SitesBLAST
Comparing WP_085770056.1 NCBI__GCF_002117405.1:WP_085770056.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
41% identity, 56% coverage: 10:255/436 of query aligns to 4:250/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
41% identity, 56% coverage: 10:255/436 of query aligns to 2:248/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (= Y20), H40 (≠ R49), S41 (= S50), G42 (= G51), G44 (= G53), K45 (= K54), S46 (= S55), T47 (= T56), Q82 (= Q91), Q135 (≠ E142), S137 (= S144), G139 (= G146), M140 (= M147), H194 (= H204)
- binding magnesium ion: S46 (= S55), Q82 (= Q91)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
39% identity, 59% coverage: 24:279/436 of query aligns to 15:276/658 of 8wm7C
Sites not aligning to the query:
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
40% identity, 54% coverage: 24:259/436 of query aligns to 15:255/256 of 8w9mC
- binding adenosine-5'-triphosphate: Y20 (≠ T29), S42 (= S50), G43 (= G51), G45 (= G53), K46 (= K54), S47 (= S55), T48 (= T56), Q83 (= Q91), K132 (≠ A138), E136 (= E142), S138 (= S144), G140 (= G146), H195 (= H204)
- binding magnesium ion: S47 (= S55), Q83 (= Q91)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
42% identity, 43% coverage: 35:220/436 of query aligns to 46:237/382 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, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
42% identity, 43% coverage: 35:220/436 of query aligns to 46:237/382 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)
42% identity, 43% coverage: 35:220/436 of query aligns to 46:237/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S50), G62 (= G51), G64 (= G53), K65 (= K54), S66 (= S55), T67 (= T56), Q111 (= Q91), K161 (= K141), Q162 (≠ E142), S164 (= S144), G166 (= G146), M167 (= M147), Q188 (≠ E168), H221 (= H204)
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)
41% identity, 46% coverage: 27:226/436 of query aligns to 29:226/378 of P69874
- F45 (≠ I43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ Y74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) 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
39% identity, 44% coverage: 28:221/436 of query aligns to 19:218/375 of 2d62A
1g291 Malk (see paper)
41% identity, 44% coverage: 28:220/436 of query aligns to 16:214/372 of 1g291
- binding magnesium ion: D69 (≠ G81), E71 (≠ V83), K72 (≠ D84), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (= C52), G41 (= G53), K42 (= K54), T43 (≠ S55), T44 (= T56)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 49% coverage: 13:227/436 of query aligns to 5:212/374 of 2awnB
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 48% coverage: 11:219/436 of query aligns to 4:214/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 48% coverage: 11:219/436 of query aligns to 4:214/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 48% coverage: 11:219/436 of query aligns to 4:214/353 of 1oxuA
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 49% coverage: 13:227/436 of query aligns to 6:213/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D133) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G146) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D167) 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.
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)
37% identity, 48% coverage: 11:219/436 of query aligns to 4:214/353 of Q97UY8
- S142 (= S144) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G146) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E168) 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+).
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 49% coverage: 13:227/436 of query aligns to 5:212/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y20), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), Q81 (= Q91), R128 (≠ A138), A132 (≠ E142), S134 (= S144), G136 (= G146), Q137 (≠ M147), E158 (= E168), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 49% coverage: 13:227/436 of query aligns to 5:212/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), S134 (= S144), Q137 (≠ M147)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G136 (= G146), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 49% coverage: 13:227/436 of query aligns to 5:212/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), V17 (= V30), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), A132 (≠ E142), S134 (= S144), Q137 (≠ M147)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H204)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 49% coverage: 13:227/436 of query aligns to 5:212/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), V17 (= V30), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ A138), A132 (≠ E142), S134 (= S144), Q137 (≠ M147)
- binding magnesium ion: S42 (= S55), Q81 (= Q91)
Query Sequence
>WP_085770056.1 NCBI__GCF_002117405.1:WP_085770056.1
MQSRSSNPPLLVIDDVSQNYGRGPDKGTTVLDHVSLTLKEGEIVGLLGRSGCGKSTLLRI
VSGLNRASGGEVRYRGEKVAGPVDGVAMVFQSFALFPWLTVLANVELGLRAKGAPREEAR
KRALQAIDIIGLDGFENAYPKEISGGMRQRVGFARALVVAPSLLLMDEPFSALDVLTAET
LRTDLLDLWVEGRMPIKSILMVTHNIEEAVLMCDRIVVLSSNPGRIAAEIGVSMQHPRNR
LDPEFRQLVDRIYALMTRRAEMAKTGSGAFPGLGLGMALPTVSTNTLAGMIEEVAAEPYD
GKADLPALADSLQLEIDDLFPVAETLQLLRFAELAEGDIKLTSAGRRFAELGVDQRKKLF
GDHLLAYVPLAQRIRRVLDERPSHHAPATRFREELQDYMSEEYAETTLRSVTTWGRYGEI
FAYDEASQSFSLENPQ
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