SitesBLAST
Comparing Pf1N1B4_2293 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2293 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)
1g291 Malk (see paper)
47% identity, 72% coverage: 14:269/358 of query aligns to 2:267/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q85), D80 (≠ A86)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (= C52), G41 (= G53), K42 (= K54), T43 (= T55), T44 (= T56)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
41% identity, 83% coverage: 14:311/358 of query aligns to 5:324/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 64% coverage: 16:245/358 of query aligns to 7:230/353 of 1vciA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
47% identity, 65% coverage: 16:248/358 of query aligns to 18:252/378 of P69874
- C26 (≠ R24) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F25) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L43) 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 (= L74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V131) mutation to M: Loss of ATPase activity and transport.
- D172 (= D168) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 1:253/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F25), S37 (= S50), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q94), R128 (≠ K139), A132 (≠ Q143), S134 (= S145), G136 (= G147), Q137 (= Q148), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 1:253/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F25), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ K139), S134 (= S145), Q137 (= Q148)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S145), G136 (= G147), H191 (= H202)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 1:253/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ K139), A132 (≠ Q143), S134 (= S145), Q137 (= Q148)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S145), G135 (= G146), G136 (= G147), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 1:253/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (= C52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ K139), A132 (≠ Q143), S134 (= S145), Q137 (= Q148)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 1:253/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 70% coverage: 14:262/358 of query aligns to 2:254/371 of P68187
- A85 (= A97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M127) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E129) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ I134) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G147) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D168) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P238) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ W249) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 70% coverage: 14:262/358 of query aligns to 2:254/369 of P19566
- L86 (= L98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P170) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D175) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
43% identity, 69% coverage: 16:262/358 of query aligns to 1:251/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F25), S35 (= S50), G36 (= G51), C37 (= C52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (≠ K139), A130 (≠ Q143), S132 (= S145), G134 (= G147), Q135 (= Q148)
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, 78% coverage: 29:309/358 of query aligns to 18:304/393 of P9WQI3
- H193 (= H202) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 84% coverage: 18:318/358 of query aligns to 6:315/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 84% coverage: 18:318/358 of query aligns to 6:315/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 84% coverage: 18:318/358 of query aligns to 6:315/353 of 1oxuA
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)
38% identity, 84% coverage: 18:318/358 of query aligns to 6:315/353 of Q97UY8
- S142 (= S145) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G147) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E169) 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+).
8hprD Lpqy-sugabc in state 4 (see paper)
38% identity, 92% coverage: 30:357/358 of query aligns to 18:351/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S50), C40 (= C52), G41 (= G53), K42 (= K54), S43 (≠ T55), T44 (= T56), Q82 (= Q94), R129 (≠ K139), Q133 (= Q143), S135 (= S145), G136 (= G146), G137 (= G147), Q159 (≠ E169), H192 (= H202)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
38% identity, 92% coverage: 30:357/358 of query aligns to 18:352/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S50), G39 (= G51), G41 (= G53), K42 (= K54), S43 (≠ T55), Q82 (= Q94), Q133 (= Q143), G136 (= G146), G137 (= G147), Q138 (= Q148), H192 (= H202)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 63% coverage: 30:255/358 of query aligns to 16:245/384 of 8hplC
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_2293 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2293
MNHSTATALTNPGAPMKVRGVQKRFGAFTALDNVSLDVAAGELVCLLGPSGCGKTTLLRC
IAGLEKQDSGELYLGDRDVSHLAPQARDYGILFQSYALFPNLSVEANIAYGLTGSSRDEV
RQCVGQMLELVGLIGSEKKYPGQLSGGQQQRVALARALAPAPSLLLLDEPMSALDARVRE
HLCTELRQLQRNLGVTTLMVTHNQDEAMLMADRIAVMNNGKVEQYATPQEIYDRPATPFV
AEFVGQGNWLPFRRSSDSHAQVGGMNMRLAEGSAKTASGRLFCRPEAINVNPPVHEENLF
PAKVREITFLGNRCRMSFELDQLPGHALLAELAPEAMPRLGAQQIMVALPPRSLQVFA
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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