SitesBLAST
Comparing SM_b21146 FitnessBrowser__Smeli:SM_b21146 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, 74% coverage: 6:236/312 of query aligns to 31:263/382 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
7aheC Opua inhibited inward facing (see paper)
43% identity, 74% coverage: 6:236/312 of query aligns to 31:263/382 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)
43% identity, 73% coverage: 6:233/312 of query aligns to 31:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (= T14), S61 (= S36), G62 (= G37), G64 (= G39), K65 (= K40), S66 (≠ T41), T67 (= T42), Q111 (= Q82), K161 (≠ H134), Q162 (≠ E135), S164 (= S137), G166 (= G139), M167 (≠ Q140), Q188 (≠ E161), H221 (= H194)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
42% identity, 79% coverage: 2:247/312 of query aligns to 7:252/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
39% identity, 91% coverage: 2:286/312 of query aligns to 7:270/353 of 1vciA
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 78% coverage: 2:243/312 of query aligns to 3:241/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y11), S38 (= S36), C40 (≠ S38), G41 (= G39), K42 (= K40), S43 (≠ T41), T44 (= T42), Q82 (= Q82), R129 (= R131), Q133 (≠ E135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q82)
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 78% coverage: 2:243/312 of query aligns to 3:241/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y11), S38 (= S36), G39 (= G37), G41 (= G39), K42 (= K40), S43 (≠ T41), Q82 (= Q82), Q133 (≠ E135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q82)
1g291 Malk (see paper)
37% identity, 91% coverage: 2:286/312 of query aligns to 4:286/372 of 1g291
- binding magnesium ion: D69 (= D61), E71 (= E63), K72 (≠ D64), K79 (≠ F71), D80 (≠ E72)
- binding pyrophosphate 2-: S38 (= S36), G39 (= G37), C40 (≠ S38), G41 (= G39), K42 (= K40), T43 (= T41), T44 (= T42)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 84% coverage: 1:263/312 of query aligns to 17:274/378 of P69874
- C26 (≠ R10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S38) mutation to T: Loss of ATPase activity and transport.
- L60 (= L44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I60) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ F121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) 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.
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 78% coverage: 2:243/312 of query aligns to 3:239/384 of 8hplC
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)
41% identity, 78% coverage: 2:243/312 of query aligns to 4:242/393 of P9WQI3
- H193 (= H194) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 82% coverage: 2:256/312 of query aligns to 4:252/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P162) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D167) 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)
37% identity, 78% coverage: 2:243/312 of query aligns to 3:240/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y11), S37 (= S36), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (= T42), Q81 (= Q82), R128 (= R131), A132 (≠ E135), S134 (= S137), G136 (= G139), Q137 (= Q140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 78% coverage: 2:243/312 of query aligns to 3:240/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y11), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (= T42), R128 (= R131), S134 (= S137), Q137 (= Q140)
- binding beryllium trifluoride ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 78% coverage: 2:243/312 of query aligns to 3:240/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y11), V17 (= V16), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (= T42), R128 (= R131), A132 (≠ E135), S134 (= S137), Q137 (= Q140)
- binding tetrafluoroaluminate ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 78% coverage: 2:243/312 of query aligns to 3:240/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y11), V17 (= V16), G38 (= G37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (= T42), R128 (= R131), A132 (≠ E135), S134 (= S137), Q137 (= Q140)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q82)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 78% coverage: 2:243/312 of query aligns to 4:241/371 of P68187
- A85 (≠ G85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S126) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G139) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D160) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F243) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 78% coverage: 2:243/312 of query aligns to 3:240/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 78% coverage: 2:243/312 of query aligns to 1:238/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y11), S35 (= S36), G36 (= G37), C37 (≠ S38), G38 (= G39), K39 (= K40), S40 (≠ T41), T41 (= T42), R126 (= R131), A130 (≠ E135), S132 (= S137), G134 (= G139), Q135 (= Q140)
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
40% identity, 73% coverage: 1:227/312 of query aligns to 2:227/241 of 4u00A
Query Sequence
>SM_b21146 FitnessBrowser__Smeli:SM_b21146
MIEIEEISKRYGDTTVVSDVSLTVAPHTVTVVVGTSGSGKTTLLRMINRLVEPTAGTIKI
DGEDNRSIPGFELRRRIGYAIQGHGLFPHRTVAQNIATVPTLLGWEKARIDAKVEELLKL
FQLDPSEFGPRYPHELSGGQQQRVGVARALAAEPNVLLMDEPFGALDPIIRAKAQDDLAA
IQKHFGTTIILVTHDMEEAFHLADRIAVMDKGEVVQYATPAEMLVRPATPFVETLVGASE
RPFRLLDIETVGEAVEPGSAEGRPVPEVLSQRDALSELLWTGRSALPVAAADGAILGKIT
LEAIVKRAARRQ
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