SitesBLAST
Comparing SMc02346 FitnessBrowser__Smeli:SMc02346 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)
40% identity, 78% coverage: 3:219/278 of query aligns to 2:236/382 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
7aheC Opua inhibited inward facing (see paper)
40% identity, 78% coverage: 3:219/278 of query aligns to 2:236/382 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, 78% coverage: 3:219/278 of query aligns to 2:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F13), T39 (vs. gap), S61 (= S53), G62 (= G54), G64 (= G56), K65 (= K57), S66 (= S58), T67 (≠ V59), Q111 (= Q94), K161 (≠ S144), Q162 (= Q145), S164 (= S147), G166 (= G149), M167 (= M150), Q188 (≠ E171), H221 (= H204)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 88% coverage: 33:278/278 of query aligns to 32:281/378 of P69874
- F45 (= F46) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S55) mutation to T: Loss of ATPase activity and transport.
- L60 (= L61) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I77) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ F133) mutation to M: Loss of ATPase activity and transport.
- D172 (= D170) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ A273) mutation to A: Lower ATPase activity and transport efficiency.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: 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.
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 66% coverage: 39:221/278 of query aligns to 22:207/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
46% identity, 66% coverage: 39:221/278 of query aligns to 24:209/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S53), G39 (= G54), G41 (= G56), K42 (= K57), S43 (= S58), Q82 (= Q94), Q133 (= Q145), G136 (= G148), G137 (= G149), Q138 (≠ M150), H192 (= H204)
- binding magnesium ion: S43 (= S58), Q82 (= Q94)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
46% identity, 66% coverage: 39:221/278 of query aligns to 24:209/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S53), C40 (≠ S55), G41 (= G56), K42 (= K57), S43 (= S58), T44 (≠ V59), Q82 (= Q94), R129 (= R141), Q133 (= Q145), S135 (= S147), G136 (= G148), G137 (= G149), Q159 (≠ E171), H192 (= H204)
- binding magnesium ion: S43 (= S58), Q82 (= Q94)
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, 79% coverage: 1:219/278 of query aligns to 1:208/393 of P9WQI3
- H193 (= H204) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 68% coverage: 31:220/278 of query aligns to 19:217/375 of 2d62A
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
40% identity, 76% coverage: 4:214/278 of query aligns to 2:220/232 of 1f3oA
1g291 Malk (see paper)
40% identity, 66% coverage: 37:220/278 of query aligns to 22:214/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (≠ D78), K79 (≠ P85), D80 (≠ H86)
- binding pyrophosphate 2-: S38 (= S53), G39 (= G54), C40 (≠ S55), G41 (= G56), K42 (= K57), T43 (≠ S58), T44 (≠ V59)
Sites not aligning to the query:
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
40% identity, 76% coverage: 4:214/278 of query aligns to 2:220/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F13), S40 (= S53), G41 (= G54), S42 (= S55), G43 (= G56), K44 (= K57), S45 (= S58), T46 (≠ V59), F138 (= F142), Q145 (= Q145), S147 (= S147), G149 (= G149), Q150 (≠ M150), H204 (= H204)
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
39% identity, 68% coverage: 31:219/278 of query aligns to 14:209/240 of 4ymuJ
- binding adenosine-5'-triphosphate: V16 (= V33), S36 (= S53), G37 (= G54), S38 (= S55), G39 (= G56), K40 (= K57), S41 (= S58), T42 (≠ V59), E162 (= E171), H194 (= H204)
- binding magnesium ion: S41 (= S58), E162 (= E171)
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
39% identity, 68% coverage: 31:218/278 of query aligns to 20:215/226 of 5xu1B
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 77% coverage: 20:232/278 of query aligns to 2:220/374 of 2awnB
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: 20:232/278 of query aligns to 3:221/371 of P68187
- A85 (= A97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ F129) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ H131) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ N136) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G149) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D170) 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.
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: 20:232/278 of query aligns to 2:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (vs. gap), S37 (= S53), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (≠ V59), Q81 (= Q94), R128 (= R141), A132 (≠ Q145), S134 (= S147), G136 (= G149), Q137 (≠ M150), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 77% coverage: 20:232/278 of query aligns to 2:220/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (vs. gap), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (≠ V59), R128 (= R141), S134 (= S147), Q137 (≠ M150)
- binding beryllium trifluoride ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q94), S134 (= S147), G136 (= G149), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 77% coverage: 20:232/278 of query aligns to 2:220/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (vs. gap), V17 (= V33), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (≠ V59), R128 (= R141), A132 (≠ Q145), S134 (= S147), Q137 (≠ M150)
- binding tetrafluoroaluminate ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q94), S134 (= S147), G135 (= G148), G136 (= G149), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 77% coverage: 20:232/278 of query aligns to 2:220/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (vs. gap), V17 (= V33), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (≠ V59), R128 (= R141), A132 (≠ Q145), S134 (= S147), Q137 (≠ M150)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
Query Sequence
>SMc02346 FitnessBrowser__Smeli:SMc02346
MERIAVNGVCKTFTLKPGQTVTVDGVTSNRIAVLDGVDLSIDRGEFITLVGPSGSGKSVL
LDVIAGLTGATSGVASIDGIEVSKPHARTAYVFQQYALFPWRTALQNVEYALEVRGVPAA
ERREKARHFLHLFGLNGFEDRFPSQLSGGMQQRVAIARALSTDPQVLLMDEPFAALDAQT
RDILQSELLRIWEQIKTTVVFVTHSIDEAIYLADRVVVMTARPARVKEIVEIDLPRPRDL
DIRNGEAFNAYRGRVWESLRDEVSKAQRDWALASSYAN
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