SitesBLAST
Comparing GFF770 FitnessBrowser__Marino:GFF770 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 78% coverage: 12:291/357 of query aligns to 17:299/378 of P69874
- C26 (≠ G21) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V132) mutation to M: Loss of ATPase activity and transport.
- D172 (= D169) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ A273) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ D289) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
38% identity, 94% coverage: 22:357/357 of query aligns to 13:367/372 of 1g291
- binding magnesium ion: D69 (≠ L78), E71 (vs. gap), K72 (vs. gap), K79 (≠ E86), D80 (≠ K87), E292 (≠ G279), D293 (≠ T280), K359 (≠ H349)
- binding pyrophosphate 2-: S38 (= S47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 80% coverage: 13:299/357 of query aligns to 4:298/371 of P68187
- A85 (= A98) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V125) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L128) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N130) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q135) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G148) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D169) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R239) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F250) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W276) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G279) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ D283) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ L285) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
39% identity, 80% coverage: 13:299/357 of query aligns to 3:297/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
39% identity, 80% coverage: 13:299/357 of query aligns to 3:297/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y22), S37 (= S47), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), Q81 (= Q95), R128 (≠ N140), A132 (≠ E144), S134 (= S146), G136 (= G148), Q137 (= Q149), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q95)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 80% coverage: 13:299/357 of query aligns to 3:297/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (≠ N140), S134 (= S146), Q137 (= Q149)
- binding beryllium trifluoride ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q95), S134 (= S146), G136 (= G148), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q95)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 80% coverage: 13:299/357 of query aligns to 3:297/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (= V27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (≠ N140), A132 (≠ E144), S134 (= S146), Q137 (= Q149)
- binding tetrafluoroaluminate ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q95), S134 (= S146), G135 (= G147), G136 (= G148), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S52), Q81 (= Q95)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 80% coverage: 13:299/357 of query aligns to 3:297/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (= V27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (≠ N140), A132 (≠ E144), S134 (= S146), Q137 (= Q149)
- binding magnesium ion: S42 (= S52), Q81 (= Q95)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 80% coverage: 13:299/357 of query aligns to 1:295/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y22), S35 (= S47), G36 (= G48), C37 (= C49), G38 (= G50), K39 (= K51), S40 (= S52), T41 (= T53), R126 (≠ N140), A130 (≠ E144), S132 (= S146), G134 (= G148), Q135 (= Q149)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 64% coverage: 17:246/357 of query aligns to 11:244/375 of 2d62A
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, 80% coverage: 13:299/357 of query aligns to 4:296/369 of P19566
- L86 (= L99) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P171) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D176) 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.
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
43% identity, 80% coverage: 13:297/357 of query aligns to 4:288/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y22), Q14 (≠ G23), T16 (≠ D25), V18 (= V27), S38 (= S47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53), R133 (≠ N140), E137 (= E144), S139 (= S146), G141 (= G148), Q142 (= Q149)
- binding calcium ion: T43 (≠ S52), Q86 (= Q95)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 96% coverage: 15:356/357 of query aligns to 6:353/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 96% coverage: 15:356/357 of query aligns to 6:353/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 96% coverage: 15:356/357 of query aligns to 6:353/353 of 1oxuA
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
35% identity, 96% coverage: 15:356/357 of query aligns to 6:353/353 of Q97UY8
- S142 (= S146) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G148) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E170) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
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, 66% coverage: 24:257/357 of query aligns to 16:251/393 of P9WQI3
- H193 (= H203) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 77% coverage: 26:299/357 of query aligns to 9:267/344 of 2awnC
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 64% coverage: 26:254/357 of query aligns to 15:243/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 64% coverage: 26:254/357 of query aligns to 17:245/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S47), C40 (= C49), G41 (= G50), K42 (= K51), S43 (= S52), T44 (= T53), Q82 (= Q95), R129 (≠ N140), Q133 (≠ E144), S135 (= S146), G136 (= G147), G137 (= G148), Q159 (≠ E170), H192 (= H203)
- binding magnesium ion: S43 (= S52), Q82 (= Q95)
Sites not aligning to the query:
Query Sequence
>GFF770 FitnessBrowser__Marino:GFF770
MSTTAQSPADWLLEVNNLSCGYGGDSVVKDVSFALSHGDIGCLLGPSGCGKSTILRALAG
FLPLSGGEISLQSQAISLPGRTLPPEKRRIGMVFQDYALFPHLTIADNVGFGLRNLNKAE
KRQKVMELLNVVHLQDLADNYPHELSGGQQQRVALARALAPEPTLILLDEPFSNLDADLR
RRLSLDVREILKTLGISAILVTHDQQEAFAMCDQVAVLRDGRIQQWDVPYNLYHEPANRF
VASFVGQGGFVPGTALGPDTIESELGVIHGNRAYKWEPGTLVDVLIRPDDIVHDPDSDLQ
PKVVEKTFAGTSTLYRFRCSEDTEFEALFRSHLDFNLGEHVPVRVEADHLIAFERTT
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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