SitesBLAST
Comparing 8500039 FitnessBrowser__Miya:8500039 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
43% identity, 46% coverage: 25:223/434 of query aligns to 42:244/382 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)
43% identity, 46% coverage: 25:223/434 of query aligns to 42:244/382 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)
42% identity, 46% coverage: 24:223/434 of query aligns to 41:244/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S44), G62 (= G45), G64 (= G47), K65 (= K48), S66 (= S49), T67 (= T50), Q111 (= Q85), K161 (≠ R135), Q162 (≠ E136), S164 (= S138), G166 (= G140), M167 (= M141), Q188 (≠ E162), H221 (= H198)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 48% coverage: 6:215/434 of query aligns to 7:218/375 of 2d62A
1g291 Malk (see paper)
40% identity, 44% coverage: 23:215/434 of query aligns to 17:215/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (≠ E74), K79 (vs. gap), D80 (≠ N77)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
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)
38% identity, 52% coverage: 6:230/434 of query aligns to 4:223/369 of P19566
- L86 (= L89) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D168) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 3:222/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y15), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q85), R128 (≠ A132), A132 (≠ E136), S134 (= S138), G136 (= G140), Q137 (≠ M141), E158 (= E162), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 3:222/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A132), S134 (= S138), Q137 (≠ M141)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S138), G136 (= G140), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 3:222/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A132), A132 (≠ E136), S134 (= S138), Q137 (≠ M141)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 3:222/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A132), A132 (≠ E136), S134 (= S138), Q137 (≠ M141)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 1:220/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y15), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ A132), A130 (≠ E136), S132 (= S138), G134 (= G140), Q135 (≠ M141)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 52% coverage: 6:230/434 of query aligns to 3:222/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 52% coverage: 6:230/434 of query aligns to 4:223/371 of P68187
- A85 (= A88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A127) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) 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.
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
37% identity, 48% coverage: 5:214/434 of query aligns to 3:217/226 of 5xu1B
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 49% coverage: 3:213/434 of query aligns to 15:221/378 of P69874
- C26 (≠ A14) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y15) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ Y68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
42% identity, 48% coverage: 6:215/434 of query aligns to 7:204/353 of 1vciA
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
38% identity, 49% coverage: 4:214/434 of query aligns to 1:210/241 of 4u00A
3c4jA Abc protein artp in complex with atp-gamma-s
35% identity, 55% coverage: 5:243/434 of query aligns to 3:241/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
35% identity, 55% coverage: 5:243/434 of query aligns to 3:241/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
35% identity, 55% coverage: 5:243/434 of query aligns to 3:241/242 of 2olkA
Query Sequence
>8500039 FitnessBrowser__Miya:8500039
MHAPLVTLRGLGKAYGSGARRFTAVSGVNLEIAEGEFVALLGPSGCGKSTLLRMITGLIA
PTEGEVLYRGGRLEGVNPHATIVFQTFALFPWLTVQENVEVVLKARGVPPRVRARRALDL
LDRVGLAGFDNAYPRELSGGMRQKVGFARAMAVEPELLCLDEPFSALDVLSAETLRGELL
ELWTSGKIPTRAILMVSHNIDEAVFMADRIVIMDKDPGHIVRVMPVDLPHPRQRKSPEYL
AFVDRVYALLAGQTLTEDEELGTAPGQPGHTRRLPDLTINEIAGLVERMADQPSHGADIY
RLTEELHVSSDYLLKVIEAAELLGFVTIRAGDMELTPLGETFAEASILARKEIFGSRLRR
LPLVVWLLDLLRASGNRQIKFEVAETALSLEFPRAEAARQVETMINWGRYAEILSYDDNS
EVILLEPEGGVHLE
Or try a new SitesBLAST search
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