SitesBLAST
Comparing HSERO_RS04850 FitnessBrowser__HerbieS:HSERO_RS04850 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 94% coverage: 1:342/362 of query aligns to 4:353/375 of 2d62A
1g291 Malk (see paper)
39% identity, 88% coverage: 24:340/362 of query aligns to 18:348/372 of 1g291
- binding magnesium ion: D69 (= D69), E71 (≠ R71), K72 (≠ D72), K79 (≠ R79), D80 (= D80), E292 (= E289), D293 (vs. gap)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
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, 94% coverage: 1:342/362 of query aligns to 4:331/353 of 1vciA
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, 81% coverage: 1:295/362 of query aligns to 1:291/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 94% coverage: 2:342/362 of query aligns to 1:338/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q88), R129 (≠ Q135), Q133 (≠ G139), S135 (= S141), G136 (≠ A142), G137 (≠ D143), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 94% coverage: 2:342/362 of query aligns to 1:339/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q88), Q133 (≠ G139), G136 (≠ A142), G137 (≠ D143), Q138 (≠ A144), H192 (= H199)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 89% coverage: 24:344/362 of query aligns to 16:346/384 of 8hplC
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 90% coverage: 1:325/362 of query aligns to 1:321/369 of P19566
- L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ Q310) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 89% coverage: 1:322/362 of query aligns to 1:320/371 of P68187
- A85 (≠ V91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ D143) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ T235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F248) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ L275) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ K283) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G285) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A304) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ Q310) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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)
34% identity, 89% coverage: 2:322/362 of query aligns to 1:319/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
34% identity, 89% coverage: 2:322/362 of query aligns to 1:319/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q88), R128 (≠ Q135), A132 (≠ G139), S134 (= S141), G136 (≠ D143), Q137 (≠ A144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
34% identity, 89% coverage: 2:322/362 of query aligns to 1:319/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ Q135), S134 (= S141), Q137 (≠ A144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S141), G136 (≠ D143), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
34% identity, 89% coverage: 2:322/362 of query aligns to 1:319/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ S19), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ Q135), A132 (≠ G139), S134 (= S141), Q137 (≠ A144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S141), G135 (≠ A142), G136 (≠ D143), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
34% identity, 89% coverage: 2:322/362 of query aligns to 1:319/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ S19), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ Q135), A132 (≠ G139), S134 (= S141), Q137 (≠ A144)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
34% identity, 88% coverage: 4:322/362 of query aligns to 1:317/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ Q135), A130 (≠ G139), S132 (= S141), G134 (≠ D143), Q135 (≠ A144)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 1:294/362 of query aligns to 1:284/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 1:294/362 of query aligns to 1:284/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 1:294/362 of query aligns to 1:284/353 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)
35% identity, 81% coverage: 1:294/362 of query aligns to 1:284/353 of Q97UY8
- S142 (= S141) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (≠ D143) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E166) 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+).
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 81% coverage: 28:322/362 of query aligns to 14:289/344 of 2awnC
Sites not aligning to the query:
Query Sequence
>HSERO_RS04850 FitnessBrowser__HerbieS:HSERO_RS04850
MARIEFKNLGHAYSGNPASLKDYALQPMNMVWEDGGAYALLGPSGCGKSTLLNIISGLLQ
PSEGQVLFDGRDMTRMATRDRNIAQVFQFPVLYDTMSVFDNLAFPLRNRKIAEREVQARV
REIAEMLDLTRDLKQRAAGLSADAKQKISLGRGLVRKDVAAILFDEPLTVIDPHMKWELR
QKLKEIHHQLKLTLIYVTHDQVEALTFADEVVVMTEGKVVQQGKPEALFLRPDHTFVGYF
IGSPGMNFCPVRLEGDAVLLGQQRLQIEAAQLQALKNSNGELKLGIRPEFVELAAPGATG
AVSAEITQVQHLGTSQLVTAQFEGMSVKARLSPEMKIATGNQWLRLAKPETIYFSNDERI
GR
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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