SitesBLAST
Comparing BPHYT_RS20230 FitnessBrowser__BFirm:BPHYT_RS20230 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)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
46% identity, 83% coverage: 23:260/288 of query aligns to 26:263/265 of P07821
- K50 (= K47) mutation to Q: Lack of activity.
- D172 (= D169) mutation to E: Lack of activity.
- E173 (= E170) mutation to A: Lack of activity.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
36% identity, 73% coverage: 23:233/288 of query aligns to 17:224/241 of 4u00A
Sites not aligning to the query:
3c4jA Abc protein artp in complex with atp-gamma-s
33% identity, 79% coverage: 11:237/288 of query aligns to 6:231/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
33% identity, 79% coverage: 11:237/288 of query aligns to 6:231/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
33% identity, 79% coverage: 11:237/288 of query aligns to 6:231/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
33% identity, 79% coverage: 11:237/288 of query aligns to 6:231/242 of 2oljA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 75% coverage: 23:238/288 of query aligns to 32:242/378 of P69874
- F45 (≠ V36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (vs. gap) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ S132) mutation to M: Loss of ATPase activity and transport.
- D172 (= D169) 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.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
33% identity, 73% coverage: 23:233/288 of query aligns to 16:224/240 of 4ymuJ
- binding adenosine-5'-triphosphate: V16 (= V23), S36 (≠ N43), G37 (= G44), S38 (≠ C45), G39 (= G46), K40 (= K47), S41 (= S48), T42 (= T49), E162 (= E170), H194 (= H203)
- binding magnesium ion: S41 (= S48), E162 (= E170)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 77% coverage: 7:229/288 of query aligns to 1:217/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 77% coverage: 7:229/288 of query aligns to 2:218/371 of P68187
- A85 (≠ Q92) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ W113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A123) 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 (≠ S132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G148) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D169) 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)
33% identity, 77% coverage: 7:229/288 of query aligns to 1:217/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y18), S37 (≠ N43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q89), R128 (= R140), A132 (= A144), S134 (= S146), G136 (= G148), Q137 (≠ E149), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S48), Q81 (= Q89)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 77% coverage: 7:229/288 of query aligns to 1:217/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R140), S134 (= S146), Q137 (≠ E149)
- binding beryllium trifluoride ion: S37 (≠ N43), G38 (= G44), K41 (= K47), Q81 (= Q89), S134 (= S146), G136 (= G148), H191 (= H203)
- binding magnesium ion: S42 (= S48), Q81 (= Q89)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
33% identity, 77% coverage: 7:229/288 of query aligns to 1:217/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R140), A132 (= A144), S134 (= S146), Q137 (≠ E149)
- binding tetrafluoroaluminate ion: S37 (≠ N43), G38 (= G44), K41 (= K47), Q81 (= Q89), S134 (= S146), G135 (= G147), G136 (= G148), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S48), Q81 (= Q89)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
33% identity, 77% coverage: 7:229/288 of query aligns to 1:217/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R140), A132 (= A144), S134 (= S146), Q137 (≠ E149)
- binding magnesium ion: S42 (= S48), Q81 (= Q89)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 77% coverage: 7:229/288 of query aligns to 2:218/369 of P19566
- L86 (≠ I93) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P171) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D176) 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)
33% identity, 76% coverage: 12:229/288 of query aligns to 4:215/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y18), S35 (≠ N43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (= S48), T41 (= T49), R126 (= R140), A130 (= A144), S132 (= S146), G134 (= G148), Q135 (≠ E149)
5x40A Structure of a cbio dimer bound with amppcp (see paper)
37% identity, 79% coverage: 9:236/288 of query aligns to 5:231/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y18), V18 (= V22), A20 (≠ V23), N40 (= N43), G41 (= G44), G43 (= G46), K44 (= K47), S45 (= S48), T46 (= T49), Q88 (≠ A88), H139 (≠ A143), M140 (≠ A144), L141 (= L145), S142 (= S146), G144 (= G148), Q145 (≠ E149), Q166 (≠ E170), H198 (= H203)
- binding magnesium ion: S45 (= S48), Q88 (≠ A88)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
30% identity, 75% coverage: 18:232/288 of query aligns to 16:230/375 of 2d62A
1g291 Malk (see paper)
30% identity, 72% coverage: 27:234/288 of query aligns to 22:229/372 of 1g291
- binding magnesium ion: D69 (≠ S74), E71 (≠ R76), K72 (≠ R77), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (≠ N43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
30% identity, 78% coverage: 7:232/288 of query aligns to 1:221/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y18), S38 (≠ N43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (= S48), Q82 (= Q89), Q133 (≠ A144), G136 (= G147), G137 (= G148), Q138 (≠ E149), H192 (= H203)
- binding magnesium ion: S43 (= S48), Q82 (= Q89)
Query Sequence
>BPHYT_RS20230 FitnessBrowser__BFirm:BPHYT_RS20230
MTKSHGAALAAHSLTVGYRDHVVLHGLNLNIAAGRVTALCGPNGCGKSTLLRTLAGLQPA
LSGSVDVNGVPLASHRRRVLARTLTMLAQFNQIPSGLTVRELVAYGRYAHGGWLRGLSRA
DHAAIDEALVTSGLADDAARDVAALSGGERQRAWIAMALAQQAPIVLLDEPTTYLDIHHQ
LDILRELRRLNRERGLTIVWVLHDLNQAAAYSDEIVLMRAGRIVAQGSPDAMLDPRHLNE
TFSVPMLKIAHPQTGAPMCVPAYEGDFTDSNADAASLREEAISKDVAA
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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