SitesBLAST
Comparing GFF3740 FitnessBrowser__Phaeo:GFF3740 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)
31% identity, 88% coverage: 41:491/514 of query aligns to 92:528/595 of P54582
- W101 (= W60) 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 (= E91) mutation to A: Strongly decreased betaine transport.
- G149 (≠ L105) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ L106) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (≠ A107) mutation to A: Nearly abolishes betaine transport.
- I152 (≠ G108) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ GG 108:109) binding
- G153 (= G109) 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 (= F112) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W150) mutation to C: Mildly decreased betaine transport.
- W194 (= W155) mutation to L: Strongly decreased betaine transport.
- Y197 (≠ L158) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ E172) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ P215) binding
- G301 (= G262) mutation to L: Strongly decreased betaine transport.
- N309 (= N270) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ R312) 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 (= W323) mutation to C: Strongly decreased betaine transport.
- W366 (= W327) mutation to C: No effect on betaine transport.
- F369 (= F330) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W332) mutation to L: No effect on betaine transport.
- W373 (= W334) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WFMGY 334:338) binding
- W374 (≠ F335) 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 (≠ Y338) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (≠ L341) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F345) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R348) mutation to A: Mildly decreased betaine transport.
- R392 (= R353) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
31% identity, 88% coverage: 41:491/514 of query aligns to 36:469/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ L106), G95 (≠ A107), D97 (≠ G109), W314 (= W334), W315 (≠ F335), W318 (≠ Y338)
- binding sodium ion: A91 (≠ C103), M94 (≠ L106), G95 (≠ A107), F405 (= F429), T408 (= T432), S409 (≠ T433)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
32% identity, 88% coverage: 41:491/514 of query aligns to 36:468/508 of 3p03C
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
25% identity, 95% coverage: 6:492/514 of query aligns to 1:483/514 of B4EY22
- E111 (= E117) mutation to A: Abolishes transport activity.
- R262 (≠ N270) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W327) mutation to A: 2.5-fold decrease in Vmax.
- M331 (= M342) mutation to V: 10-fold decrease in Vmax.
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
27% identity, 79% coverage: 86:492/514 of query aligns to 72:475/495 of 4m8jA
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 79% coverage: 86:492/514 of query aligns to 85:488/508 of 2wswA
Sites not aligning to the query:
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 95% coverage: 6:492/514 of query aligns to 1:483/504 of P31553
- Y114 (≠ H121) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W150) binding
- D288 (≠ S296) 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 (≠ G303) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ Q307) 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 (≠ R312) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- G-W 315:316 (≠ GWW 325:327) binding
- W316 (= W327) mutation to L: Decrease in transport activity.
- W323 (= W334) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (≠ WF 334:335) binding
- W324 (≠ F335) mutation to L: Abolishes transport activity.
- Y327 (= Y338) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ YGPL 338:341) binding
- Q330 (≠ L341) mutation to L: Decrease in transport activity.
- M331 (= M342) binding
3hfxA Crystal structure of carnitine transporter (see paper)
24% identity, 91% coverage: 27:492/514 of query aligns to 11:472/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
24% identity, 91% coverage: 27:492/514 of query aligns to 15:476/496 of 2wsxA
Query Sequence
>GFF3740 FitnessBrowser__Phaeo:GFF3740
MSETSMETTPQESRINKPLFLLSGGFIALFCVAALVNLDGLSALVDWGFNIAATYFGLYW
QILLLATFLIGLVLCILPGGRAIMGGLATPEFTTFQWGSMIMCTLLAGGGVFWAAGEPIA
HFLYSPPLYGAEGGSEAAVTPAIAQSFMHWGFLAWAILGSLSTVMLMHYHYEKGLPLAPR
TLLYPVFGDKAINGPIGVIADASSIIAVVAGTVGPIGFLGLQVSYGLSDLFGIPDVFATQ
FVVIGALVALYTISAMTGLSRGIQLLSKINVILAAVLLIYVLLAGPTGFIFGSFFSGFAT
YLGNFFQMALYRGDAAVFGAPGWLGWWTVFFWGWFMGYGPLMAMFIARVSRGRSIRSIII
MLSIIAPIVTNFWFTIIGGTGIAMELAEPGTVSAAFEGFNLPAALLAITNNLPMGFLVSI
LFLILTTIFVATTGDSMSYVISATMTKGDTPSTAVRVFWGIAMGVMAVILISVGSGGVSK
LQSFIVVTAVPVSLILLPSLWDALRITLAKGKES
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