SitesBLAST
Comparing GFF510 FitnessBrowser__Phaeo:GFF510 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 20 (the maximum) hits to proteins with known functional sites (download)
8hprD Lpqy-sugabc in state 4 (see paper)
34% identity, 90% coverage: 32:364/372 of query aligns to 19:351/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (≠ T51), C40 (≠ S53), G41 (= G54), K42 (= K55), S43 (≠ T56), T44 (≠ S57), Q82 (= Q95), R129 (= R142), Q133 (≠ E146), S135 (= S148), G136 (= G149), G137 (= G150), Q159 (≠ E172), H192 (≠ S205)
- binding magnesium ion: S43 (≠ T56), Q82 (= Q95)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
34% identity, 90% coverage: 32:364/372 of query aligns to 19:352/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (≠ T51), G39 (= G52), G41 (= G54), K42 (= K55), S43 (≠ T56), Q82 (= Q95), Q133 (≠ E146), G136 (= G149), G137 (= G150), Q138 (= Q151), H192 (≠ S205)
- binding magnesium ion: S43 (≠ T56), Q82 (= Q95)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 95% coverage: 17:370/372 of query aligns to 7:350/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
41% identity, 64% coverage: 17:253/372 of query aligns to 7:249/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
36% identity, 79% coverage: 32:325/372 of query aligns to 17:319/384 of 8hplC
Sites not aligning to the query:
1g291 Malk (see paper)
39% identity, 64% coverage: 16:253/372 of query aligns to 3:246/372 of 1g291
- binding magnesium ion: D69 (= D76), E71 (≠ Q78), K72 (≠ D79), K79 (≠ Q86), D80 (≠ K87)
- binding pyrophosphate 2-: S38 (≠ T51), G39 (= G52), C40 (≠ S53), G41 (= G54), K42 (= K55), T43 (= T56), T44 (≠ S57)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 3:358/369 of P19566
- L86 (≠ N99) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P173) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D178) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E315) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 76% coverage: 3:285/372 of query aligns to 5:286/378 of P69874
- C26 (≠ R25) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ V26) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F44) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S53) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I59) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ M75) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L134) mutation to M: Loss of ATPase activity and transport.
- D172 (= D171) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ T275) mutation to A: Lower ATPase activity and transport efficiency.
Sites not aligning to the query:
- 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)
40% identity, 60% coverage: 32:256/372 of query aligns to 20:244/393 of P9WQI3
- H193 (≠ S205) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 2:359/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 95% coverage: 16:369/372 of query aligns to 3:360/371 of P68187
- A85 (≠ I98) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V127) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A130) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D132) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ R137) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G150) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D171) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ V241) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ T254) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W272) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G284) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T287) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ A289) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G309) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E315) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ M331) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G349) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ Y355) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F364) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
33% identity, 95% coverage: 17:369/372 of query aligns to 1:357/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ V26), S35 (≠ T51), G36 (= G52), C37 (≠ S53), G38 (= G54), K39 (= K55), S40 (≠ T56), T41 (≠ S57), R126 (= R142), A130 (≠ E146), S132 (= S148), G134 (= G150), Q135 (= Q151)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 2:359/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ V26), S37 (≠ T51), G38 (= G52), C39 (≠ S53), G40 (= G54), K41 (= K55), S42 (≠ T56), T43 (≠ S57), Q81 (= Q95), R128 (= R142), A132 (≠ E146), S134 (= S148), G136 (= G150), Q137 (= Q151), E158 (= E172), H191 (≠ S205)
- binding magnesium ion: S42 (≠ T56), Q81 (= Q95)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 2:359/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ V26), G38 (= G52), C39 (≠ S53), G40 (= G54), K41 (= K55), S42 (≠ T56), T43 (≠ S57), R128 (= R142), S134 (= S148), Q137 (= Q151)
- binding beryllium trifluoride ion: S37 (≠ T51), G38 (= G52), K41 (= K55), Q81 (= Q95), S134 (= S148), G136 (= G150), H191 (≠ S205)
- binding magnesium ion: S42 (≠ T56), Q81 (= Q95)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 2:359/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ V26), V17 (≠ H31), G38 (= G52), C39 (≠ S53), G40 (= G54), K41 (= K55), S42 (≠ T56), T43 (≠ S57), R128 (= R142), A132 (≠ E146), S134 (= S148), Q137 (= Q151)
- binding tetrafluoroaluminate ion: S37 (≠ T51), G38 (= G52), K41 (= K55), Q81 (= Q95), S134 (= S148), G135 (= G149), G136 (= G150), E158 (= E172), H191 (≠ S205)
- binding magnesium ion: S42 (≠ T56), Q81 (= Q95)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
33% identity, 95% coverage: 16:369/372 of query aligns to 2:359/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ V26), V17 (≠ H31), G38 (= G52), C39 (≠ S53), G40 (= G54), K41 (= K55), S42 (≠ T56), T43 (≠ S57), R128 (= R142), A132 (≠ E146), S134 (= S148), Q137 (= Q151)
- binding magnesium ion: S42 (≠ T56), Q81 (= Q95)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 91% coverage: 33:369/372 of query aligns to 12:329/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:249/372 of query aligns to 8:243/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:249/372 of query aligns to 8:243/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:249/372 of query aligns to 8:243/353 of 1oxuA
Query Sequence
>GFF510 FitnessBrowser__Phaeo:GFF510
MPRATGRPPESQSKMALELINVTKRVGAQLHIKETSLVLEPGHFNVLLGATGSGKTSLIK
MMAGLDPIASGQVVMDGQDVTALSTQKRNISLVHQFFINYPHMTVYENIASPLKVAGMAK
SEIEGRVEEAADILQLRPMLHRRPHELSGGQQQRTALARAIAKESRAVFLDEPLANLDYK
LREELRDQLPELFAGRGAVVVYATSEPEEALLLGGKTALMQDGRVTQFGTTADIYRNPDN
VAAARVFSDPPINTAPIVKQGSTARLGPDVSWSLTGAAADLADGPYTIAIRPYHVLPVAT
PLTTVQLSGQVQVTELSGSESSAHFDMGLDMDHGSWVSLSAGVHPYEVGEQHDFYMDPSA
AYVFAPDGSRVA
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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