SitesBLAST
Comparing GFF2651 FitnessBrowser__Phaeo:GFF2651 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
33% identity, 95% coverage: 12:509/522 of query aligns to 1:494/501 of P04983
- K43 (= K54) mutation to R: Loss of transport.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 41% coverage: 18:230/522 of query aligns to 6:220/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 41% coverage: 18:230/522 of query aligns to 6:220/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 41% coverage: 18:230/522 of query aligns to 6:220/353 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)
34% identity, 41% coverage: 18:230/522 of query aligns to 6:220/353 of Q97UY8
- S142 (≠ T153) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G155) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E177) 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+).
6xjhC Pmtcd abc exporter without the basket domain at c2 symmetry (see paper)
29% identity, 42% coverage: 16:232/522 of query aligns to 1:201/219 of 6xjhC
- binding phosphothiophosphoric acid-adenylate ester: Y10 (≠ F25), V15 (≠ A30), N35 (= N50), G36 (= G51), G38 (= G53), K39 (= K54), T40 (= T55), T41 (= T56), K115 (≠ A147), K119 (≠ R151), S121 (≠ T153)
- binding magnesium ion: T40 (= T55), E70 (≠ Q97)
6xjiC Pmtcd abc exporter at c1 symmetry (see paper)
29% identity, 42% coverage: 16:232/522 of query aligns to 1:201/290 of 6xjiC
- binding phosphothiophosphoric acid-adenylate ester: Y10 (≠ F25), V15 (≠ A30), N35 (= N50), G36 (= G51), G38 (= G53), K39 (= K54), T40 (= T55), T41 (= T56), K115 (≠ A147), K119 (≠ R151), S121 (≠ T153)
- binding magnesium ion: T40 (= T55), E70 (≠ Q97)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
31% identity, 41% coverage: 16:229/522 of query aligns to 7:221/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 3:211/374 of 2awnB
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
34% identity, 42% coverage: 15:232/522 of query aligns to 5:226/233 of P75957
- G42 (= G48) mutation to D: Loss of lipoprotein release when overexpressed.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 41% coverage: 16:229/522 of query aligns to 4:212/369 of P19566
- L86 (= L101) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P178) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ S187) 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.
7mdyC Lolcde nucleotide-bound
34% identity, 42% coverage: 15:232/522 of query aligns to 2:223/226 of 7mdyC
- binding adp orthovanadate: Y12 (≠ F25), G42 (= G51), S43 (≠ A52), G44 (= G53), K45 (= K54), S46 (≠ T55), T47 (= T56), Q91 (= Q97), H138 (≠ A147), E142 (≠ R151), S144 (≠ T153), G145 (≠ V154), G146 (= G155), E168 (= E177), N172 (≠ V181), H201 (= H209)
- binding magnesium ion: S46 (≠ T55), Q91 (= Q97)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 3:211/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F25), S37 (≠ N50), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q97), R128 (≠ A147), A132 (≠ R151), S134 (≠ T153), G136 (= G155), Q137 (≠ E156), E158 (= E177), H191 (= H209)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q97)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 3:211/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F25), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A147), S134 (≠ T153), Q137 (≠ E156)
- binding beryllium trifluoride ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (≠ T153), G136 (= G155), H191 (= H209)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q97)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 3:211/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A147), A132 (≠ R151), S134 (≠ T153), Q137 (≠ E156)
- binding tetrafluoroaluminate ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (≠ T153), G135 (≠ V154), G136 (= G155), E158 (= E177), H191 (= H209)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q97)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 3:211/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A147), A132 (≠ R151), S134 (≠ T153), Q137 (≠ E156)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q97)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 41% coverage: 16:229/522 of query aligns to 4:212/371 of P68187
- A85 (≠ T100) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I132) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L135) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E137) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K142) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G155) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D176) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
31% identity, 41% coverage: 16:229/522 of query aligns to 1:209/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F25), S35 (≠ N50), G36 (= G51), C37 (≠ A52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (≠ A147), A130 (≠ R151), S132 (≠ T153), G134 (= G155), Q135 (≠ E156)
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
34% identity, 42% coverage: 15:232/522 of query aligns to 4:225/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: V23 (vs. gap), S43 (≠ N50), G44 (= G51), G46 (= G53), K47 (= K54), S48 (≠ T55), T49 (= T56), Q93 (= Q97), R137 (vs. gap), H140 (≠ A147), E144 (≠ R151), S146 (≠ T153), G148 (= G155), E149 (= E156), H203 (= H209)
- binding magnesium ion: S48 (≠ T55), Q93 (= Q97)
7arlD Lolcde in complex with lipoprotein and adp (see paper)
34% identity, 42% coverage: 15:231/522 of query aligns to 2:222/222 of 7arlD
Query Sequence
>GFF2651 FitnessBrowser__Phaeo:GFF2651
MASDKMGQAPGLTPVLRLQNITKRFGSVTANDDVSFDLFPGEVIALLGENGAGKTTLMNI
LFGQYMADTGGVELFGAPLPPGAPRAALDGGVGMVHQHFTLADNLTVWENITLGVEPLLG
LGLRAGPAKARIRALAEQFHLKVDPNAKVSRLTVGERQRVEILKALYRDARILILDEPTA
VLTPQESDALFATLREAINRGLSVIFISHKLHEVMAISDRVLVLRHGKLVAERQTADTDS
DALAALMVGADVVPAKFAANTPGPALLQLRDVTTPSAGASPGLRHVSLDLAAGQITGLAG
VSGNGQAALSDLVSGLITPQSGSLTLNGAAPAGWSPREAITAGIARIPEDRHKTGTIADF
DLTENAILETYATRFSHRGWLDWRAARDFAKTVITGYDVRCPGPDTRIRLLSGGNMQKLI
LGRVLEQSPQIILANQPVRGLDIGAVTYVHEQLAKACARGAAVLLISEDLDEIMQLSDVI
HVISEGRLSPGFARGSKQPEELGAWMAGHGFDTPQTEDGHAA
Or try a new SitesBLAST search
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