SitesBLAST
Comparing SMc02739 FitnessBrowser__Smeli:SMc02739 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)
51% identity, 78% coverage: 13:284/349 of query aligns to 11:271/382 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)
51% identity, 78% coverage: 13:284/349 of query aligns to 11:271/382 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)
53% identity, 72% coverage: 13:265/349 of query aligns to 11:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F14), T39 (≠ V41), S61 (= S63), G62 (= G64), G64 (= G66), K65 (= K67), S66 (= S68), T67 (= T69), Q111 (= Q117), K161 (≠ N167), Q162 (≠ E168), S164 (= S170), G166 (= G172), M167 (= M173), Q188 (≠ E194), H221 (= H227)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 64% coverage: 49:273/349 of query aligns to 38:252/378 of P69874
- F45 (≠ I56) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S65) mutation to T: Loss of ATPase activity and transport.
- L60 (= L71) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V87) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V156) mutation to M: Loss of ATPase activity and transport.
- D172 (= D193) 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.
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
43% identity, 66% coverage: 39:269/349 of query aligns to 17:243/375 of 2d62A
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
42% identity, 65% coverage: 48:273/349 of query aligns to 22:237/358 of 8y5iA
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, 64% coverage: 48:269/349 of query aligns to 24:235/393 of P9WQI3
- H193 (= H227) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1g291 Malk (see paper)
39% identity, 72% coverage: 33:282/349 of query aligns to 8:255/372 of 1g291
- binding magnesium ion: D69 (≠ N95), E71 (≠ Y97), K72 (≠ R98), K79 (≠ R105), D80 (= D106)
- binding pyrophosphate 2-: S38 (= S63), G39 (= G64), C40 (≠ S65), G41 (= G66), K42 (= K67), T43 (≠ S68), T44 (= T69)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
39% identity, 64% coverage: 48:269/349 of query aligns to 21:232/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 64% coverage: 48:269/349 of query aligns to 23:234/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S63), G39 (= G64), G41 (= G66), K42 (= K67), S43 (= S68), Q82 (= Q117), Q133 (≠ E168), G136 (= G171), G137 (= G172), Q138 (≠ M173), H192 (= H227)
- binding magnesium ion: S43 (= S68), Q82 (= Q117)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 64% coverage: 48:269/349 of query aligns to 23:234/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S63), C40 (≠ S65), G41 (= G66), K42 (= K67), S43 (= S68), T44 (= T69), Q82 (= Q117), R129 (= R164), Q133 (≠ E168), S135 (= S170), G136 (= G171), G137 (= G172), Q159 (≠ E194), H192 (= H227)
- binding magnesium ion: S43 (= S68), Q82 (= Q117)
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, 68% coverage: 34:269/349 of query aligns to 8:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ T38), S37 (= S63), G38 (= G64), C39 (≠ S65), G40 (= G66), K41 (= K67), S42 (= S68), T43 (= T69), Q81 (= Q117), R128 (= R164), A132 (≠ E168), S134 (= S170), G136 (= G172), Q137 (≠ M173), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S68), Q81 (= Q117)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 68% coverage: 34:269/349 of query aligns to 8:233/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ T38), G38 (= G64), C39 (≠ S65), G40 (= G66), K41 (= K67), S42 (= S68), T43 (= T69), R128 (= R164), S134 (= S170), Q137 (≠ M173)
- binding beryllium trifluoride ion: S37 (= S63), G38 (= G64), K41 (= K67), Q81 (= Q117), S134 (= S170), G136 (= G172), H191 (= H227)
- binding magnesium ion: S42 (= S68), Q81 (= Q117)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 68% coverage: 34:269/349 of query aligns to 8:233/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ T38), V17 (≠ G43), G38 (= G64), C39 (≠ S65), G40 (= G66), K41 (= K67), S42 (= S68), T43 (= T69), R128 (= R164), A132 (≠ E168), S134 (= S170), Q137 (≠ M173)
- binding tetrafluoroaluminate ion: S37 (= S63), G38 (= G64), K41 (= K67), Q81 (= Q117), S134 (= S170), G135 (= G171), G136 (= G172), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S68), Q81 (= Q117)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 68% coverage: 34:269/349 of query aligns to 8:233/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ T38), V17 (≠ G43), G38 (= G64), C39 (≠ S65), G40 (= G66), K41 (= K67), S42 (= S68), T43 (= T69), R128 (= R164), A132 (≠ E168), S134 (= S170), Q137 (≠ M173)
- binding magnesium ion: S42 (= S68), Q81 (= Q117)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 68% coverage: 34:269/349 of query aligns to 6:231/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ T38), S35 (= S63), G36 (= G64), C37 (≠ S65), G38 (= G66), K39 (= K67), S40 (= S68), T41 (= T69), R126 (= R164), A130 (≠ E168), S132 (= S170), G134 (= G172), Q135 (≠ M173)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 68% coverage: 34:269/349 of query aligns to 9:234/371 of P68187
- A85 (= A120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A141) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V149) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Q152) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E154) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A159) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G172) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D193) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ Q263) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 68% coverage: 34:269/349 of query aligns to 8:233/374 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)
37% identity, 64% coverage: 48:269/349 of query aligns to 23:234/369 of P19566
- L86 (= L121) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P195) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D200) 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 64% coverage: 48:269/349 of query aligns to 15:203/344 of 2awnC
Sites not aligning to the query:
Query Sequence
>SMc02739 FitnessBrowser__Smeli:SMc02739
MSDAVVFKNVDIIFGKNPQLAVQMVDQGKTRDEIGAATGLVLGVAGASLTINEGEILVLM
GLSGSGKSTLLRAVNGLAPVVRGEVEVKTANGSLNPYRCNAKSLRDFRMHTVSMVFQQFA
LLPWRTVADNVGFGLELAGVADAERRKRVGEQLELVNLAKWADRKVNELSGGMQQRVGLA
RAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTIIFVSHDLDEAFRIGNRIA
IMEGGRIIQCGTPQEIVKKPANQYVADFVQHMNPITMLTAKDVMQTGVGRAAASTGVSAT
ARPTTPLVDILDAMSRQPGSIGVVDNGSVVGTIDAQNIVEGLTRHRNKG
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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