SitesBLAST
Comparing WP_110803735.1 NCBI__GCF_003217355.1:WP_110803735.1 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)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
46% identity, 94% coverage: 8:250/259 of query aligns to 3:253/658 of 8wm7C
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
46% identity, 94% coverage: 8:250/259 of query aligns to 3:253/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (= F17), Y20 (≠ E25), S42 (= S46), G43 (= G47), G45 (= G49), K46 (= K50), S47 (= S51), T48 (= T52), Q83 (= Q87), K132 (≠ A134), E136 (≠ Q138), S138 (= S140), G140 (= G142), H195 (= H197)
- binding magnesium ion: S47 (= S51), Q83 (= Q87)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
46% identity, 93% coverage: 8:249/259 of query aligns to 5:253/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
45% identity, 93% coverage: 8:249/259 of query aligns to 3:251/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (≠ F17), H40 (≠ A45), S41 (= S46), G42 (= G47), G44 (= G49), K45 (= K50), S46 (= S51), T47 (= T52), Q82 (= Q87), Q135 (= Q138), S137 (= S140), G139 (= G142), M140 (= M143), H194 (= H197)
- binding magnesium ion: S46 (= S51), Q82 (= Q87)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 83% coverage: 5:219/259 of query aligns to 15:226/378 of P69874
- C26 (≠ V16) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F17) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F39) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C48) mutation to T: Loss of ATPase activity and transport.
- L60 (= L54) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
44% identity, 83% coverage: 6:219/259 of query aligns to 1:211/358 of 8y5iA
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
39% identity, 75% coverage: 20:213/259 of query aligns to 15:217/375 of 2d62A
1g291 Malk (see paper)
38% identity, 87% coverage: 15:240/259 of query aligns to 11:237/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (≠ D71), K79 (≠ P78), D80 (≠ A79)
- binding pyrophosphate 2-: S38 (= S46), G39 (= G47), C40 (= C48), G41 (= G49), K42 (= K50), T43 (≠ S51), T44 (= T52)
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)
41% identity, 83% coverage: 27:240/259 of query aligns to 20:232/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 72% coverage: 27:212/259 of query aligns to 17:205/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 72% coverage: 27:212/259 of query aligns to 19:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S46), C40 (= C48), G41 (= G49), K42 (= K50), S43 (= S51), T44 (= T52), Q82 (= Q87), R129 (≠ A134), Q133 (= Q138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (= S51), Q82 (= Q87)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 72% coverage: 27:212/259 of query aligns to 19:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S46), G39 (= G47), G41 (= G49), K42 (= K50), S43 (= S51), Q82 (= Q87), Q133 (= Q138), G136 (= G141), G137 (= G142), Q138 (≠ M143), H192 (= H197)
- binding magnesium ion: S43 (= S51), Q82 (= Q87)
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
36% identity, 80% coverage: 8:213/259 of query aligns to 2:219/232 of 1f3oA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
39% identity, 83% coverage: 7:222/259 of query aligns to 3:215/369 of P19566
- L86 (= L91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) 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.
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
35% identity, 80% coverage: 8:213/259 of query aligns to 2:219/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F17), S40 (= S46), G41 (= G47), S42 (≠ C48), G43 (= G49), K44 (= K50), S45 (= S51), T46 (= T52), F138 (= F131), Q145 (= Q138), S147 (= S140), G149 (= G142), Q150 (≠ M143), H204 (= H197)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 83% coverage: 7:222/259 of query aligns to 2:214/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 83% coverage: 7:222/259 of query aligns to 3:215/371 of P68187
- A85 (≠ R90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ H122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) 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)
38% identity, 83% coverage: 7:222/259 of query aligns to 2:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F17), S37 (= S46), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), Q81 (= Q87), R128 (≠ A134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (≠ M143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 83% coverage: 7:222/259 of query aligns to 2:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F17), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ A134), S134 (= S140), Q137 (≠ M143)
- binding beryllium trifluoride ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q87), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 83% coverage: 7:222/259 of query aligns to 2:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F17), V17 (= V26), G38 (= G47), C39 (= C48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ A134), A132 (≠ Q138), S134 (= S140), Q137 (≠ M143)
- binding tetrafluoroaluminate ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q87), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
Query Sequence
>WP_110803735.1 NCBI__GCF_003217355.1:WP_110803735.1
MTEPTPALQIRALSKVFALREGALEVLRDITLTVDPGEFVTIVGASGCGKSTLLRLILGL
DRDFRGEIRVDGVPVTGPAADRAIVFQDHRLLPWLTAEANVAAALLNSPLDAETRAREVR
EHLDLVGLSKFAKAWPRQLSGGMAQRVAIARALVGRPRFLLLDEPLGALDALTRLRMQEE
LKRIVAHEGATALLVTHDVDEAVYLGHRVVVMQPHPGRIATILEVPPEARADRSSPAFVA
LRDRILGLLGVGAIEALAV
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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