SitesBLAST
Comparing BWI76_RS27490 FitnessBrowser__Koxy:BWI76_RS27490 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 11 hits to proteins with known functional sites (download)
P02921 Melibiose permease; Melibiose carrier; Melibiose transporter; Melibiose/cation symporter; Na+ (Li+)/melibiose symporter; Thiomethylgalactoside permease II from Escherichia coli (strain K12) (see 5 papers)
26% identity, 100% coverage: 1:442/444 of query aligns to 1:450/473 of P02921
- M1 (= M1) modified: Initiator methionine, Removed
- K18 (≠ I18) mutation to C: Abolishes transporter activity.
- D19 (≠ N19) mutation to C: Abolishes transporter activity. Can bind Na(+). Large decrease in the affinity for melibiose in the presence of H(+).
- D35 (= D35) mutation to C: Abolishes transporter activity.
- R52 (= R52) mutation to C: Abolishes transporter activity.
- D55 (= D55) mutation to C: Abolishes transporter activity. Chemical restoration of the charge via the oxidation of the thiol to the sulfinic and/or sulfonic acid results in partial recovery of transporter activity. Does not bind Na(+). Binds melibiose in the presence of H(+).
- D59 (= D59) mutation to C: Loses ability to catalyze Na(+) or H(+)-coupled melibiose transport against a concentration gradient. Does not bind Na(+). Binds melibiose in the presence of H(+).
- D124 (≠ T124) mutation to C: Abolishes transporter activity. Chemical restoration of the charge via the oxidation of the thiol to the sulfinic and/or sulfonic acid results in partial recovery of transporter activity. Can bind Na(+), but structural changes induced by Na(+) are less complete and of smaller amplitude. Large decrease in the affinity for melibiose in the presence of H(+).
- K138 (≠ P138) mutation to C: Can transport melibiose.
- R139 (≠ V139) mutation to C: Can transport melibiose.
- R141 (= R141) mutation R->C,Q: Abolishes melibiose transport. Decreases affinity for melibiose.; mutation to K: Retains ion-coupled melibiose transport.
- R149 (≠ F149) mutation to C: Abolishes melibiose transport.; mutation R->K,Q: Retains ion-coupled melibiose transport.
- R199 (≠ L193) mutation to C: Does not affect transporter activity.
- E203 (≠ C197) mutation to C: Does not affect transporter activity.
P30878 Melibiose permease; Melibiose carrier; Melibiose transporter; Melibiose/cation symporter; Na+ (Li+)/melibiose symporter; Thiomethylgalactoside permease II from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
27% identity, 100% coverage: 1:442/444 of query aligns to 1:450/476 of P30878
- K18 (≠ I18) mutation to C: Loss of transporter activity.
- KD 18:19 (≠ IN 18:19) binding
- D19 (≠ N19) mutation to C: Loss of transporter activity.
- R52 (= R52) mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
- D55 (= D55) mutation to C: Alters cation selectivity. Retains a low level of H(+)-coupled melibiose transport, but retains only a weak activity with Na(+) or Li(+).
- N58 (≠ I58) mutation to C: Alters cation selectivity. Decreases H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
- D59 (= D59) mutation to C: Alters cation selectivity. Retains only a low level of H(+)-coupled melibiose binding and active transport, but Na(+) or Li(+) does not stimulate either binding or transport.
- Y120 (= Y120) mutation to C: Loss of transporter activity.
- T121 (= T121) mutation to C: Alters cation selectivity. Inhibits H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
- M123 (≠ I123) mutation to C: Does not affect transporter activity.
- D124 (≠ T124) binding ; mutation to C: Alters cation selectivity. Loss of transporter activity.
- W128 (≠ I128) binding ; mutation to C: Loss of transporter activity.
- R149 (≠ F149) binding ; mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
- K377 (= K370) mutation to C: Inhibits Na(+)- and Li(+)-coupled activity, with little effect on H(+)-coupled melibiose transport.
7l17A Crystal structure of sugar-bound melibiose permease melb (see paper)
26% identity, 99% coverage: 2:442/444 of query aligns to 1:449/453 of 7l17A
7l16A Crystal structure of sugar-bound melibiose permease melb (see paper)
26% identity, 99% coverage: 2:442/444 of query aligns to 1:449/453 of 7l16A
F1NCD6 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; GgMFSD2A from Gallus gallus (Chicken) (see paper)
21% identity, 98% coverage: 3:439/444 of query aligns to 36:506/528 of F1NCD6
- C207 (≠ M165) modified: Disulfide link with 460
- N218 (= N174) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N227 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C460 (≠ V393) modified: Disulfide link with 207
Q8NA29 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; HsMFSD2A; MFSD2a from Homo sapiens (Human) (see 6 papers)
21% identity, 99% coverage: 1:439/444 of query aligns to 39:519/543 of Q8NA29
- Q57 (≠ N19) mutation to E: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to L: Abolished lysophosphatidylcholine (LPC) transport.
