SitesBLAST
Comparing HSERO_RS03005 FitnessBrowser__HerbieS:HSERO_RS03005 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
48% identity, 80% coverage: 10:297/361 of query aligns to 18:310/378 of P69874
- C26 (≠ S18) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F19) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ T38) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C47) mutation to T: Loss of ATPase activity and transport.
- L60 (= L53) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L257) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E283) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 80% coverage: 9:295/361 of query aligns to 6:307/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
47% identity, 88% coverage: 6:321/361 of query aligns to 3:314/353 of 1vciA
1g291 Malk (see paper)
51% identity, 68% coverage: 10:255/361 of query aligns to 4:255/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ E81), D80 (≠ K82)
- binding pyrophosphate 2-: S38 (= S45), G39 (= G46), C40 (= C47), G41 (= G48), K42 (= K49), T43 (= T50), T44 (= T51)
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)
47% identity, 77% coverage: 10:287/361 of query aligns to 4:280/393 of P9WQI3
- H193 (= H200) 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)
41% identity, 94% coverage: 10:349/361 of query aligns to 3:348/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F19), S38 (= S45), C40 (= C47), G41 (= G48), K42 (= K49), S43 (≠ T50), T44 (= T51), Q82 (= Q90), R129 (= R137), Q133 (= Q141), S135 (= S143), G136 (= G144), G137 (= G145), Q159 (≠ E167), H192 (= H200)
- binding magnesium ion: S43 (≠ T50), Q82 (= Q90)
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 94% coverage: 10:349/361 of query aligns to 3:349/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F19), S38 (= S45), G39 (= G46), G41 (= G48), K42 (= K49), S43 (≠ T50), Q82 (= Q90), Q133 (= Q141), G136 (= G144), G137 (= G145), Q138 (= Q146), H192 (= H200)
- binding magnesium ion: S43 (≠ T50), Q82 (= Q90)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
42% identity, 87% coverage: 9:322/361 of query aligns to 3:322/369 of P19566
- L86 (= L94) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ F306) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 87% coverage: 9:322/361 of query aligns to 2:323/374 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)
41% identity, 87% coverage: 9:322/361 of query aligns to 2:323/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F19), S37 (= S45), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), Q81 (= Q90), R128 (= R137), A132 (≠ Q141), S134 (= S143), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q90)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 87% coverage: 9:322/361 of query aligns to 2:323/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F19), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R137), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (= S45), G38 (= G46), K41 (= K49), Q81 (= Q90), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q90)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 87% coverage: 9:322/361 of query aligns to 2:323/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ R24), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R137), A132 (≠ Q141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (= S45), G38 (= G46), K41 (= K49), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q90)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 87% coverage: 9:322/361 of query aligns to 2:323/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ R24), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R137), A132 (≠ Q141), S134 (= S143), Q137 (= Q146)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q90)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 87% coverage: 9:322/361 of query aligns to 3:324/371 of P68187
- A85 (= A93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D236) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ R247) 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 (= G273) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ Q277) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ L279) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G300) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ F306) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ A320) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 77% coverage: 10:287/361 of query aligns to 3:277/384 of 8hplC
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 81% coverage: 29:322/361 of query aligns to 19:321/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S45), G36 (= G46), C37 (= C47), G38 (= G48), K39 (= K49), S40 (≠ T50), T41 (= T51), R126 (= R137), A130 (≠ Q141), S132 (= S143), G134 (= G145), Q135 (= Q146)
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 81% coverage: 29:322/361 of query aligns to 14:293/344 of 2awnC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
36% identity, 94% coverage: 12:349/361 of query aligns to 7:344/348 of 3d31A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 8:301/361 of query aligns to 2:298/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 8:301/361 of query aligns to 2:298/353 of 1oxvA
Query Sequence
>HSERO_RS03005 FitnessBrowser__HerbieS:HSERO_RS03005
MKSHQEAVSIRLSQCAKSFANGTRALQPLDLQIHPGETLVLLGPSGCGKTTTLRMIAGLE
FPDEGGRVLFGEEDVTMLPIEKRGVGMVFQNYALFPNMSVGENIAYGMKIRKIAAGERAE
RVERLLEMVHLQGLSHRRVDQLSGGQKQRVALARALAMEPRVLLLDEPLTALDAKLREAV
RSDLNKLLRSLGITAIYVTHDQGEAMALGDRIVVMERGKISQIGTPQEIYYHPANDFVAE
FIGAMNRVDGIVAGDRLQLPTGTLPLPPDAVAGQPAQALFRPEDVEVIDITEADAHCLRG
KLINTFFLGDRTRFEIEIGAERPVIAETSRRGWWEAGQQIAIRVPATALVTMAPRAAKET
A
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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