SitesBLAST
Comparing GFF3707 FitnessBrowser__psRCH2:GFF3707 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)
36% identity, 81% coverage: 5:535/657 of query aligns to 52:584/595 of P54582
- W101 (= W54) 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 (≠ D88) mutation to A: Strongly decreased betaine transport.
- G149 (= G102) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M103) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G104) mutation to A: Nearly abolishes betaine transport.
- I152 (= I105) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 105:106) binding
- G153 (= G106) 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 (= F109) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W144) mutation to C: Mildly decreased betaine transport.
- W194 (= W149) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y152) mutation to L: Nearly abolishes betaine transport.
- R210 (= R165) mutation to A: Nearly abolishes betaine transport.
- S253 (= S207) binding
- G301 (= G254) mutation to L: Strongly decreased betaine transport.
- N309 (= N262) 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 (= W312) mutation to C: Strongly decreased betaine transport.
- W366 (= W316) mutation to C: No effect on betaine transport.
- F369 (= F319) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W321) mutation to L: No effect on betaine transport.
- W373 (= W323) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WWLAW 323:327) binding
- W374 (= W324) 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 (= W327) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F330) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F334) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R337) mutation to A: Mildly decreased betaine transport.
- R392 (= R342) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
38% identity, 76% coverage: 11:507/657 of query aligns to 2:497/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M103), G95 (= G104), D97 (≠ G106), W314 (= W323), W315 (= W324), W318 (= W327)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (= R505)
- binding sodium ion: A91 (≠ S100), M94 (= M103), G95 (= G104), F405 (= F418), T408 (= T421), S409 (= S422)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
37% identity, 76% coverage: 11:507/657 of query aligns to 2:496/508 of 3p03C
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
30% identity, 62% coverage: 70:479/657 of query aligns to 74:487/508 of 2wswA
Sites not aligning to the query:
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
30% identity, 62% coverage: 70:479/657 of query aligns to 69:482/514 of B4EY22
- E111 (= E114) mutation to A: Abolishes transport activity.
- R262 (≠ N262) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W316) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V331) mutation to V: 10-fold decrease in Vmax.
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
29% identity, 62% coverage: 70:479/657 of query aligns to 61:474/495 of 4m8jA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
27% identity, 72% coverage: 4:479/657 of query aligns to 3:482/504 of P31553
- Y114 (≠ M117) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W144) binding
- D288 (≠ Q288) 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 (≠ S295) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ D299) 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 (≠ L304) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (= GW 315:316) binding
- W316 (= W316) mutation to L: Decrease in transport activity.
- W323 (= W323) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 323:324) binding
- W324 (= W324) mutation to L: Abolishes transport activity.
- Y327 (≠ W327) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 327:330) binding
- Q330 (≠ F330) mutation to L: Decrease in transport activity.
- M331 (≠ V331) binding
3hfxA Crystal structure of carnitine transporter (see paper)
29% identity, 62% coverage: 70:479/657 of query aligns to 58:471/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
29% identity, 62% coverage: 70:479/657 of query aligns to 62:475/496 of 2wsxA
Query Sequence
>GFF3707 FitnessBrowser__psRCH2:GFF3707
MEAKQPSSSHLNAPVFYGSAVIILALVIYSVAFQSHAQTLFGDTQAWIIANVSWLYILAV
ALILLMVVLLAFSRYGDIKLGPDHSEPDYSALTWFAMLFSAGMGIGLMFFGVAEPVMHFL
SPPTGEGGTTLAAREAMKITFFHWGLHAWSIYAIVAMILAYFAYRHGLPLTLRSALYPLI
GERIYGPIGHAVDIFAIIGTVLGVATSLGLGVTQINTGLNHLYGLPISVPVQIGLIIATT
LLATVSVVTGLDKGVRRLSELNLTLAALLLLMVLVAGPTVFILQTFVQNTGSYLSDIVDK
TFNLYAYEPNDWIGGWTLFYWGWWLAWSPFVGLFIARISRGRTIREFVAGVLLVPTAFTL
LWMTVFGDTAIHMILWEHVTSLGDAIEQDSSLALFAFLEHFPFSALISLIAIIMVVVFFV
TSADSGALVVDMLASGGKQGTPVWQRIFWAMSMGGVAIALLLADGLTALQTATIASALPF
TIALLCSMWGLLKALRLDATKQGLRYQALSTSPSAPRTAGGWQRRLRTLMLFPRRAHVVR
FITEVVRPAYEDIAEEMRKQGYVVEISEGEDRRLRFEITHDGEPDFIYEVRPRAYAMPSF
VATSDDDEREERKYFRAEVHLKEGGQDYDVMGWSREDVISDILGQYEKHMHFLHMVR
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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