- F65 (≠ L27) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- F66 (≠ L28) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- D73 (= D35) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- V81 (vs. gap) natural variant: Missing (in NEDMISBA; uncertain significance; dbSNP:rs1570238098)
- R103 (= R52) mutation R->A,K,E: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: No effect on cell sensitivity toward tunicamycin.
- D106 (= D55) mutation to A: No effect on cell sensitivity toward tunicamycin.
- D110 (= D59) mutation to A: Drastic loss of cell sensitivity toward tunicamycin. Abolished lysophosphatidylcholine (LPC) transport.
- T172 (= T121) to M: in NEDMISBA; no effect on cell membrane localization; loss of LPC transport activity; dbSNP:rs1057517688
- P177 (= P126) mutation to T: Reduced expression; no effect on cell membrane localization; decreased LPC transport activity.
- S179 (≠ I128) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057517689
- M200 (≠ F149) mutation to F: Reduced lysophosphatidylcholine (LPC) transport.
- T211 (= T160) to M: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs756467073
- C225 (≠ L177) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- N230 (≠ S182) mutation to Q: Loss of glycosylation; when associated with Q-240.
- N240 (vs. gap) mutation to Q: Loss of glycosylation; when associated with Q-230.
- V263 (vs. gap) to F: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity
- E325 (≠ G245) mutation E->A,D,Q,R: Abolished lysophosphatidylcholine (LPC) transport.
- F328 (≠ A248) mutation F->A,Y: Reduced lysophosphatidylcholine (LPC) transport.
- Y334 (= Y254) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.
- R339 (≠ G259) to H: in NEDMISBA; reduced expression; no effect on cell membrane localization; no effect on LPC transport activity; dbSNP:rs776741331; mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- F342 (≠ L262) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- L346 (≠ F266) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- I349 (≠ T269) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- M350 (≠ G270) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- S352 (≠ V272) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057519087
- I357 (≠ A277) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
- Q361 (≠ T281) mutation to W: Reduced lysophosphatidylcholine (LPC) transport.
- A404 (≠ I327) mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
- F412 (≠ M335) mutation F->I,W: Reduced lysophosphatidylcholine (LPC) transport.
- W416 (= W339) mutation W->A,F: Reduced lysophosphatidylcholine (LPC) transport.
- K449 (= K370) mutation K->A,R,Q: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: Loss of plasma membrane localization. Loss of cell sensitivity toward tunicamycin.
- Y468 (= Y389) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- C473 (≠ V393) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- P506 (≠ L426) to L: in NEDMISBA; reduced expression; no effect on cell membrane localization; loss of LPC transport activity
7mjsX Single-particle cryo-em structure of major facilitator superfamily domain containing 2a in complex with lpc-18:3 (see paper)
27% identity, 36% coverage: 3:162/444 of query aligns to 1:160/458 of 7mjsX
Sites not aligning to the query:
Q9DA75 Sodium-dependent lysophosphatidylcholine symporter 1; NLS1; Sodium-dependent LPC symporter 1; Major facilitator superfamily domain-containing protein 2A; Mfsd2a from Mus musculus (Mouse) (see 2 papers)
21% identity, 99% coverage: 1:439/444 of query aligns to 38:510/534 of Q9DA75
- Y55 (≠ I18) mutation to A: Significant reduction in LPC transport.
- Q56 (≠ N19) mutation to A: Slightly reduced LPC transport.
- F64 (≠ L27) mutation to A: Slightly increased LPC transport.
- Q67 (≠ A30) mutation to H: Abolishes LPC transport.
- S82 (≠ G45) mutation to A: No effect on LPC transport.
- F86 (≠ V49) mutation to A: Slightly reduced LPC transport.
- R89 (= R52) mutation to A: No effect on LPC transport.
- D92 (= D55) mutation to A: Significant reduction in LPC transport. Abolishes LPC transport; when associated with A-96.
- T95 (≠ I58) mutation to A: Significant reduction in LPC transport.
- D96 (= D59) mutation to A: Abolishes LPC transport. Abolishes LPC transport; when associated with A-92.
- E159 (≠ T117) mutation to A: Slightly reduced LPC transport.
- T163 (= T121) mutation to A: Slightly reduced LPC transport.; mutation to M: Abolishes LPC transport.
- H166 (≠ T124) mutation to A: Abolishes LPC transport.
- P168 (= P126) mutation to T: Significant reduction in LPC transport.
- S170 (≠ I128) mutation to L: Significant reduction in LPC transport.
