SitesBLAST
Comparing GFF1371 FitnessBrowser__Phaeo:GFF1371 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)
40% identity, 86% coverage: 78:543/545 of query aligns to 94:547/595 of P54582
- W101 (= W85) 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 (≠ D119) mutation to A: Strongly decreased betaine transport.
- G149 (= G133) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M134) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G135) mutation to A: Nearly abolishes betaine transport.
- I152 (= I136) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 136:137) binding
- G153 (= G137) 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 (= F140) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W193) mutation to C: Mildly decreased betaine transport.
- W194 (= W198) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y201) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ N214) mutation to A: Nearly abolishes betaine transport.
- S253 (= S256) binding
- G301 (= G303) mutation to L: Strongly decreased betaine transport.
- N309 (= N311) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ L349) 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 (≠ Y360) mutation to C: Strongly decreased betaine transport.
- W366 (= W364) mutation to C: No effect on betaine transport.
- F369 (= F367) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W369) mutation to L: No effect on betaine transport.
- W373 (= W371) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 371:375) binding
- W374 (= W372) 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 (= W375) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F378) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F382) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R385) mutation to A: Mildly decreased betaine transport.
- R392 (= R390) mutation to K: Moderately decreased betaine transport.
3p03C Crystal structure of betp-g153d with choline bound (see paper)
40% identity, 86% coverage: 77:543/545 of query aligns to 37:487/508 of 3p03C
4llhA Substrate bound outward-open state of the symporter betp (see paper)
40% identity, 86% coverage: 78:543/545 of query aligns to 38:488/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M134), G95 (= G135), D97 (≠ G137), W314 (= W371), W315 (= W372), W318 (= W375)
- binding sodium ion: A91 (= A131), M94 (= M134), G95 (= G135), F405 (= F463), T408 (= T466), S409 (= S467)
Sites not aligning to the query:
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 95% coverage: 28:545/545 of query aligns to 8:508/508 of 2wswA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
27% identity, 95% coverage: 26:545/545 of query aligns to 1:503/514 of B4EY22
- E111 (= E145) mutation to A: Abolishes transport activity.
- R262 (≠ N311) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W364) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V379) mutation to V: 10-fold decrease in Vmax.
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
28% identity, 82% coverage: 99:545/545 of query aligns to 59:495/495 of 4m8jA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 82% coverage: 99:545/545 of query aligns to 67:503/504 of P31553
- Y114 (≠ S148) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W193) binding
- D288 (= D337) 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 (≠ Q344) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ A348) 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 (≠ S350) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (= GW 363:364) binding
- W316 (= W364) mutation to L: Decrease in transport activity.
- W323 (= W371) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 371:372) binding
- W324 (= W372) mutation to L: Abolishes transport activity.
- Y327 (≠ W375) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 375:378) binding
- Q330 (≠ F378) mutation to L: Decrease in transport activity.
- M331 (≠ V379) binding
3hfxA Crystal structure of carnitine transporter (see paper)
28% identity, 82% coverage: 99:545/545 of query aligns to 56:492/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
28% identity, 82% coverage: 99:545/545 of query aligns to 60:496/496 of 2wsxA
Query Sequence
>GFF1371 FitnessBrowser__Phaeo:GFF1371
MTDETANQGIPAPDGEAAVIDTEYEIGQDNLEGSVGPIGFDIHNPVFMVSGISIMLFVFY
ALVLPEQAAAFFGWLRPAVTSSFDWFFLSAGNFFVLFCFFLIVSPWGKVRLGGADAAPDY
TYTGWFAMLFAAGMGIGLMFYGVSEPMSHYSTSFGGVSMGENGARTDWAPLGGAAGDSAE
SVRLGMAATIYHWGLHPWAIYAIVALSLALFSFNKGLPLTIRSAFYPIFGERVWGWTGHI
IDILAVFATLFGLATSLGFGATQANAGLNELFGVPVGATTEVVLISAITAVALISVLRGL
DGGVKILSEINMGLAFLLLIFVLLVGPTLLIITGFFDSLLAYVQYLPALSMPFGREDANY
SQGWTAFYWAWWISWSPFVGMFIARVSRGRTVREFIICVLLIPSLVCVLWMSVFGGTAIH
QVVADGYTGAQDTALELKLFKMLDQLPLAAITSFVGILLVIVFFVTSSDSGSLVIDTITA
GGKVDAPMPQRVFWCVFEGAVAIVLLLGGGLVALQAMVISTGLPFTVVLLLMCWAIVRGL
QTETR
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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