
- D31 (= D31) mutation to N: Loss of galactonate transport activity.
- R32 (≠ L32) binding
- Y64 (≠ L64) binding
- E118 (≠ L118) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ Y332) binding
Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
31% identity, 30% coverage: 40:162/405 of query aligns to 191:313/742 of Q02563
- DMCLS 196:200 (≠ DLGLK 45:49) mutation Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E).
Sites not aligning to the query:
- 321:331 mutation Missing: No change in uptake of BoNT/D or BoNT/E.
- 498 N→Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D.
- 548 N→Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D.
- 570:573 RLVN→TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E.
- 573 N→Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D.
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
23% identity, 95% coverage: 15:397/405 of query aligns to 11:402/409 of 6e9nA
P9WJY3 Probable triacylglyceride transporter Rv1410c; MFS-type drug efflux transporter P55 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 34% coverage: 51:189/405 of query aligns to 45:185/518 of P9WJY3
Sites not aligning to the query:
- 22 D→A: Susceptible to ethidium bromide, tested in M.smegmatis.; D→E: Decreases resistance to ethidium bromide, tested in M.smegmatis.
Q8BN82 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Mus musculus (Mouse) (see paper)
27% identity, 49% coverage: 51:247/405 of query aligns to 106:316/495 of Q8BN82
- H183 (≠ I126) mutation to R: Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.
Sites not aligning to the query:
- 39 R→C: Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
25% identity, 44% coverage: 15:192/405 of query aligns to 14:185/393 of 6e9oA
Sites not aligning to the query:
Q9NRA2 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Membrane glycoprotein HP59; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Homo sapiens (Human) (see 8 papers)
26% identity, 49% coverage: 51:247/405 of query aligns to 106:316/495 of Q9NRA2
- K136 (= K81) to E: in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity; dbSNP:rs80338795
- H183 (≠ I126) to R: in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity; dbSNP:rs119491109
- LL 198:199 (≠ AV 141:142) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ FV 209:210) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ EALAG 211:215) natural variant: Missing (in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity)
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane.; LL→GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R → C: in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity; dbSNP:rs80338794
- 328 G → E: in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs386833996
- 334 P → R: in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs119491110
- 371 G → V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
Q5Q0U0 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 (Anion/sugar transporter), member 5; Vesicular excitatory amino acid transporter; VEAT from Rattus norvegicus (Rat) (see 2 papers)
27% identity, 49% coverage: 51:247/405 of query aligns to 106:316/495 of Q5Q0U0
- K136 (= K81) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R111) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ T114) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G115) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (≠ L118) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (= G119) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ L122) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P123) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I126) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V129) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ EALAG 211:215) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R→C: Markedly decreases H(+)-coupled sialic acid transporter activity.
- 334 P→R: Abolishes H(+)-coupled sialic acid transporter activity.
- 371 G→V: Remains in the endoplasmic reticulum.
Q94KE0 Sugar transporter ESL1; Protein EARLY-RESPONSIVE TO DEHYDRATION 6-LIKE 1; ERD six-like 1; Sugar transporter ERD6-like 3; Sugar transporter-like protein 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 43% coverage: 35:207/405 of query aligns to 53:219/470 of Q94KE0
Sites not aligning to the query:
- 10 L→A: Localizes mainly to the endoplasmic reticulum.
- 10:16 Essential for the localization to the vacuole membrane
- 14 L→A: Localizes to the plasma membrane. Loss of localization to the vacuole membrane; when associated with A-15 and A-16.
- 15 L→A: Localizes to the plasma membrane. Loss of localization to the vacuole membrane; when associated with A-14 and A-16.
- 16 L→A: Loss of localization to the vacuole membrane; when associated with A-14 and A-15.
O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
28% identity, 40% coverage: 56:219/405 of query aligns to 152:332/556 of O08966
Sites not aligning to the query:
- 32 L→F: Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.
- 36 Y→C: Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.
Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
30% identity, 35% coverage: 56:195/405 of query aligns to 152:287/556 of Q63089
- C155 (≠ I59) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
- C179 (≠ T83) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474.
- M212 (≠ V116) mutation to L: No change in TEA and MPP(+) uptake.
- V213 (≠ G117) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
- S214 (≠ L118) mutation to G: Decreased TEA and MPP(+) uptake.
- K215 (≠ G119) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
- G216 (= G120) mutation to A: Decreased TEA and MPP(+) uptake.
- S217 (≠ A121) mutation to G: No change in TEA and MPP(+) uptake.
- W218 (≠ L122) mutation to F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax.; mutation to Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
- V219 (≠ P123) mutation to L: No change in TEA and MPP(+) uptake.
- S220 (≠ N124) mutation to I: Decreased TEA and MPP(+) uptake.
- G221 (≠ L125) mutation to A: Decreased TEA and MPP(+) uptake.
- Y222 (≠ I126) mutation to F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
- T223 (≠ A127) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
- L224 (≠ I128) mutation to V: Decreased TEA and MPP(+) uptake.
- I225 (≠ V129) mutation to G: No change in TEA and MPP(+) uptake.
- T226 (≠ A130) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
- E227 (= E131) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
- F228 (≠ S132) mutation to I: No change in TEA and MPP(+) uptake.
- V229 (= V133) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
- S286 (≠ T194) mutation to A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550.
Sites not aligning to the query:
- 26 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
- 292 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550.
- 296 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550.
- 322 C→S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451.
- 328 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550.
- 358 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474.
- 418 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474.
- 437 C→S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474.
- 451 C→M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322.
- 470 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474.
- 474 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470.
- 475 D→E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; D→N: Decreased MPP(+) uptake.; D→R: Decreased MPP(+) uptake.
- 550 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328.
6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
26% identity, 92% coverage: 29:401/405 of query aligns to 19:390/404 of 6zguA
6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
26% identity, 92% coverage: 29:401/405 of query aligns to 19:390/404 of 6zgtA
6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
26% identity, 92% coverage: 29:401/405 of query aligns to 19:390/404 of 6zgsA
Query Sequence
>CCNA_02495 FitnessBrowser__Caulo:CCNA_02495
MTTKGRSAAGTHGGLVAVAICCLLAVFEGFDLQAAGVAAPRLAPDLGLKPEDLGWFFSIS
TFGLMVGAALGGRLSDRFGRKVTLLVSVAAFGLLSIATGLAQDLNGLLVARFLTGVGLGG
ALPNLIAIVAESVSPKLRGRAVGFLYAGLPCGGALASLVSLAGADPSDWRIVFFVGGVGP
LLAMLLAMVLLPDTPMAQVGPVGDQKSGFVEALAGEGRGLTTLLLWIAFFLALLIMYLLL
SWLPSLMIGRGLSRSDAGLIQMAFNLAGAAGSVATGWLMDHRRWRTLTILGAFGASAAAM
ATAAAAPASLAVFLIVGAALGATVSGVQSVVYGLAPGFYPARLRGTGVGAAVVVGRLGSA
AGPLLAATLIGAGGSSNQVLLALMPVIALGGLVSLLLATRPHSGD
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory