SitesBLAST
Comparing H281DRAFT_02450 FitnessBrowser__Burk376:H281DRAFT_02450 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
46% identity, 97% coverage: 5:385/393 of query aligns to 2:380/382 of 7ahhC
- 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: L275 (≠ M289), S297 (≠ A312), S298 (≠ F313)
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F15), T39 (≠ I42), V40 (= V43), G41 (= G44), G62 (= G65), G64 (= G67), K65 (= K68), D187 (= D190), E188 (= E191)
7aheC Opua inhibited inward facing (see paper)
46% identity, 97% coverage: 5:385/393 of query aligns to 2:380/382 of 7aheC
- 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: L275 (≠ M289), S297 (≠ A312), S298 (≠ F313)
7ahdC Opua (e190q) occluded (see paper)
58% identity, 66% coverage: 5:263/393 of query aligns to 2:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F15), T39 (≠ I42), S61 (= S64), G62 (= G65), G64 (= G67), K65 (= K68), S66 (= S69), T67 (= T70), Q111 (= Q114), K161 (≠ A164), Q162 (= Q165), S164 (= S167), G166 (= G169), M167 (= M170), Q188 (≠ E191), H221 (= H224)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
40% identity, 59% coverage: 35:265/393 of query aligns to 12:242/375 of 2d62A
1g291 Malk (see paper)
41% identity, 59% coverage: 34:265/393 of query aligns to 8:239/372 of 1g291
- binding magnesium ion: D69 (≠ S95), E71 (≠ P97), K72 (≠ R98), K79 (≠ R105), D80 (≠ R106)
- binding pyrophosphate 2-: S38 (= S64), G39 (= G65), C40 (≠ S66), G41 (= G67), K42 (= K68), T43 (≠ S69), T44 (= T70)
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)
43% identity, 56% coverage: 52:270/393 of query aligns to 40:252/378 of P69874
- F45 (≠ I57) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S66) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I72) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I88) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V153) mutation to M: Loss of ATPase activity and transport.
- D172 (= D190) 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.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 64% coverage: 39:289/393 of query aligns to 15:269/343 of P30750
- 40:46 (vs. 64:70, 86% identical) binding
- E166 (= E191) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
36% identity, 64% coverage: 39:289/393 of query aligns to 16:270/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: I19 (= I42), S41 (= S64), G42 (= G65), A43 (≠ S66), G44 (= G67), K45 (= K68), S46 (= S69), T47 (= T70), N141 (≠ Q165), S143 (= S167), Q146 (≠ M170), H200 (= H224)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
36% identity, 64% coverage: 39:289/393 of query aligns to 16:270/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
36% identity, 64% coverage: 39:289/393 of query aligns to 16:270/344 of 3tuiC
Sites not aligning to the query:
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
43% identity, 58% coverage: 44:269/393 of query aligns to 20:239/241 of 4u00A
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
38% identity, 60% coverage: 34:269/393 of query aligns to 6:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ T39), V16 (≠ G44), S36 (= S64), G37 (= G65), S38 (= S66), G39 (= G67), K40 (= K68), S41 (= S69), T42 (= T70), E162 (= E191), H194 (= H224)
- binding magnesium ion: S41 (= S69), E162 (= E191)
3d31A Modbc from methanosarcina acetivorans (see paper)
33% identity, 62% coverage: 34:277/393 of query aligns to 5:241/348 of 3d31A
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)
35% identity, 60% coverage: 33:266/393 of query aligns to 6:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ T39), S37 (= S64), G38 (= G65), C39 (≠ S66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (= T70), Q81 (= Q114), R128 (≠ K161), A132 (≠ Q165), S134 (= S167), G136 (= G169), Q137 (≠ M170), E158 (= E191), H191 (= H224)
- binding magnesium ion: S42 (= S69), Q81 (= Q114)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
35% identity, 60% coverage: 33:266/393 of query aligns to 6:233/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ T39), G38 (= G65), C39 (≠ S66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (= T70), R128 (≠ K161), S134 (= S167), Q137 (≠ M170)
- binding beryllium trifluoride ion: S37 (= S64), G38 (= G65), K41 (= K68), Q81 (= Q114), S134 (= S167), G136 (= G169), H191 (= H224)
- binding magnesium ion: S42 (= S69), Q81 (= Q114)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
35% identity, 60% coverage: 33:266/393 of query aligns to 6:233/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ T39), V17 (≠ G44), G38 (= G65), C39 (≠ S66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (= T70), R128 (≠ K161), A132 (≠ Q165), S134 (= S167), Q137 (≠ M170)
- binding tetrafluoroaluminate ion: S37 (= S64), G38 (= G65), K41 (= K68), Q81 (= Q114), S134 (= S167), G135 (= G168), G136 (= G169), E158 (= E191), H191 (= H224)
- binding magnesium ion: S42 (= S69), Q81 (= Q114)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
35% identity, 60% coverage: 33:266/393 of query aligns to 6:233/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ T39), V17 (≠ G44), G38 (= G65), C39 (≠ S66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (= T70), R128 (≠ K161), A132 (≠ Q165), S134 (= S167), Q137 (≠ M170)
- binding magnesium ion: S42 (= S69), Q81 (= Q114)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 60% coverage: 33:266/393 of query aligns to 6:233/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
35% identity, 60% coverage: 33:266/393 of query aligns to 7:234/371 of P68187
- A85 (= A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S138) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A146) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V149) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E151) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A156) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G169) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D190) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D260) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 60% coverage: 33:266/393 of query aligns to 4:231/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ T39), S35 (= S64), G36 (= G65), C37 (≠ S66), G38 (= G67), K39 (= K68), S40 (= S69), T41 (= T70), R126 (≠ K161), A130 (≠ Q165), S132 (= S167), G134 (= G169), Q135 (≠ M170)
Query Sequence
>H281DRAFT_02450 FitnessBrowser__Burk376:H281DRAFT_02450
MNSPKVVVEGLCKVFGTNPKQALAMLAGGATKEEVFARTGQIVGVHNVSFEVKEGEIFVL
MGLSGSGKSTLIRLINRLVEPSAGKVLIDGRDVASVPRAELTALRRKDMSMVFQSFALMP
QRTVLSNAAFGLEVAGVSRKEREARAMTVLEQVGLAPFAAKLPAQLSGGMQQRVGLARAL
AVNPSLMIMDEAFSALDPLKRKEMQNVLLDLQREQQRTILFVSHDLEEAMRIGTRIAIME
GGKVVQIGTPQEIITNPADDYVRAFFEGIDTSRYLTAGDLMQTDAVPLMHSHSPQIDASS
VAATLNGSADYAFVLDSERKIRGFVCRDETGSASAKLNYVECIRRTTPLDDVVERVVASR
APLPVVEADGSYCGSVNKTNVLHVLTRHRGSHV
Or try a new SitesBLAST search
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