SitesBLAST
Comparing SM_b20333 FitnessBrowser__Smeli:SM_b20333 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
8ybqA Choline transporter bett - cht bound (see paper)
45% identity, 68% coverage: 52:533/706 of query aligns to 4:489/502 of 8ybqA
P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 6 papers)
40% identity, 64% coverage: 88:541/706 of query aligns to 93:548/595 of P54582
- W101 (= W96) 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 (= E130) mutation to A: Strongly decreased betaine transport.
- G149 (= G144) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M145) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G146) mutation to A: Nearly abolishes betaine transport.
- I152 (= I147) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 147:148) binding glycine betaine
- G153 (= G148) 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 (≠ Y151) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W186) mutation to C: Mildly decreased betaine transport.
- W194 (= W191) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y194) mutation to L: Nearly abolishes betaine transport.
- R210 (= R207) mutation to A: Nearly abolishes betaine transport.
- S253 (= S249) binding glycine betaine
- G301 (= G296) mutation to L: Strongly decreased betaine transport.
- N309 (= N304) mutation to A: Decreases affinity for sodium ions.
- T351 (= T343) 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 (= W354) mutation to C: Strongly decreased betaine transport.
- W366 (= W358) mutation to C: No effect on betaine transport.
- F369 (= F361) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W363) mutation to L: No effect on betaine transport.
- W373 (= W365) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 365:369) binding glycine betaine
- W374 (= W366) 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 (= W369) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F372) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F376) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R379) mutation to A: Mildly decreased betaine transport.
- R392 (= R384) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
40% identity, 64% coverage: 88:541/706 of query aligns to 37:489/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M145), G95 (= G146), D97 (≠ G148), W314 (= W365), W315 (= W366), W318 (= W369)
- binding sodium ion: A91 (= A142), M94 (= M145), G95 (= G146), F405 (= F460), T408 (= T463), S409 (= S464)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
40% identity, 64% coverage: 88:541/706 of query aligns to 37:488/508 of 3p03C
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 69% coverage: 46:529/706 of query aligns to 3:490/504 of P31553
- Y114 (≠ T159) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W186) binding (R)-carnitine
- D288 (≠ Q330) 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 (≠ D337) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ L341) 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 (≠ I346) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ SW 357:358) binding 4-(trimethylamino)butanoate
- W316 (= W358) mutation to L: Decrease in transport activity.
- W323 (= W365) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 365:366) binding (R)-carnitine
- W324 (= W366) mutation to L: Abolishes transport activity.
- Y327 (≠ W369) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 369:372) binding (R)-carnitine
- Q330 (≠ F372) mutation to L: Decrease in transport activity.
- M331 (≠ V373) binding 4-(trimethylamino)butanoate
3hfxA Crystal structure of carnitine transporter (see paper)
29% identity, 67% coverage: 57:529/706 of query aligns to 3:479/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
29% identity, 67% coverage: 57:529/706 of query aligns to 7:483/496 of 2wsxA
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 69% coverage: 44:529/706 of query aligns to 6:495/508 of 2wswA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
28% identity, 68% coverage: 49:529/706 of query aligns to 6:490/514 of B4EY22
- E111 (= E156) mutation to A: Abolishes transport activity.
- R262 (≠ N304) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W358) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V373) mutation to V: 10-fold decrease in Vmax.
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
28% identity, 67% coverage: 57:529/706 of query aligns to 6:482/495 of 4m8jA
Query Sequence
>SM_b20333 FitnessBrowser__Smeli:SM_b20333
MQNRVVSCRFTGSTARRATMPEGIRGRSHILFLVPLSRAESVGRLHQVQRFKVNLPVFVG
SVAVIALFVGIGVIAPKRAESIFSGMQTAILSGFGWLYLLSVAVFLFSMLFLAFSRYGEL
KLGPDDSEPEFRYLSWIAMLFAAGMGIGLMYFAVGEPMTHFASPPEAEPLTIAAQREAMS
VTFFHWGVHAWAIYSVVGLSLAYFGYRYNLPLTVRSGLYPLLKEGIHGPIGHVVDIFAIC
GTMFGLATSLGFGILQINSGLNYLLGIPQSIYVQLLLVTVVTAIATISVVTGVEKGVRIL
SETNLFLAVLLMLFVLVVGPTGTLMRDFVQNIGLYLDSLVLRTFNIYAYEPRPWIDSWTL
FYWAWWISWSPFVGMFIARISRGRTVREFVTAVLFVPAMFTFLWMTVFGNTAIYVDTTIA
NGELARDVKADLSVALFQFFEYLPWPAVTSTLAVLLVSIFFVTSSDSGSLVIDTIASGGE
TATPALQRIFWCSLSGIVAAVLLSTGGLTALQSATISTALPFSLVMLILVWSLFVGMRAD
LARTQSPGSLGPRAYPASGVPWQRRLAMTLSTPDRRAVEKFLQASVLPALEAVARELTRR
SRPASVGRDAETGALTLTVPAEGHRDFVYGVQMSEHKLPAFTAYDATVADVRYEARTFFS
DGSRGYDIMGMADNQIINDVLFQFERYTGFVRSPESSLLATSPEER
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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