SitesBLAST
Comparing GFF2787 FitnessBrowser__Marino:GFF2787 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 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)
31% identity, 86% coverage: 48:474/494 of query aligns to 112:534/595 of P54582
- E135 (= E71) mutation to A: Strongly decreased betaine transport.
- G149 (≠ L85) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ L86) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (≠ A87) mutation to A: Nearly abolishes betaine transport.
- I152 (≠ G88) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ GG 88:89) binding
- G153 (= G89) 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 (= F92) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W130) mutation to C: Mildly decreased betaine transport.
- W194 (= W135) mutation to L: Strongly decreased betaine transport.
- Y197 (≠ L138) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ G152) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ P195) binding
- G301 (= G242) mutation to L: Strongly decreased betaine transport.
- N309 (= N250) mutation to A: Decreases affinity for sodium ions.
- T351 (vs. gap) 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 (= W300) mutation to C: Strongly decreased betaine transport.
- W366 (= W304) mutation to C: No effect on betaine transport.
- F369 (= F307) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (≠ F309) mutation to L: No effect on betaine transport.
- W373 (= W311) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WFIGY 311:315) binding
- W374 (≠ F312) 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 (≠ Y315) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (≠ L318) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F322) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R325) mutation to A: Mildly decreased betaine transport.
- R392 (= R330) mutation to K: Moderately decreased betaine transport.
Sites not aligning to the query:
- 101 W→A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
31% identity, 87% coverage: 45:474/494 of query aligns to 53:475/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ L86), G95 (≠ A87), D97 (≠ G89), W314 (= W311), W315 (≠ F312), W318 (≠ Y315)
- binding sodium ion: A91 (≠ C83), M94 (≠ L86), G95 (≠ A87), F405 (= F406), T408 (= T409), S409 (≠ T410)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
31% identity, 87% coverage: 45:474/494 of query aligns to 53:474/508 of 3p03C
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
26% identity, 89% coverage: 14:451/494 of query aligns to 21:459/495 of 4m8jA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
25% identity, 89% coverage: 14:451/494 of query aligns to 29:467/514 of B4EY22
- E111 (= E97) mutation to A: Abolishes transport activity.
- R262 (≠ N250) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W304) mutation to A: 2.5-fold decrease in Vmax.
- M331 (= M319) mutation to V: 10-fold decrease in Vmax.
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
26% identity, 89% coverage: 14:451/494 of query aligns to 34:472/508 of 2wswA
3hfxA Crystal structure of carnitine transporter (see paper)
26% identity, 88% coverage: 19:451/494 of query aligns to 34:456/493 of 3hfxA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 88% coverage: 19:451/494 of query aligns to 45:467/504 of P31553
- Y114 (≠ H101) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W130) binding
- D288 (≠ Q276) 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 (≠ T283) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ A287) 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 (= T292) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ WW 303:304) binding
- W316 (= W304) mutation to L: Decrease in transport activity.
- W323 (= W311) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (≠ WF 311:312) binding
- W324 (≠ F312) mutation to L: Abolishes transport activity.
- Y327 (= Y315) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ YTPL 315:318) binding
- Q330 (≠ L318) mutation to L: Decrease in transport activity.
- M331 (= M319) binding
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 88% coverage: 19:451/494 of query aligns to 38:460/496 of 2wsxA
Sites not aligning to the query:
Query Sequence
>GFF2787 FitnessBrowser__Marino:GFF2787
MLTIGFILLFVGASIVDSGYVADLIGAGFAWTATYLGSFFQVLLLLTFFIAMGTALSRAG
TARIGGLDRPEIGRFRWLSMIMCTLLAGGGVFFAAGEPVYHFVVTPPAFDTEAGSASAVA
PAMAQSFTHWGFLAWAVLGSLTALVLTRAHYGQGKPLQPRTLLYPVFGEKVIQGRLGGVI
DAFCVIAVVAGTVGPIGFLATQMSFGLHELFGVPDGYGTQLTVLVVLAGVYMTSAMTGLH
KGIQLLSRFNVILALVIAGVIFVFGPTLFLANTYTQSMGEYVTSFFAMATMTAETAPAWW
MKWWTVFFFAWFIGYTPLMAVFVARISRGRTVREMVLAVAVLAPIATTIWFTLLGGSGIY
HQLAGTFDLTEALNNFRFDVATLTVAQALPGGTWMAAAILLLTTIFVATTGDSMSYSIAM
VGAGHDEPNPWIRVFWGGAMALMAAILLYMGAGQIGVLQQFIVLTAIPVSLIILPSLWTG
PKAALAMAREQGLV
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