SitesBLAST
Comparing GFF2317 FitnessBrowser__psRCH2:GFF2317 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, 75% coverage: 23:232/279 of query aligns to 31:239/378 of P69874
- 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 (= L68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ M132) mutation to M: Loss of ATPase activity and transport.
- D172 (= D169) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 77% coverage: 4:218/279 of query aligns to 1:206/374 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)
41% identity, 77% coverage: 4:218/279 of query aligns to 1:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F15), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q85), R128 (≠ A140), A132 (≠ Q144), S134 (= S146), G136 (= G148), Q137 (≠ M149), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 77% coverage: 4:218/279 of query aligns to 1:206/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F15), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A140), S134 (= S146), Q137 (≠ M149)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S146), G136 (= G148), H191 (= H203)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 77% coverage: 4:218/279 of query aligns to 1:206/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A140), A132 (≠ Q144), S134 (= S146), Q137 (≠ M149)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S146), G135 (= G147), G136 (= G148), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 77% coverage: 4:218/279 of query aligns to 1:206/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ A140), A132 (≠ Q144), S134 (= S146), Q137 (≠ M149)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 77% coverage: 4:218/279 of query aligns to 2:207/371 of P68187
- A85 (≠ S88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A125) 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 (≠ T135) 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.
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.
1g291 Malk (see paper)
39% identity, 82% coverage: 4:232/279 of query aligns to 2:231/372 of 1g291
- binding magnesium ion: D69 (≠ G75), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
43% identity, 71% coverage: 21:218/279 of query aligns to 12:204/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ A140), A130 (≠ Q144), S132 (= S146), G134 (= G148), Q135 (≠ M149)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 82% coverage: 4:233/279 of query aligns to 5:235/375 of 2d62A
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)
39% identity, 82% coverage: 4:232/279 of query aligns to 2:226/393 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 77% coverage: 4:218/279 of query aligns to 2:207/369 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 (= 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.
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 82% coverage: 4:232/279 of query aligns to 1:225/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F15), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q85), Q133 (= Q144), G136 (= G147), G137 (= G148), Q138 (≠ M149), H192 (= H203)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 82% coverage: 4:232/279 of query aligns to 1:225/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F15), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q85), R129 (≠ A140), Q133 (= Q144), S135 (= S146), G136 (= G147), G137 (= G148), Q159 (≠ E170), H192 (= H203)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
8hplC Lpqy-sugabc in state 1 (see paper)
38% identity, 75% coverage: 24:232/279 of query aligns to 16:223/384 of 8hplC
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
36% identity, 76% coverage: 6:218/279 of query aligns to 2:218/232 of 1f3oA
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
36% identity, 76% coverage: 6:218/279 of query aligns to 2:218/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F15), S40 (= S44), G41 (= G45), S42 (≠ C46), G43 (= G47), K44 (= K48), S45 (= S49), T46 (= T50), F138 (= F137), Q145 (= Q144), S147 (= S146), G149 (= G148), Q150 (≠ M149), H204 (= H203)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 84% coverage: 4:236/279 of query aligns to 2:236/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 84% coverage: 4:236/279 of query aligns to 2:236/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 84% coverage: 4:236/279 of query aligns to 2:236/353 of 1oxuA
Query Sequence
>GFF2317 FitnessBrowser__psRCH2:GFF2317
MSDAKIRVRQVGKTFASERREVQALQSIDLDIQPNEFVTFVGASGCGKSTLLRIIAGLET
LSRGEILLDGRPIDGPGVDRAMVFQHYSLYPWLTVMQNIKFCRQLKVIGNTVRHDGDVES
AAGRADALLNLMGLTRFADAYPSQLSGGMQQRVAIARALLPKPATLLMDEPFGALDAQTR
EVMHDLIRHVHRLEKSTILFVTHDVEEAIYLGSRIVLMAPRPGRIDSVYEVPLPAQRHQD
MKLAPEFTELKREILARIRETSGMQTDLEQLAKLSAVAG
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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