SitesBLAST
Comparing GFF4122 FitnessBrowser__Marino:GFF4122 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)
61% identity, 95% coverage: 5:360/373 of query aligns to 17:375/378 of P69874
- C26 (≠ Q14) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F15) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V123) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ R263) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E285) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
61% identity, 95% coverage: 5:357/373 of query aligns to 2:357/358 of 8y5iA
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
44% identity, 87% coverage: 6:329/373 of query aligns to 7:342/375 of 2d62A
1g291 Malk (see paper)
46% identity, 76% coverage: 6:287/373 of query aligns to 4:294/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (= E67), K72 (≠ N68), K79 (≠ E75), D80 (≠ N76), E292 (= E285), D293 (= D286)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46)
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)
50% identity, 65% coverage: 6:249/373 of query aligns to 4:250/393 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.
8hplC Lpqy-sugabc in state 1 (see paper)
52% identity, 60% coverage: 24:245/373 of query aligns to 20:243/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
52% identity, 60% coverage: 24:245/373 of query aligns to 22:245/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (≠ T45), Q82 (= Q84), Q133 (= Q135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q84)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
52% identity, 60% coverage: 24:245/373 of query aligns to 22:245/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S40), C40 (= C42), G41 (= G43), K42 (= K44), S43 (≠ T45), T44 (= T46), Q82 (= Q84), R129 (= R131), Q133 (= Q135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q84)
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)
50% identity, 64% coverage: 1:237/373 of query aligns to 2:230/353 of 1vciA
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, 68% coverage: 6:258/373 of query aligns to 4:258/369 of P19566
- L86 (= L88) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
44% identity, 68% coverage: 6:258/373 of query aligns to 3:257/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
44% identity, 68% coverage: 6:258/373 of query aligns to 1:255/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F15), S35 (= S40), G36 (= G41), C37 (= C42), G38 (= G43), K39 (= K44), S40 (≠ T45), T41 (= T46), R126 (= R131), A130 (≠ Q135), S132 (= S137), G134 (= G139), Q135 (= Q140)
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, 68% coverage: 6:258/373 of query aligns to 3:257/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F15), S37 (= S40), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), Q81 (= Q84), R128 (= R131), A132 (≠ Q135), S134 (= S137), G136 (= G139), Q137 (= Q140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
44% identity, 68% coverage: 6:258/373 of query aligns to 3:257/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F15), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R131), S134 (= S137), Q137 (= Q140)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
44% identity, 68% coverage: 6:258/373 of query aligns to 3:257/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (= V20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R131), A132 (≠ Q135), S134 (= S137), Q137 (= Q140)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
44% identity, 68% coverage: 6:258/373 of query aligns to 3:257/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (= V20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R131), A132 (≠ Q135), S134 (= S137), Q137 (= Q140)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
44% identity, 68% coverage: 6:258/373 of query aligns to 4:258/371 of P68187
- A85 (= A87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A119) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A121) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q126) 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 (≠ L230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F241) 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 66% coverage: 12:258/373 of query aligns to 2:227/344 of 2awnC
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 76% coverage: 8:289/373 of query aligns to 6:283/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 76% coverage: 8:289/373 of query aligns to 6:283/353 of 1oxvA
Query Sequence
>GFF4122 FitnessBrowser__Marino:GFF4122
MKQTLLSLSNLSKQFGGKTVLDGLDLEIYDGEFITLLGPSGCGKTTLLRLMAGFEHPDEG
TITLAGENLTHTAPENRPLNTVFQHYALFPHMSVFDNVAYGLKMEKRPKDEIRQRVDEAL
AMVQLQDFARRKPHQLSGGQQQRVAIARAVVKRPRLLLLDEPLSALDYKLRRTMQVELKR
LQRELGITFVFVTHDQEEALSMSDRVVVLKDGLVQQLGTPREVYERPANLFTARFVGETN
FFPGTVESVQDGSIKVDVFGLKRTLRRPDFPVQAEQSLHVLLRPEDIRVLEPDDENGVAG
KIVERNYKGSTLDSVIHLADGTEVLASEFFDEDDPAFDYRLGEPVKVSWVDGWEWLLPEE
ASQRSEEELPADA
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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