SitesBLAST
Comparing N515DRAFT_2416 FitnessBrowser__Dyella79:N515DRAFT_2416 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)
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)
29% identity, 96% coverage: 19:465/466 of query aligns to 3:455/476 of P30878
- K18 (≠ G34) mutation to C: Loss of transporter activity.
- KD 18:19 (≠ GN 34:35) binding
- D19 (≠ N35) mutation to C: Loss of transporter activity.
- R52 (= R68) mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
- D55 (= D71) 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 (≠ A74) mutation to C: Alters cation selectivity. Decreases H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
- D59 (= D75) 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 (= Y136) mutation to C: Loss of transporter activity.
- T121 (= T137) mutation to C: Alters cation selectivity. Inhibits H(+)- and Na(+)-coupled activity, with little effect on Li(+)-coupled melibiose transport.
- M123 (≠ I139) mutation to C: Does not affect transporter activity.
- D124 (≠ N140) binding ; mutation to C: Alters cation selectivity. Loss of transporter activity.
- W128 (≠ C144) binding ; mutation to C: Loss of transporter activity.
- R149 (= R164) binding ; mutation to C: Retains weak activity with Na(+), Li(+) or H(+).
- K377 (= K388) 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)
28% identity, 95% coverage: 19:461/466 of query aligns to 2:450/453 of 7l17A
7l16A Crystal structure of sugar-bound melibiose permease melb (see paper)
28% identity, 95% coverage: 19:461/466 of query aligns to 2:450/453 of 7l16A
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)
28% identity, 96% coverage: 19:465/466 of query aligns to 3:455/473 of P02921
- K18 (≠ G34) mutation to C: Abolishes transporter activity.
- D19 (≠ N35) mutation to C: Abolishes transporter activity. Can bind Na(+). Large decrease in the affinity for melibiose in the presence of H(+).
- D35 (= D51) mutation to C: Abolishes transporter activity.
- R52 (= R68) mutation to C: Abolishes transporter activity.
- D55 (= D71) 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 (= D75) 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 (≠ N140) 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 (≠ R154) mutation to C: Can transport melibiose.
- R139 (= R155) mutation to C: Can transport melibiose.
- R141 (≠ V157) mutation R->C,Q: Abolishes melibiose transport. Decreases affinity for melibiose.; mutation to K: Retains ion-coupled melibiose transport.
- R149 (= R164) mutation to C: Abolishes melibiose transport.; mutation R->K,Q: Retains ion-coupled melibiose transport.
- R199 (= R225) mutation to C: Does not affect transporter activity.
- E203 (= E227) mutation to C: Does not affect transporter activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8d2sA Zebrafish mfsd2a isoform b in inward open ligand bound conformation (see paper)
25% identity, 32% coverage: 17:164/466 of query aligns to 1:148/475 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
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)
23% identity, 42% coverage: 11:207/466 of query aligns to 32:230/534 of Q9DA75
- Y55 (≠ G34) mutation to A: Significant reduction in LPC transport.
- Q56 (≠ N35) mutation to A: Slightly reduced LPC transport.
- F64 (≠ N43) mutation to A: Slightly increased LPC transport.
- Q67 (≠ N46) mutation to H: Abolishes LPC transport.
- S82 (≠ G61) mutation to A: No effect on LPC transport.
- F86 (≠ L65) mutation to A: Slightly reduced LPC transport.
- R89 (= R68) mutation to A: No effect on LPC transport.
- D92 (= D71) mutation to A: Significant reduction in LPC transport. Abolishes LPC transport; when associated with A-96.
- T95 (≠ A74) mutation to A: Significant reduction in LPC transport.
- D96 (= D75) mutation to A: Abolishes LPC transport. Abolishes LPC transport; when associated with A-92.
- E159 (≠ S133) mutation to A: Slightly reduced LPC transport.
- T163 (= T137) mutation to A: Slightly reduced LPC transport.; mutation to M: Abolishes LPC transport.
- H166 (≠ N140) mutation to A: Abolishes LPC transport.
- P168 (= P142) mutation to T: Significant reduction in LPC transport.
- S170 (≠ C144) mutation to L: Significant reduction in LPC transport.
- R190 (= R164) mutation to A: Abolishes LPC transport.
- E194 (≠ C168) mutation to A: Significant reduction in LPC transport.
- T202 (≠ S176) mutation to A: Slightly increased LPC transport.; mutation to F: Significant reduction in LPC transport.; mutation to M: Significant reduction in LPC transport.
- Q207 (≠ W181) mutation to A: Slightly reduced LPC transport.
- C216 (≠ A193) modified: Disulfide link with 464; mutation to A: Significant reduction in LPC transport.
Sites not aligning to the query:
- 254 A→F: Abolishes LPC transport.
- 305 F→A: Significant reduction in LPC transport.
- 309 S→A: Significant reduction in LPC transport.
- 330 R→H: No effect on LPC transport.
- 334 Q→A: Slightly reduced LPC transport.
- 335 N→A: Significant reduction in LPC transport.
- 343 S→L: Significant reduction in LPC transport.
- 403 F→A: Significant reduction in LPC transport.
- 406 P→H: Significant reduction in LPC transport.
