SitesBLAST
Comparing GFF3872 FitnessBrowser__Phaeo:GFF3872 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)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
40% identity, 92% coverage: 7:239/252 of query aligns to 17:251/265 of P07821
- K50 (= K40) mutation to Q: Lack of activity.
- D172 (= D160) mutation to E: Lack of activity.
- E173 (= E161) mutation to A: Lack of activity.
O65934 ABC transporter ATP-binding/permease protein Rv1747; EC 7.-.-.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
33% identity, 88% coverage: 2:224/252 of query aligns to 319:541/865 of O65934
- E479 (= E161) mutation to Q: Loss of ATPase activity.
Sites not aligning to the query:
- 33 R→A: Strong decrease in phosphorylation.
- 47 S→A: Strong decrease in phosphorylation. Lack of interaction with PknF. Attenuates growth in macrophages.
- 69 N→A: Strong decrease in phosphorylation.
- 152 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-210.
- 210 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-152.
- 234 R→A: Strong decrease in phosphorylation.
- 248 S→A: Strong decrease in phosphorylation. Decreases interaction with PknF.
- 270 N→A: Strong decrease in phosphorylation.
6z5uK Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp (see paper)
33% identity, 94% coverage: 1:236/252 of query aligns to 2:232/253 of 6z5uK
- binding phosphoaminophosphonic acid-adenylate ester: R12 (≠ L11), S37 (≠ N36), G38 (= G37), G40 (= G39), K41 (= K40), T42 (≠ S41), T43 (= T42), Q86 (= Q82), E164 (= E161), H197 (= H194)
- binding magnesium ion: Q86 (= Q82), E164 (= E161)
7d0aB Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation (see paper)
33% identity, 94% coverage: 1:236/252 of query aligns to 4:234/263 of 7d0aB
7d08B Acinetobacter mlafedb complex in atp-bound vtrans1 conformation (see paper)
33% identity, 94% coverage: 1:236/252 of query aligns to 4:234/263 of 7d08B
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
30% identity, 88% coverage: 1:223/252 of query aligns to 17:235/378 of P69874
- C26 (≠ T10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ L11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A38) mutation to T: Loss of ATPase activity and transport.
- L60 (= L44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L60) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ F123) 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.
5x40A Structure of a cbio dimer bound with amppcp (see paper)
38% identity, 80% coverage: 17:218/252 of query aligns to 21:222/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: N40 (= N36), G41 (= G37), G43 (= G39), K44 (= K40), S45 (= S41), T46 (= T42), Q88 (= Q82), H139 (≠ D134), M140 (≠ E135), L141 (= L136), S142 (= S137), G144 (= G139), Q145 (= Q140), Q166 (≠ E161), H198 (= H194)
- binding magnesium ion: S45 (= S41), Q88 (= Q82)
Sites not aligning to the query:
7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp (see paper)
32% identity, 85% coverage: 2:214/252 of query aligns to 4:218/262 of 7chaI
8hprC Lpqy-sugabc in state 4 (see paper)
32% identity, 79% coverage: 27:226/252 of query aligns to 29:224/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (≠ N36), G39 (= G37), G41 (= G39), K42 (= K40), S43 (= S41), Q82 (= Q82), Q133 (≠ E135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (= S41), Q82 (= Q82)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
32% identity, 79% coverage: 27:226/252 of query aligns to 29:224/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (≠ N36), C40 (≠ A38), G41 (= G39), K42 (= K40), S43 (= S41), T44 (= T42), Q82 (= Q82), R129 (= R131), Q133 (≠ E135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (= S41), Q82 (= Q82)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
32% identity, 79% coverage: 27:226/252 of query aligns to 27:222/384 of 8hplC
Sites not aligning to the query:
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
33% identity, 83% coverage: 17:226/252 of query aligns to 23:227/658 of 8wm7C
Sites not aligning to the query:
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
32% identity, 83% coverage: 17:226/252 of query aligns to 23:227/256 of 8w9mC
- binding adenosine-5'-triphosphate: S42 (≠ N36), G43 (= G37), G45 (= G39), K46 (= K40), S47 (= S41), T48 (= T42), Q83 (= Q82), K132 (≠ R131), E136 (= E135), S138 (= S137), G140 (= G139), H195 (= H194)
- binding magnesium ion: S47 (= S41), Q83 (= Q82)
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)
29% identity, 95% coverage: 1:239/252 of query aligns to 5:229/393 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
30% identity, 79% coverage: 27:226/252 of query aligns to 52:253/382 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, 39, 40, 41
6tejB Structure of apo irtab devoid sid in complex with sybody syb_nl5 (see paper)
35% identity, 88% coverage: 2:223/252 of query aligns to 331:551/585 of 6tejB
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 82% coverage: 12:218/252 of query aligns to 14:216/369 of P19566
- L86 (≠ V86) 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)
32% identity, 76% coverage: 27:218/252 of query aligns to 28:215/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
32% identity, 76% coverage: 27:218/252 of query aligns to 26:213/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ N36), G36 (= G37), C37 (≠ A38), G38 (= G39), K39 (= K40), S40 (= S41), T41 (= T42), R126 (= R131), A130 (≠ E135), S132 (= S137), G134 (= G139), Q135 (= Q140)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 76% coverage: 27:218/252 of query aligns to 29:216/371 of P68187
- A85 (≠ D85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ Q113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D126) 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.
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.
Query Sequence
>GFF3872 FitnessBrowser__Phaeo:GFF3872
MIDVTGLSFTLGDKPILDTVDACLPAGQITALIGPNGAGKSTLLKLIAQQLTASWGRICL
SGCDLRSITPEQLARRMAVVGQQLDVASRVRVRDLVGFGRWPHSRGRLRAEDQAAIADAL
ALFELDDLRDRFLDELSGGQRQRAFIAMAYAQDTDWLLLDEPLNNLDLNHARNLMAQLRH
LADTRGKSIVIVLHDLNYAISWADHVVALAAGRVAFAGPVAEVATSESLSALYQTPVALR
EVEGRPIACYHG
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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