SitesBLAST
Comparing GFF3313 FitnessBrowser__Phaeo:GFF3313 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)
32% identity, 49% coverage: 33:330/604 of query aligns to 68:348/595 of P54582
- W101 (≠ A66) 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 (= E101) mutation to A: Strongly decreased betaine transport.
- G149 (= G115) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ L116) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G117) mutation to A: Nearly abolishes betaine transport.
- I152 (≠ V118) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ VG 118:119) binding
- G153 (= G119) 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 (≠ V122) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (≠ Y162) mutation to C: Mildly decreased betaine transport.
- W194 (= W167) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y170) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ T183) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ T225) binding
- G301 (= G283) mutation to L: Strongly decreased betaine transport.
- N309 (= N291) mutation to A: Decreases affinity for sodium ions.
Sites not aligning to the query:
- 351 T→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.
- 362 W→C: Strongly decreased betaine transport.
- 366 W→C: No effect on betaine transport.
- 369 F→G: Decreases affinity for glycine betaine. Decreases betaine transport.
- 371 W→L: No effect on betaine transport.
- 373 W→A: Strongly decreases affinity for glycine betaine and betaine transport.
- 373:377 binding
- 374 W→A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; W→L: No effect on betaine transport.
- 377 W→A: Abolishes betaine transport.; W→L: Nearly abolishes betaine transport.
- 380 F→A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- 384 F→A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- 387 R→A: Mildly decreased betaine transport.
- 392 R→K: Moderately decreased betaine transport.
3p03C Crystal structure of betp-g153d with choline bound (see paper)
32% identity, 49% coverage: 33:330/604 of query aligns to 12:288/508 of 3p03C
Sites not aligning to the query:
4llhA Substrate bound outward-open state of the symporter betp (see paper)
33% identity, 49% coverage: 33:330/604 of query aligns to 12:289/524 of 4llhA
Sites not aligning to the query:
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
26% identity, 91% coverage: 51:598/604 of query aligns to 23:505/514 of B4EY22
- E111 (= E127) mutation to A: Abolishes transport activity.
- R262 (≠ N291) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W407) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V422) mutation to V: 10-fold decrease in Vmax.
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
25% identity, 91% coverage: 46:592/604 of query aligns to 23:501/508 of 2wswA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
25% identity, 91% coverage: 46:592/604 of query aligns to 10:488/495 of 4m8jA
3hfxA Crystal structure of carnitine transporter (see paper)
25% identity, 91% coverage: 46:597/604 of query aligns to 7:493/493 of 3hfxA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
25% identity, 91% coverage: 46:597/604 of query aligns to 18:504/504 of P31553
- Y114 (≠ G130) binding ; mutation to L: Small decrease in transport activity.
- W142 (≠ Y162) binding
- D288 (≠ S317) 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 (≠ L324) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ Q328) 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 (≠ G335) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- G----------------------------W 315:316 (≠ GLPASAAALDANAVYAAGEPGRQFGWQAGW 378:407) binding
- W316 (= W407) mutation to L: Decrease in transport activity.
- W323 (= W414) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 414:415) binding
- W324 (= W415) mutation to L: Abolishes transport activity.
- Y327 (≠ F418) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ FSPF 418:421) binding
- Q330 (≠ F421) mutation to L: Decrease in transport activity.
- M331 (≠ V422) binding
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
25% identity, 91% coverage: 46:592/604 of query aligns to 11:489/496 of 2wsxA
Query Sequence
>GFF3313 FitnessBrowser__Phaeo:GFF3313
MSIKPPFTELEIETAPSGFYEGHSLPIALISKIIMTTLVLWALVWPSKASGILSWVNSEL
LNGFNAFYIVSVGAFAFFLFVLAILPATGSKKLGPADAAPEFSNFSWFSMMFGAGLGVGL
MVFATAEPLGLWGSNPVVLSGAVAANSEEAVQSAYRYTFLHYGFHAWAIYVLTGLSLAYY
AYTRDMPLTIRSALTPLLGKAANGFVGHLVDVLGVVATILGVSVTIGFGVSQFVDGVYAV
SGMEWLMNGDTEAPKPSTVGLLSALFVIMGLSILSAVSGVGRGIKYLSNLNLVLSVILLL
TFVFFGSFFFAMTKFGSGLVDYILHFTQMSFGAYGPQSAEAFAAALPDAAQALPAEDLST
VYGSATSPWGSLGGFTEGLPASAAALDANAVYAAGEPGRQFGWQAGWTTFYWAWWIAFSP
FVGLFLARISKGRTVREFILGCVIAPAIVCFLWMTILGGTAIDLELNGGAAGSIIGATNT
AKLFATLEQMISGGFLSAITVMCVVLIMTFLVTSADSGILVMNTIMSGGEQETGIKHRII
WGLILTSVIGALIIAGNSGTASNPFGALQNAMIIGALPFTIVMVFMMISLAKALYRDSLR
AKAD
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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