- 407 W→A: Significant reduction in LPC transport.
- 439 T→A: No effect on LPC transport.
- 440 K→A: Abolishes LPC transport.
- 451 T→A: Slightly reduced LPC transport.
- 455 D→A: Slightly reduced LPC transport.
- 461 R→A: Slightly reduced LPC transport.
- 464 modified: Disulfide link with 216; C→A: Significant reduction in LPC transport.
- 497 P→L: Abolishes LPC transport.
7mjsX Single-particle cryo-em structure of major facilitator superfamily domain containing 2a in complex with lpc-18:3 (see paper)
22% identity, 85% coverage: 19:413/466 of query aligns to 1:415/458 of 7mjsX
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, 95% coverage: 19:459/466 of query aligns to 36:508/528 of F1NCD6
- C207 (≠ V175) modified: Disulfide link with 460
- N218 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N227 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C460 (≠ V411) 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)
22% identity, 95% coverage: 17:458/466 of query aligns to 39:520/543 of Q8NA29
- Q57 (≠ N35) mutation to E: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to L: Abolished lysophosphatidylcholine (LPC) transport.
- F65 (≠ N43) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- F66 (= F44) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- D73 (= D51) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- V81 (vs. gap) natural variant: Missing (in NEDMISBA; uncertain significance; dbSNP:rs1570238098)
- R103 (= R68) mutation R->A,K,E: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: No effect on cell sensitivity toward tunicamycin.
- D106 (= D71) mutation to A: No effect on cell sensitivity toward tunicamycin.
- D110 (= D75) mutation to A: Drastic loss of cell sensitivity toward tunicamycin. Abolished lysophosphatidylcholine (LPC) transport.
- T172 (= T137) to M: in NEDMISBA; no effect on cell membrane localization; loss of LPC transport activity; dbSNP:rs1057517688
- P177 (= P142) mutation to T: Reduced expression; no effect on cell membrane localization; decreased LPC transport activity.
- S179 (≠ C144) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057517689
- M200 (≠ F165) mutation to F: Reduced lysophosphatidylcholine (LPC) transport.
- T211 (vs. gap) to M: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs756467073
- C225 (vs. gap) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- N230 (≠ V175) mutation to Q: Loss of glycosylation; when associated with Q-240.
- N240 (≠ Q185) mutation to Q: Loss of glycosylation; when associated with Q-230.
- V263 (≠ A208) to F: in NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity
- E325 (≠ G262) mutation E->A,D,Q,R: Abolished lysophosphatidylcholine (LPC) transport.
- F328 (≠ Y265) mutation F->A,Y: Reduced lysophosphatidylcholine (LPC) transport.
- Y334 (= Y271) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.
- R339 (≠ D276) 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 (≠ Y279) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- L346 (≠ F283) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- I349 (≠ A291) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- M350 (≠ I292) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- S352 (≠ G294) to L: in NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity; dbSNP:rs1057519087
- I357 (≠ G299) mutation to A: Does not affect lysophosphatidylcholine (LPC) transport.; mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
- Q361 (≠ R303) mutation to W: Reduced lysophosphatidylcholine (LPC) transport.
- A404 (≠ S345) mutation to W: Abolished lysophosphatidylcholine (LPC) transport.
- F412 (≠ L353) mutation F->I,W: Reduced lysophosphatidylcholine (LPC) transport.
- W416 (≠ F357) mutation W->A,F: Reduced lysophosphatidylcholine (LPC) transport.
- K449 (= K388) mutation K->A,R,Q: Reduced lysophosphatidylcholine (LPC) transport.; mutation to A: Loss of plasma membrane localization. Loss of cell sensitivity toward tunicamycin.
- Y468 (= Y407) mutation to A: Abolished lysophosphatidylcholine (LPC) transport.
- C473 (≠ V411) mutation to A: Reduced lysophosphatidylcholine (LPC) transport.
- P506 (≠ R444) to L: in NEDMISBA; reduced expression; no effect on cell membrane localization; loss of LPC transport activity
Query Sequence
>N515DRAFT_2416 FitnessBrowser__Dyella79:N515DRAFT_2416
MTIALESSPARAAAMADRLTLREKVGYGLGDAGGNVVIVLAMNFLNFFYTDVYGISPATV
GLMFLAVRIFDAFADPVMGILADHTRSRWGRYRPWQLWVALPLGVAVVLAFTVPPLQGDA
RIAWACVTYLLLSLGYTAINVPYCAMINAMTVSRREVVSCQSWRFALCGAAALLVSTALP
WLVEQWSGAGGPARGYQRGAAAMCAVAAAMFLCCFLWVRERVPLRNEAFSLRRLADGLRR
NDQLQLMLVMSFLLITILNVRGGGYLYFITYVLRGDARYASLFFGAVALAAILGALLVGP
LSRWLDTVRFYRYVNLALAAVSASMWFIPGGADAQLAWLLAMFGSGVVLGLCLPLHFSVM
AFADDYGQWKTGVRSSGMNFAFNLVFIKLAWASGAGIIALVLYLVRYQAGVAQTVTALGG
ITAIQTLIPAAIHLLLAFTLGFCRLDDATMKRVSQDLQQRHTDRPG
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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