SitesBLAST
Comparing WP_011022261.1 NCBI__GCF_000007345.1:WP_011022261.1 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
34% identity, 92% coverage: 31:383/383 of query aligns to 24:366/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 75% coverage: 20:307/383 of query aligns to 24:299/378 of P69874
- C26 (≠ R22) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ S23) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S49) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ F55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L134) mutation to M: Loss of ATPase activity and transport.
- D172 (= D171) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ R275) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E305) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
37% identity, 79% coverage: 4:307/383 of query aligns to 3:294/372 of 1g291
- binding magnesium ion: D69 (= D78), E71 (≠ D80), K72 (= K81), K79 (≠ Q88), D80 (≠ K89), E292 (= E305), D293 (≠ N306)
- binding pyrophosphate 2-: S38 (= S47), G39 (= G48), C40 (≠ S49), G41 (= G50), K42 (= K51), T43 (= T52), T44 (= T53)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
32% identity, 95% coverage: 22:383/383 of query aligns to 14:373/384 of 8hplC
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
38% identity, 71% coverage: 37:309/383 of query aligns to 31:280/353 of 1vciA
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
34% identity, 75% coverage: 22:307/383 of query aligns to 16:286/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S47), G39 (= G48), G41 (= G50), K42 (= K51), S43 (≠ T52), Q82 (= Q97), Q133 (= Q146), G136 (= G149), G137 (= G150), Q138 (= Q151), H192 (= H205)
- binding magnesium ion: S43 (≠ T52), Q82 (= Q97)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
34% identity, 75% coverage: 22:307/383 of query aligns to 16:286/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S47), C40 (≠ S49), G41 (= G50), K42 (= K51), S43 (≠ T52), T44 (= T53), Q82 (= Q97), R129 (≠ H142), Q133 (= Q146), S135 (= S148), G136 (= G149), G137 (= G150), Q159 (≠ E172), H192 (= H205)
- binding magnesium ion: S43 (≠ T52), Q82 (= Q97)
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)
38% identity, 60% coverage: 18:248/383 of query aligns to 9:236/393 of P9WQI3
- H193 (= H205) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
3d31A Modbc from methanosarcina acetivorans (see paper)
38% identity, 77% coverage: 17:309/383 of query aligns to 3:278/348 of 3d31A
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
43% identity, 59% coverage: 31:256/383 of query aligns to 21:247/350 of 3fvqB
- binding adenosine-5'-triphosphate: S38 (= S47), G39 (= G48), C40 (≠ S49), G41 (= G50), K42 (= K51), T43 (= T52), T44 (= T53), R133 (≠ H142), E137 (≠ Q146), S139 (= S148), G141 (= G150), Q142 (= Q151)
- binding calcium ion: T43 (= T52), Q86 (= Q97)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 58% coverage: 21:243/383 of query aligns to 34:259/382 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)
38% identity, 58% coverage: 21:243/383 of query aligns to 34:259/382 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
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 74% coverage: 25:309/383 of query aligns to 16:283/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 74% coverage: 25:309/383 of query aligns to 16:283/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 74% coverage: 25:309/383 of query aligns to 16:283/353 of 1oxuA
Sites not aligning to the query:
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
35% identity, 74% coverage: 25:309/383 of query aligns to 16:283/353 of Q97UY8
- S142 (= S148) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G150) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E172) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
7ahdC Opua (e190q) occluded (see paper)
38% identity, 58% coverage: 21:243/383 of query aligns to 34:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ K26), S61 (= S47), G62 (= G48), G64 (= G50), K65 (= K51), S66 (≠ T52), T67 (= T53), Q111 (= Q97), K161 (≠ S145), Q162 (= Q146), S164 (= S148), G166 (= G150), M167 (≠ Q151), Q188 (≠ E172), H221 (= H205)
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)
35% identity, 74% coverage: 31:313/383 of query aligns to 21:293/371 of P68187
- A85 (≠ T100) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V127) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M130) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N132) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E137) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G150) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D171) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L241) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F253) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ R284) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G295) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (= S299) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G301) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
35% identity, 74% coverage: 31:313/383 of query aligns to 20:292/374 of 2awnB
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, 74% coverage: 31:313/383 of query aligns to 20:292/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S47), G38 (= G48), C39 (≠ S49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), Q81 (= Q97), R128 (≠ H142), A132 (≠ Q146), S134 (= S148), G136 (= G150), Q137 (= Q151), E158 (= E172), H191 (= H205)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q97)
Sites not aligning to the query:
Query Sequence
>WP_011022261.1 NCBI__GCF_000007345.1:WP_011022261.1
MRLGVKVDIKKHYTEAEINRKRSTGKAFTLDVSFEMDNELVVLFGPSGSGKTTLFKCISG
ITQPDNGKITVGSKIYYDKDKKINLPIQKRNLGYVFQNYTLFPHMNVRKNIECGLKKWEK
EDREVRVMEMLNLLHIEELETHYPSQLSGGQKQRVALARALAPKPELLLLDEPFSALDRV
LRIELAEKLKKLQKRIGIPLAFITHSLDEAFVLADRILILYRGEVQQFGAPEEIFYHPRN
LHVAELAGLSNIFDDARVEEQVEKLVEGNNAGPKRTVLKSGEMRIAVNPLNLKEGDKVSW
GIHPENITLLLPNSGSEDKDENVYSAYVHSITGKGPKKRIVLKLARHEKSLNAEVPAQFA
DALNLNTGDLCLVKMDMSKVVAF
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