SitesBLAST
Comparing Pf1N1B4_2419 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2419 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)
56% identity, 75% coverage: 13:514/668 of query aligns to 2:498/502 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)
35% identity, 75% coverage: 56:557/668 of query aligns to 98:591/595 of P54582
- W101 (= W59) 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 (≠ D93) mutation to A: Strongly decreased betaine transport.
- G149 (= G107) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ I108) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G109) mutation to A: Nearly abolishes betaine transport.
- I152 (= I110) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ IS 110:111) binding glycine betaine
- G153 (≠ S111) 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 (≠ Y114) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W149) mutation to C: Mildly decreased betaine transport.
- W194 (= W154) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y157) mutation to L: Nearly abolishes betaine transport.
- R210 (= R170) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ N213) binding glycine betaine
- G301 (= G260) mutation to L: Strongly decreased betaine transport.
- N309 (= N268) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ S317) 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 (= WWISW 334:338) binding glycine betaine
- W374 (= W335) 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 (= W338) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F341) 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)
35% identity, 75% coverage: 56:553/668 of query aligns to 42:523/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I108), G95 (= G109), D97 (≠ S111), W314 (= W334), W315 (= W335), W318 (= W338)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (= R525), R499 (≠ G529)
- binding sodium ion: A91 (≠ S105), M94 (≠ I108), G95 (= G109), F405 (≠ L429), T408 (= T432), S409 (≠ P433)
3p03C Crystal structure of betp-g153d with choline bound (see paper)
36% identity, 71% coverage: 56:528/668 of query aligns to 42:505/508 of 3p03C
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
28% identity, 66% coverage: 56:493/668 of query aligns to 59:487/508 of 2wswA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 76% coverage: 7:512/668 of query aligns to 1:501/504 of P31553
- Y114 (≠ D122) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W149) binding (R)-carnitine
- D288 (≠ Q294) 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 (≠ K306) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ L310) 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 (≠ G315) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ LW 326:327) binding 4-(trimethylamino)butanoate
- W316 (= W327) mutation to L: Decrease in transport activity.
- W323 (= W334) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 334:335) binding (R)-carnitine
- W324 (= W335) mutation to L: Abolishes transport activity.
- Y327 (≠ W338) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WAPF 338:341) binding (R)-carnitine
- Q330 (≠ F341) mutation to L: Decrease in transport activity.
- M331 (≠ V342) binding 4-(trimethylamino)butanoate
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
28% identity, 66% coverage: 56:493/668 of query aligns to 46:474/495 of 4m8jA
3hfxA Crystal structure of carnitine transporter (see paper)
27% identity, 68% coverage: 56:512/668 of query aligns to 43:490/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
27% identity, 68% coverage: 56:512/668 of query aligns to 47:494/496 of 2wsxA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
28% identity, 66% coverage: 56:493/668 of query aligns to 54:482/514 of B4EY22
- E111 (= E119) mutation to A: Abolishes transport activity.
- R262 (≠ N268) 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 (≠ V342) mutation to V: 10-fold decrease in Vmax.
Query Sequence
>Pf1N1B4_2419 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2419
MSSASLIKTPPEKVTVNGWVFYTSTALILLLTAILIIAPQEAGRMLGIAQAWLSRSFGWY
YMVVIAAYLVFVVGLAFSSYGKLKLGSKDDTPDFSYGAWAGMLFSSGIGISLLYFGASEP
LDHYFNPPEGVAGSNLAARQAVQLTFLHWGLHGWAIYALVGLAVAYFAYRHNQPLALRSA
LYPLVGERWVKGAAGHAVDGFGMFVTLLGLVTNLGIGSLQVSSGLENLFGMEHSNTNLLI
VIIVMSTVATIAAVSGVENGIRRLSNLNIVLFSGLLIFVLLFGPTLHLLNGFVQNIGDYL
NGVVLKTFDLYVYEGDSEKSDRWLGLWTLFYWAWWISWAPFVGMFIARISRGRTVRELVA
GVLLIPLGFTLAWLSIFGNSALDLVMNHGAVELGKTALEQPSMAIYQLLEHYPASKIVIG
VSIFVGFVLFLTPADSGAVMMANLSCKGGNVDEDAPHWLRIFWSAVITLVTIGLLFAGNF
EAMQTMVVLAGLPFSVVLVFFMFGLHKAMRQDVQIEQEQAELAARGRRGFSERLTQLDLQ
PNQSIVQRFMDKRVSPALEDAAVQLRAQGLDVQTLLGKAKRCMGVRIEMEEGNPFVYEVS
LDGYLAAASDTVSAESADEPRARYYRAEVYLHNGSQDYDLMGFTQDQITRDVLDQFESHR
QLLGRVYS
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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