SitesBLAST
Comparing Echvi_0794 FitnessBrowser__Cola:Echvi_0794 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
38% identity, 98% coverage: 7:522/529 of query aligns to 53:585/595 of P54582
- W101 (= W51) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
- E135 (= E85) mutation to A: Strongly decreased betaine transport.
- G149 (= G99) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M100) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G101) mutation to A: Nearly abolishes betaine transport.
- I152 (= I102) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 102:103) binding
- G153 (= G103) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
- F156 (= F106) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W141) mutation to C: Mildly decreased betaine transport.
- W194 (= W146) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y149) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ N162) mutation to A: Nearly abolishes betaine transport.
- S253 (= S204) binding
- G301 (= G251) mutation to L: Strongly decreased betaine transport.
- N309 (= N259) mutation to A: Decreases affinity for sodium ions.
- T351 (= T301) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
- W362 (= W309) mutation to C: Strongly decreased betaine transport.
- W366 (= W313) mutation to C: No effect on betaine transport.
- F369 (= F316) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W318) mutation to L: No effect on betaine transport.
- W373 (= W320) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WWVSW 320:324) binding
- W374 (= W321) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
- W377 (= W324) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F327) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F331) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R334) mutation to A: Mildly decreased betaine transport.
- R392 (= R339) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
40% identity, 90% coverage: 45:522/529 of query aligns to 39:523/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M100), G95 (= G101), D97 (≠ G103), W314 (= W320), W315 (= W321), W318 (= W324)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (≠ K494), R499 (= R498)
- binding sodium ion: A91 (≠ S97), M94 (= M100), G95 (= G101), F405 (= F415), T408 (= T418), S409 (= S419)
3p03C Crystal structure of betp-g153d with choline bound (see paper)
41% identity, 87% coverage: 45:505/529 of query aligns to 39:497/508 of 3p03C
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
29% identity, 92% coverage: 3:490/529 of query aligns to 10:501/508 of 2wswA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
29% identity, 91% coverage: 8:490/529 of query aligns to 2:488/495 of 4m8jA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
28% identity, 96% coverage: 3:508/529 of query aligns to 5:514/514 of B4EY22
- E111 (= E111) mutation to A: Abolishes transport activity.
- R262 (≠ N259) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W313) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V328) mutation to V: 10-fold decrease in Vmax.
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 93% coverage: 3:495/529 of query aligns to 5:501/504 of P31553
- Y114 (≠ S114) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W141) binding
- D288 (≠ Q285) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
- M295 (≠ N292) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ A296) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
- T304 (= T301) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ TW 312:313) binding
- W316 (= W313) mutation to L: Decrease in transport activity.
- W323 (= W320) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 320:321) binding
- W324 (= W321) mutation to L: Abolishes transport activity.
- Y327 (≠ W324) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 324:327) binding
- Q330 (≠ F327) mutation to L: Decrease in transport activity.
- M331 (≠ V328) binding
3hfxA Crystal structure of carnitine transporter (see paper)
28% identity, 91% coverage: 12:495/529 of query aligns to 3:490/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
28% identity, 92% coverage: 8:495/529 of query aligns to 3:494/496 of 2wsxA
Query Sequence
>Echvi_0794 FitnessBrowser__Cola:Echvi_0794
MLKKYFDVHAPVFWPASVLIIIFIAITLIVGEPMEKAFDAIKFFITDKTGWLFIIAINIF
IVFCFYLAFSKYGTIRLGGKDAETEFSTSAWFAMLFSAGMGIGLLFWGVAEPVSHYAKPP
YGEPFSIGSAQRGMNLTFLHWGFHAWAIYAVVALALAFFTFNRKLPLTIRSIFYPILGDR
IHGWIGDVIDVMAVLATLFGLATSLGFGVRQINGGLNYLFDVDISVTVQVLLISGITLMA
TASVFSGLDKGVRVLSEWNVRIAAALLIFVILAGPTVFIFRGFVQNLGNYLNQFIAVSTW
TEAYRDNEWQGTWTIFYWAWWVSWSPFVGMFIARISKGRTIREFILGVLLVPALLTFFWL
TAMGGSAIFMDMQNETHQFAKDIIKDESTALFVFLHEFPLSTLGSGIGVLLVMSFFVTSS
DSGSLVIDSITAGGKLDAPVGQRIFWALAEGTVAAVLLIGGGLTALQTATITTGLPFLIV
LLIMCFSLFRGLQKEHARKEALKQDINRKNYEKNLAEIIKKNLPKDSPK
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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