SitesBLAST
Comparing Echvi_1095 FitnessBrowser__Cola:Echvi_1095 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)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
52% identity, 92% coverage: 21:270/272 of query aligns to 4:253/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
52% identity, 92% coverage: 21:270/272 of query aligns to 2:251/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (= Y31), H40 (= H59), S41 (= S60), G42 (= G61), G44 (= G63), K45 (= K64), S46 (= S65), T47 (= T66), Q82 (= Q101), Q135 (≠ S154), S137 (= S156), G139 (= G158), M140 (= M159), H194 (= H213)
- binding magnesium ion: S46 (= S65), Q82 (= Q101)
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
49% identity, 91% coverage: 25:272/272 of query aligns to 6:254/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (≠ Y31), Y20 (= Y38), S42 (= S60), G43 (= G61), G45 (= G63), K46 (= K64), S47 (= S65), T48 (= T66), Q83 (= Q101), K132 (= K150), E136 (≠ S154), S138 (= S156), G140 (= G158), H195 (= H213)
- binding magnesium ion: S47 (= S65), Q83 (= Q101)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
50% identity, 91% coverage: 25:272/272 of query aligns to 6:254/658 of 8wm7C
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)
38% identity, 83% coverage: 22:247/272 of query aligns to 4:226/393 of P9WQI3
- H193 (= H213) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 81% coverage: 22:240/272 of query aligns to 3:221/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y31), S38 (= S60), C40 (= C62), G41 (= G63), K42 (= K64), S43 (= S65), T44 (= T66), Q82 (= Q101), R129 (≠ K150), Q133 (≠ S154), S135 (= S156), G136 (≠ Q157), G137 (= G158), Q159 (≠ E180), H192 (= H213)
- binding magnesium ion: S43 (= S65), Q82 (= Q101)
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 81% coverage: 22:240/272 of query aligns to 3:221/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y31), S38 (= S60), G39 (= G61), G41 (= G63), K42 (= K64), S43 (= S65), Q82 (= Q101), Q133 (≠ S154), G136 (≠ Q157), G137 (= G158), Q138 (≠ M159), H192 (= H213)
- binding magnesium ion: S43 (= S65), Q82 (= Q101)
8hplC Lpqy-sugabc in state 1 (see paper)
36% identity, 81% coverage: 22:240/272 of query aligns to 3:219/384 of 8hplC
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 11:216/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S60), G36 (= G61), C37 (= C62), G38 (= G63), K39 (= K64), S40 (= S65), T41 (= T66), R126 (≠ K150), A130 (≠ S154), S132 (= S156), G134 (= G158), Q135 (≠ M159)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 13:218/374 of 2awnB
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 77% coverage: 40:248/272 of query aligns to 32:240/378 of P69874
- F45 (= F53) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C62) mutation to T: Loss of ATPase activity and transport.
- L60 (= L68) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V84) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V142) mutation to M: Loss of ATPase activity and transport.
- D172 (= D179) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 13:218/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S60), G38 (= G61), C39 (= C62), G40 (= G63), K41 (= K64), S42 (= S65), T43 (= T66), Q81 (= Q101), R128 (≠ K150), A132 (≠ S154), S134 (= S156), G136 (= G158), Q137 (≠ M159), E158 (= E180), H191 (= H213)
- binding magnesium ion: S42 (= S65), Q81 (= Q101)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 13:218/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G61), C39 (= C62), G40 (= G63), K41 (= K64), S42 (= S65), T43 (= T66), R128 (≠ K150), S134 (= S156), Q137 (≠ M159)
- binding beryllium trifluoride ion: S37 (= S60), G38 (= G61), K41 (= K64), Q81 (= Q101), S134 (= S156), G136 (= G158), H191 (= H213)
- binding magnesium ion: S42 (= S65), Q81 (= Q101)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 13:218/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V40), G38 (= G61), C39 (= C62), G40 (= G63), K41 (= K64), S42 (= S65), T43 (= T66), R128 (≠ K150), A132 (≠ S154), S134 (= S156), Q137 (≠ M159)
- binding tetrafluoroaluminate ion: S37 (= S60), G38 (= G61), K41 (= K64), Q81 (= Q101), S134 (= S156), G135 (≠ Q157), G136 (= G158), E158 (= E180), H191 (= H213)
- binding magnesium ion: S42 (= S65), Q81 (= Q101)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 75% coverage: 36:240/272 of query aligns to 13:218/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V40), G38 (= G61), C39 (= C62), G40 (= G63), K41 (= K64), S42 (= S65), T43 (= T66), R128 (≠ K150), A132 (≠ S154), S134 (= S156), Q137 (≠ M159)
- binding magnesium ion: S42 (= S65), Q81 (= Q101)
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)
36% identity, 75% coverage: 36:240/272 of query aligns to 14:219/371 of P68187
- A85 (≠ S104) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K131) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L139) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V142) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G145) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G158) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D179) 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 75% coverage: 36:240/272 of query aligns to 14:219/369 of P19566
- L86 (= L105) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P181) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D186) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
37% identity, 74% coverage: 36:237/272 of query aligns to 37:245/382 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
7aheC Opua inhibited inward facing (see paper)
37% identity, 74% coverage: 36:237/272 of query aligns to 37:245/382 of 7aheC
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
7ahdC Opua (e190q) occluded (see paper)
37% identity, 74% coverage: 36:237/272 of query aligns to 37:245/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ Y38), S61 (= S60), G62 (= G61), G64 (= G63), K65 (= K64), S66 (= S65), T67 (= T66), Q111 (= Q101), K161 (≠ H153), Q162 (≠ S154), S164 (= S156), G166 (= G158), M167 (= M159), Q188 (≠ E180), H221 (= H213)
Sites not aligning to the query:
Query Sequence
>Echvi_1095 FitnessBrowser__Cola:Echvi_1095
MQALIERKHQTVQHLKDQPEMLVCDQLKKVYPTPKGDYVVLDDLNLSIRKGEFVSIIGHS
GCGKSTLLTMIAGLNDISGGKIKVDGTPVIEAGPDRAVVFQSPSLLPWLSALDNVMIGVK
QVFPHASRAQKQDICKYYLDKVGLGADFDKKAHSLSQGMQQRVGIARAFALKPKLLLLDE
PFGMLDSLTRGELQDVLLEIWQREKITAVAITHDVDESIFLADRVIMMTSGPYAKIGDEL
IIPFERPRVRKAVLEHPEYYDYRGYLMNFLNH
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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