SitesBLAST
Comparing BPHYT_RS28215 FitnessBrowser__BFirm:BPHYT_RS28215 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
42% identity, 96% coverage: 11:500/509 of query aligns to 5:494/501 of P04983
- K43 (= K49) mutation to R: Loss of transport.
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
25% identity, 42% coverage: 18:229/509 of query aligns to 12:232/253 of 1g9xB
5x40A Structure of a cbio dimer bound with amppcp (see paper)
34% identity, 47% coverage: 21:259/509 of query aligns to 16:242/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: V18 (= V23), A20 (= A25), N40 (= N45), G41 (= G46), G43 (= G48), K44 (= K49), S45 (= S50), T46 (= T51), Q88 (≠ Y91), H139 (≠ R146), M140 (≠ G147), L141 (= L148), S142 (= S149), G144 (≠ A151), Q145 (≠ D152), Q166 (≠ E173), H198 (= H205)
- binding magnesium ion: S45 (= S50), Q88 (≠ Y91)
Sites not aligning to the query:
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
25% identity, 42% coverage: 18:229/509 of query aligns to 12:232/254 of 1g6hA
4f4cA The crystal structure of the multi-drug transporter (see paper)
32% identity, 41% coverage: 30:237/509 of query aligns to 1043:1249/1250 of 4f4cA
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 46% coverage: 10:245/509 of query aligns to 3:242/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 46% coverage: 10:245/509 of query aligns to 3:242/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 46% coverage: 10:245/509 of query aligns to 3:242/353 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)
28% identity, 46% coverage: 10:245/509 of query aligns to 3:242/353 of Q97UY8
- S142 (= S149) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (≠ A151) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E173) 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+).
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
28% identity, 42% coverage: 18:229/509 of query aligns to 9:218/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F20), V16 (≠ A25), S36 (≠ N45), G37 (= G46), S38 (≠ A47), G39 (= G48), K40 (= K49), S41 (= S50), T42 (= T51), E162 (= E173), H194 (= H205)
- binding magnesium ion: S41 (= S50), E162 (= E173)
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
29% identity, 42% coverage: 274:485/509 of query aligns to 22:226/226 of 5xu1B
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 15:212/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (≠ V294), G38 (= G295), C39 (≠ A296), G40 (= G297), K41 (≠ R298), S42 (= S299), T43 (≠ E300), Q81 (≠ R344), R128 (≠ N396), A132 (≠ T401), S134 (= S403), G136 (= G405), Q137 (≠ N406), E158 (= E427), H191 (≠ S459)
- binding magnesium ion: S42 (= S299), Q81 (≠ R344)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 15:212/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G295), C39 (≠ A296), G40 (= G297), K41 (≠ R298), S42 (= S299), T43 (≠ E300), R128 (≠ N396), S134 (= S403), Q137 (≠ N406)
- binding beryllium trifluoride ion: S37 (≠ V294), G38 (= G295), K41 (≠ R298), Q81 (≠ R344), S134 (= S403), G136 (= G405), H191 (≠ S459)
- binding magnesium ion: S42 (= S299), Q81 (≠ R344)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 15:212/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V274), G38 (= G295), C39 (≠ A296), G40 (= G297), K41 (≠ R298), S42 (= S299), T43 (≠ E300), R128 (≠ N396), A132 (≠ T401), S134 (= S403), Q137 (≠ N406)
- binding tetrafluoroaluminate ion: S37 (≠ V294), G38 (= G295), K41 (≠ R298), Q81 (≠ R344), S134 (= S403), G135 (= G404), G136 (= G405), E158 (= E427), H191 (≠ S459)
- binding magnesium ion: S42 (= S299), Q81 (≠ R344)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 15:212/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V274), G38 (= G295), C39 (≠ A296), G40 (= G297), K41 (≠ R298), S42 (= S299), T43 (≠ E300), R128 (≠ N396), A132 (≠ T401), S134 (= S403), Q137 (≠ N406)
- binding magnesium ion: S42 (= S299), Q81 (≠ R344)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 41% coverage: 272:480/509 of query aligns to 16:213/371 of P68187
- A85 (≠ G347) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R375) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A381) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ W384) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ T386) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K391) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G405) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D426) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
27% identity, 48% coverage: 2:245/509 of query aligns to 9:249/378 of P69874
- C26 (≠ S19) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F20) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V38) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A47) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ V53) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V69) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L135) mutation to M: Loss of ATPase activity and transport.
- D172 (= D172) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 15:212/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
30% identity, 41% coverage: 272:480/509 of query aligns to 13:210/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ V294), G36 (= G295), C37 (≠ A296), G38 (= G297), K39 (≠ R298), S40 (= S299), T41 (≠ E300), R126 (≠ N396), A130 (≠ T401), S132 (= S403), G134 (= G405), Q135 (≠ N406)
Sites not aligning to the query:
7o12B Abc transporter nosdfy, amppnp-bound in gdn (see paper)
31% identity, 45% coverage: 11:238/509 of query aligns to 3:218/298 of 7o12B
Query Sequence
>BPHYT_RS28215 FitnessBrowser__BFirm:BPHYT_RS28215
MQQPTSAVPRLELRHASKSFGRVRALSDGDLALWPGEVHALLGENGAGKSTVVKILAGVH
QPDTGELVVDGEARRFATPAEARDAGLAVIYQEPTLFFDLSIAENIFMGRQPVDRIGRIQ
YDAMRREVDGLLASLGVDLRADQLVRGLSIADQQVIEIAKALSLNANVLIMDEPTAALSL
PEVERLFTIVRKLRERDVAILFITHRLDEVFALTQRVTIMRDGAKVFDGLTTDLNTEAIV
AKMVGRDLETFYPKAERPPGEVRLSVRGLTRVGVFKDISFDVRAGEIVALAGLVGAGRSE
VARAIFGIDPLDSGEIWIAGKRLTAGRPAAAVRAGLALVPEDRRQQGLALELSIARNASM
TVLGRLVKHGLISARSETQLANQWGTRLRLKAGDPNAPVGTLSGGNQQKVVLGKWLATGP
KVLIIDEPTRGIDVGAKAEVYSALAELVRDGMAVLMISSELPEVLGMADRVLVMHEGRIS
ADIARADADEERIMGAALGQPMPPLGHAA
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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