SitesBLAST
Comparing GFF188 FitnessBrowser__WCS417:GFF188 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 93% coverage: 3:305/326 of query aligns to 18:349/378 of P69874
- C26 (≠ N11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L30) 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 (≠ F61) 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.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ H256) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to 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)
43% identity, 91% coverage: 1:298/326 of query aligns to 5:300/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
45% identity, 72% coverage: 3:238/326 of query aligns to 7:244/375 of 2d62A
1g291 Malk (see paper)
45% identity, 71% coverage: 7:238/326 of query aligns to 8:241/372 of 1g291
- binding magnesium ion: D69 (≠ G68), E71 (≠ D70), K72 (vs. gap), K79 (≠ R72), D80 (= D73)
- binding pyrophosphate 2-: S38 (= S37), G39 (= G38), C40 (= C39), G41 (= G40), K42 (= K41), T43 (= T42), T44 (= T43)
Sites not aligning to the query:
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)
46% identity, 72% coverage: 3:238/326 of query aligns to 4:236/393 of P9WQI3
- H193 (= H195) 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)
44% identity, 73% coverage: 2:239/326 of query aligns to 2:235/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
44% identity, 73% coverage: 2:239/326 of query aligns to 3:236/371 of P68187
- A85 (= A84) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D127) 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.
- R228 (≠ D231) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
44% identity, 73% coverage: 2:239/326 of query aligns to 2:235/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F12), S37 (= S37), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), Q81 (= Q81), R128 (= R132), A132 (≠ Q136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
44% identity, 73% coverage: 2:239/326 of query aligns to 2:235/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F12), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), R128 (= R132), S134 (= S138), Q137 (= Q141)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q81), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
44% identity, 73% coverage: 2:239/326 of query aligns to 2:235/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F12), V17 (≠ A17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), R128 (= R132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding tetrafluoroaluminate ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q81), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
44% identity, 73% coverage: 2:239/326 of query aligns to 2:235/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F12), V17 (≠ A17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (= T43), R128 (= R132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 77% coverage: 17:266/326 of query aligns to 16:264/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 79% coverage: 8:266/326 of query aligns to 8:266/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F12), S38 (= S37), G39 (= G38), G41 (= G40), K42 (= K41), S43 (≠ T42), Q82 (= Q81), Q133 (= Q136), G136 (= G139), G137 (= G140), Q138 (= Q141), H192 (= H195)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 79% coverage: 8:266/326 of query aligns to 8:266/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F12), S38 (= S37), C40 (= C39), G41 (= G40), K42 (= K41), S43 (≠ T42), T44 (= T43), Q82 (= Q81), R129 (= R132), Q133 (= Q136), S135 (= S138), G136 (= G139), G137 (= G140), Q159 (≠ E162), H192 (= H195)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
44% identity, 73% coverage: 2:239/326 of query aligns to 3:236/369 of P19566
- L86 (= L85) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
44% identity, 73% coverage: 3:239/326 of query aligns to 1:233/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F12), S35 (= S37), G36 (= G38), C37 (= C39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (= T43), R126 (= R132), A130 (≠ Q136), S132 (= S138), G134 (= G140), Q135 (= Q141)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 87% coverage: 3:287/326 of query aligns to 4:315/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 87% coverage: 3:287/326 of query aligns to 4:315/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 87% coverage: 3:287/326 of query aligns to 4:315/353 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)
36% identity, 87% coverage: 3:287/326 of query aligns to 4:315/353 of Q97UY8
- S142 (= S138) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G140) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E162) 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+).
Query Sequence
>GFF188 FitnessBrowser__WCS417:GFF188
MSIEVRNVSKNFNAFKALNSINLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDDGSIV
FHGEDVSGHDVRDRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKNQRPSESQIAVKVHEL
LNMVQLDWLSDRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLA
RLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDS
NRLHVGEDKHVLFRPHEVSLSRHELEDHHAAEVRDIRPLGATTRVTLKVEGQSELIEAEV
VKDHDSLTGLARGETLFFKPKVWQKA
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