SitesBLAST
Comparing GFF2789 FitnessBrowser__Phaeo:GFF2789 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
34% identity, 83% coverage: 2:213/255 of query aligns to 6:224/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 3:206/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 79% coverage: 3:203/255 of query aligns to 4:207/371 of P68187
- A85 (= A81) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R102) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V113) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A115) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S120) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G133) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D154) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 1:204/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y12), S35 (= S37), G36 (= G38), C37 (= C39), G38 (= G40), K39 (= K41), S40 (= S42), T41 (= T43), R126 (≠ A125), A130 (≠ Q129), S132 (= S131), G134 (= G133), Q135 (≠ M134)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 3:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y12), S37 (= S37), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), Q81 (= Q78), R128 (≠ A125), A132 (≠ Q129), S134 (= S131), G136 (= G133), Q137 (≠ M134), E158 (= E155), H191 (= H188)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 3:206/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ A125), S134 (= S131), Q137 (≠ M134)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q78), S134 (= S131), G136 (= G133), H191 (= H188)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 3:206/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ A125), A132 (≠ Q129), S134 (= S131), Q137 (≠ M134)
- binding tetrafluoroaluminate ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q78), S134 (= S131), G135 (= G132), G136 (= G133), E158 (= E155), H191 (= H188)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 79% coverage: 3:203/255 of query aligns to 3:206/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ A125), A132 (≠ Q129), S134 (= S131), Q137 (≠ M134)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
41% identity, 79% coverage: 2:203/255 of query aligns to 3:207/369 of P19566
- L86 (= L82) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P156) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D161) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1g291 Malk (see paper)
35% identity, 80% coverage: 3:205/255 of query aligns to 4:215/372 of 1g291
- binding magnesium ion: D69 (≠ Q64), E71 (≠ P66), K72 (≠ E67), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S37), G39 (= G38), C40 (= C39), G41 (= G40), K42 (= K41), T43 (≠ S42), T44 (= T43)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 76% coverage: 20:213/255 of query aligns to 44:244/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
38% identity, 76% coverage: 20:213/255 of query aligns to 44:244/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
37% identity, 76% coverage: 20:213/255 of query aligns to 44:244/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S37), G62 (= G38), G64 (= G40), K65 (= K41), S66 (= S42), T67 (= T43), Q111 (= Q78), K161 (= K128), Q162 (= Q129), S164 (= S131), G166 (= G133), M167 (= M134), Q188 (≠ E155), H221 (= H188)
Sites not aligning to the query:
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 87% coverage: 3:223/255 of query aligns to 2:239/343 of P30750
- 40:46 (vs. 37:43, 86% identical) binding
- E166 (= E155) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 82% coverage: 3:212/255 of query aligns to 18:228/378 of P69874
- C26 (≠ A11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ Q61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ T117) mutation to M: Loss of ATPase activity and transport.
- D172 (= D154) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 79% coverage: 2:203/255 of query aligns to 3:208/393 of P9WQI3
- H193 (= H188) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprD Lpqy-sugabc in state 4 (see paper)
38% identity, 83% coverage: 2:213/255 of query aligns to 2:215/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S37), C40 (= C39), G41 (= G40), K42 (= K41), S43 (= S42), T44 (= T43), Q82 (= Q78), R129 (≠ A125), Q133 (= Q129), S135 (= S131), G136 (= G132), G137 (= G133), Q159 (≠ E155), H192 (= H188)
- binding magnesium ion: S43 (= S42), Q82 (= Q78)
8hprC Lpqy-sugabc in state 4 (see paper)
38% identity, 83% coverage: 2:213/255 of query aligns to 2:215/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S37), G39 (= G38), G41 (= G40), K42 (= K41), S43 (= S42), Q82 (= Q78), Q133 (= Q129), G136 (= G132), G137 (= G133), Q138 (≠ M134), H192 (= H188)
- binding magnesium ion: S43 (= S42), Q82 (= Q78)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
36% identity, 87% coverage: 3:223/255 of query aligns to 3:240/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
36% identity, 87% coverage: 3:223/255 of query aligns to 3:240/344 of 3tuiC
Query Sequence
>GFF2789 FitnessBrowser__Phaeo:GFF2789
MDIRLSAVGHAYDNVAVLSDITLDIPSGKIVCIVGPSGCGKSTLLRFIGGLERPTQGEVL
QVGQPPEGCLNPLTYVFQDFALLPWRTVRGNISLVLEDHGIRGAAAARIIDDVLARTKLS
DFAGALPKQLSGGMKQRVAIARALAVNPAVMLMDEPLSALDSQTRELLMDDLVALWTRTP
FTAVYVTHNLAEAVRLGHAIVVLSRRPGQIREIVHLDTPLAERAFGDADLEQKQKYLWQL
MRDEARAADAELMNV
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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