SitesBLAST
Comparing HSERO_RS16975 FitnessBrowser__HerbieS:HSERO_RS16975 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)
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 69% coverage: 38:226/272 of query aligns to 16:207/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 69% coverage: 38:226/272 of query aligns to 18:209/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (≠ T58), C40 (= C60), G41 (= G61), K42 (= K62), S43 (= S63), T44 (= T64), Q82 (= Q99), R129 (≠ H146), Q133 (= Q150), S135 (= S152), G136 (= G153), G137 (= G154), Q159 (≠ E176), H192 (= H209)
- binding magnesium ion: S43 (= S63), Q82 (= Q99)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 69% coverage: 38:226/272 of query aligns to 18:209/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (≠ T58), G39 (= G59), G41 (= G61), K42 (= K62), S43 (= S63), Q82 (= Q99), Q133 (= Q150), G136 (= G153), G137 (= G154), Q138 (≠ M155), H192 (= H209)
- binding magnesium ion: S43 (= S63), Q82 (= Q99)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 70% coverage: 35:224/272 of query aligns to 38:236/382 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)
39% identity, 70% coverage: 35:224/272 of query aligns to 38:236/382 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)
39% identity, 70% coverage: 35:224/272 of query aligns to 38:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (= T36), S61 (≠ T58), G62 (= G59), G64 (= G61), K65 (= K62), S66 (= S63), T67 (= T64), Q111 (= Q99), K161 (≠ H149), Q162 (= Q150), S164 (= S152), G166 (= G154), M167 (= M155), Q188 (≠ E176), H221 (= H209)
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)
40% identity, 69% coverage: 38:224/272 of query aligns to 19:208/393 of P9WQI3
- H193 (= H209) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 79% coverage: 11:224/272 of query aligns to 10:221/378 of P69874
- C26 (≠ R27) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F28) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F51) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C60) mutation to T: Loss of ATPase activity and transport.
- L60 (= L66) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V82) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V138) mutation to M: Loss of ATPase activity and transport.
- D172 (= D175) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 76% coverage: 19:225/272 of query aligns to 7:217/375 of 2d62A
1g291 Malk (see paper)
36% identity, 69% coverage: 38:225/272 of query aligns to 18:214/372 of 1g291
- binding magnesium ion: D69 (≠ Q85), E71 (≠ V87), K72 (≠ N88), K79 (vs. gap), D80 (= D91)
- binding pyrophosphate 2-: S38 (≠ T58), G39 (= G59), C40 (= C60), G41 (= G61), K42 (= K62), T43 (≠ S63), T44 (= T64)
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
37% identity, 77% coverage: 18:226/272 of query aligns to 2:208/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ D32), S37 (≠ T58), G38 (= G59), C39 (= C60), G40 (= G61), K41 (= K62), S42 (= S63), T43 (= T64), Q81 (= Q99), R128 (≠ H146), A132 (≠ Q150), S134 (= S152), G136 (= G154), Q137 (≠ M155), E158 (= E176), H191 (= H209)
- binding magnesium ion: S42 (= S63), Q81 (= Q99)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 77% coverage: 18:226/272 of query aligns to 2:208/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ D32), G38 (= G59), C39 (= C60), G40 (= G61), K41 (= K62), S42 (= S63), T43 (= T64), R128 (≠ H146), S134 (= S152), Q137 (≠ M155)
- binding beryllium trifluoride ion: S37 (≠ T58), G38 (= G59), K41 (= K62), Q81 (= Q99), S134 (= S152), G136 (= G154), H191 (= H209)
- binding magnesium ion: S42 (= S63), Q81 (= Q99)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 77% coverage: 18:226/272 of query aligns to 2:208/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ D32), V17 (= V37), G38 (= G59), C39 (= C60), G40 (= G61), K41 (= K62), S42 (= S63), T43 (= T64), R128 (≠ H146), A132 (≠ Q150), S134 (= S152), Q137 (≠ M155)
- binding tetrafluoroaluminate ion: S37 (≠ T58), G38 (= G59), K41 (= K62), Q81 (= Q99), S134 (= S152), G135 (= G153), G136 (= G154), E158 (= E176), H191 (= H209)
- binding magnesium ion: S42 (= S63), Q81 (= Q99)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 77% coverage: 18:226/272 of query aligns to 2:208/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ D32), V17 (= V37), G38 (= G59), C39 (= C60), G40 (= G61), K41 (= K62), S42 (= S63), T43 (= T64), R128 (≠ H146), A132 (≠ Q150), S134 (= S152), Q137 (≠ M155)
- binding magnesium ion: S42 (= S63), Q81 (= Q99)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 77% coverage: 18:226/272 of query aligns to 3:209/371 of P68187
- A85 (= A102) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A131) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ W134) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R136) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D141) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G154) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D175) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 77% coverage: 18:226/272 of query aligns to 2:208/374 of 2awnB
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 77% coverage: 18:226/272 of query aligns to 3:209/369 of P19566
- L86 (≠ V103) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P177) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D182) 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)
37% identity, 76% coverage: 19:226/272 of query aligns to 1:206/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ D32), S35 (≠ T58), G36 (= G59), C37 (= C60), G38 (= G61), K39 (= K62), S40 (= S63), T41 (= T64), R126 (≠ H146), A130 (≠ Q150), S132 (= S152), G134 (= G154), Q135 (≠ M155)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 69% coverage: 40:226/272 of query aligns to 12:178/344 of 2awnC
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
35% identity, 72% coverage: 19:214/272 of query aligns to 4:206/226 of 5xu1B
Query Sequence
>HSERO_RS16975 FitnessBrowser__HerbieS:HSERO_RS16975
INQHAFTPAGQAAQETPAIELRNVSCRFITADGRATVALRDFSMSVARGEFVAVVGPTGC
GKSTTLSLITGLLKPTLGEVRVMGQPVNGIDPRIGFVFQNDAVFPWRSVRENVAAGPLFR
GQPKAQAHALADEWIRRVGLDKFGDHYPHQLSGGMRKRVALAQTFINSPEILLMDEPFSA
LDMQTRTLMQDELLRLWSAHSGSVVFVTHDLEEAIALADKVYVLTARPATLKSVYPIDLP
RPRVMEEVRYEQRFIDISRRIWADLREEVHIA
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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