- R190 (= R148) mutation to A: Abolishes LPC transport.
- E194 (≠ T152) mutation to A: Significant reduction in LPC transport.
- T202 (= T160) mutation to A: Slightly increased LPC transport.; mutation to F: Significant reduction in LPC transport.; mutation to M: Significant reduction in LPC transport.
- Q207 (vs. gap) mutation to A: Slightly reduced LPC transport.
- C216 (≠ M165) modified: Disulfide link with 464; mutation to A: Significant reduction in LPC transport.
- A254 (≠ G187) mutation to F: Abolishes LPC transport.
- F305 (≠ I234) mutation to A: Significant reduction in LPC transport.
- S309 (≠ M238) mutation to A: Significant reduction in LPC transport.
- R330 (≠ G259) mutation to H: No effect on LPC transport.
- Q334 (≠ I263) mutation to A: Slightly reduced LPC transport.
- N335 (≠ S264) mutation to A: Significant reduction in LPC transport.
- S343 (≠ V272) mutation to L: Significant reduction in LPC transport.
- F403 (≠ M335) mutation to A: Significant reduction in LPC transport.
- P406 (≠ F338) mutation to H: Significant reduction in LPC transport.
- W407 (= W339) mutation to A: Significant reduction in LPC transport.
- T439 (≠ Q369) mutation to A: No effect on LPC transport.
- K440 (= K370) mutation to A: Abolishes LPC transport.
- T451 (≠ G381) mutation to A: Slightly reduced LPC transport.
- D455 (≠ S385) mutation to A: Slightly reduced LPC transport.
- R461 (≠ A391) mutation to A: Slightly reduced LPC transport.
- C464 (≠ V393) modified: Disulfide link with 216; mutation to A: Significant reduction in LPC transport.
- P497 (≠ L426) mutation to L: Abolishes LPC transport.
8d2sA Zebrafish mfsd2a isoform b in inward open ligand bound conformation (see paper)
26% identity, 33% coverage: 2:148/444 of query aligns to 2:148/475 of 8d2sA
Sites not aligning to the query:
- binding [(2~{R})-2-oxidanyl-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propyl] (9~{Z},12~{Z},15~{Z})-octadeca-9,12,15-trienoate: 149, 150, 152, 153, 156, 157, 280, 302, 305, 306, 306, 307, 309, 356, 364, 368, 368, 389, 389, 393, 393, 400, 401
Q3T9M1 Sphingosine-1-phosphate transporter MFSD2B; Major facilitator superfamily domain-containing protein 2B; mMfsd2b from Mus musculus (Mouse) (see 2 papers)
27% identity, 39% coverage: 2:175/444 of query aligns to 28:200/494 of Q3T9M1
- D85 (= D59) mutation to A: Decreased sphingosine-1-phosphate transport.
- T147 (= T121) mutation to A: Decreased export of sphingosine-1-phosphate.
Sites not aligning to the query:
- 413 K→A: Decreased sphingosine-1-phosphate transport.
A6NFX1 Sphingosine-1-phosphate transporter MFSD2B; Major facilitator superfamily domain-containing protein 2B; hMfsd2b from Homo sapiens (Human) (see paper)
21% identity, 90% coverage: 2:400/444 of query aligns to 38:453/504 of A6NFX1
- D95 (= D59) mutation to A: Abolishes export of sphingosine-1-phosphate.
- T157 (= T121) mutation to A: Abolishes export of sphingosine-1-phosphate.
- K423 (= K370) mutation to A: Does not affect export of sphingosine-1-phosphate.
Query Sequence
>BWI76_RS27490 FitnessBrowser__Koxy:BWI76_RS27490
MKLSIVEKIGFGAGDMAINVVIIAMQLLLAYFYTDIYGLSAADVGVLFVVVRMIDAIIDP
AMGVLTDKLNTRWGRYRPWLLWFAIPFGFAVYLMFITPDMVYMAKLAWAYGTYILMTLVY
TAITIPYISMIGVITSDPVERLSANGYRFVMTKIAAFLVTIVVPMLAVWLGQGNKALGYQ
FSMGLMGAMGALLFIFCFLTTRERSEPEITSLSVGKQFKYLLRNDQWIILGVVILLLMCG
YVIRGSVAAYYAKYYLNGGDSLISPFLTTGVVASILAMIATTWITKFWDKIKMFRYTQII
TFVLSAMMYFFVGRENLILAFTFYFLINFFCDMQMPVFWSSIAEAVDYGEKKTGLRVSGL
AFGGILFFQKFGMGIAGGVLGFLLSHFGYQADVEQSARSLTGIALMMTLIPALFHLAVGL
LMKKYLINNEYYRDIQLALAQKQA
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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