SitesBLAST
Comparing GFF2162 FitnessBrowser__WCS417:GFF2162 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)
44% identity, 99% coverage: 4:496/500 of query aligns to 3:494/501 of P04983
- K43 (= K44) mutation to R: Loss of transport.
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
35% identity, 43% coverage: 6:222/500 of query aligns to 5:224/648 of P75831
- K47 (= K44) mutation to L: Lack of activity.
- D169 (= D166) mutation to N: Lack of activity.
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
28% identity, 44% coverage: 2:220/500 of query aligns to 1:229/254 of 1g6hA
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
29% identity, 43% coverage: 6:221/500 of query aligns to 2:225/232 of 1f3oA
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
30% identity, 46% coverage: 1:228/500 of query aligns to 1:232/233 of P75957
- G42 (= G38) mutation to D: Loss of lipoprotein release when overexpressed.
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
28% identity, 44% coverage: 2:220/500 of query aligns to 1:229/253 of 1g9xB
7mdyC Lolcde nucleotide-bound
32% identity, 40% coverage: 21:218/500 of query aligns to 22:219/226 of 7mdyC
- binding adp orthovanadate: G42 (= G41), S43 (≠ A42), G44 (= G43), K45 (= K44), S46 (= S45), T47 (= T46), Q91 (= Q87), H138 (≠ E137), E142 (≠ R141), S144 (= S143), G145 (≠ L144), G146 (= G145), E168 (= E167), N172 (≠ S171), H201 (= H199)
- binding magnesium ion: S46 (= S45), Q91 (= Q87)
Sites not aligning to the query:
7arlD Lolcde in complex with lipoprotein and adp (see paper)
32% identity, 40% coverage: 21:218/500 of query aligns to 22:219/222 of 7arlD
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
28% identity, 42% coverage: 9:220/500 of query aligns to 5:215/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F15), V16 (≠ A20), S36 (≠ N40), G37 (= G41), S38 (≠ A42), G39 (= G43), K40 (= K44), S41 (= S45), T42 (= T46), E162 (= E167), H194 (= H199)
- binding magnesium ion: S41 (= S45), E162 (= E167)
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
28% identity, 43% coverage: 6:221/500 of query aligns to 2:225/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F15), S40 (≠ N40), G41 (= G41), S42 (≠ A42), G43 (= G43), K44 (= K44), S45 (= S45), T46 (= T46), F138 (≠ D134), Q145 (≠ R141), S147 (= S143), G149 (= G145), Q150 (= Q146), H204 (= H199)
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
32% identity, 40% coverage: 21:218/500 of query aligns to 24:221/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: S43 (≠ N40), G44 (= G41), G46 (= G43), K47 (= K44), S48 (= S45), T49 (= T46), Q93 (= Q87), R137 (≠ D134), H140 (≠ E137), E144 (≠ R141), S146 (= S143), G148 (= G145), E149 (≠ Q146), H203 (= H199)
- binding magnesium ion: S48 (= S45), Q93 (= Q87)
Sites not aligning to the query:
P21439 Phosphatidylcholine translocator ABCB4; ATP-binding cassette sub-family B member 4; Multidrug resistance protein 3; P-glycoprotein 3; EC 7.6.2.1 from Homo sapiens (Human) (see 22 papers)
28% identity, 42% coverage: 6:217/500 of query aligns to 394:606/1286 of P21439
- Y403 (≠ F15) to H: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol; dbSNP:rs121918443
- R406 (vs. gap) binding ; to Q: found in patients with cholangitis; uncertain significance; dbSNP:rs763807769
- GCGKST 432:437 (≠ GAGKST 41:46) binding
- K435 (= K44) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (≠ S59) to G: in dbSNP:rs1189003716
- D459 (≠ Q67) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q87) binding
- P479 (≠ L89) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (= L91) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (= A122) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (= E137) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (≠ L144) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- G536 (= G145) binding ; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (≠ V150) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (= A155) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E167) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H199) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (= R200) to Q: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs45575636
Sites not aligning to the query:
- 34 modified: Phosphothreonine; T → M: in GBD1; reduces efflux activity for PC in a phosphorylation-dependent manner; dbSNP:rs142794414; T→D: Does not inhibit efflux activity for PC.
- 44 T→A: Reduces efflux activity for PC. Does not alter apical membrane location.
- 47 R → G: in GBD1; partly retained intracellularly; reduces efflux activity for PC in a phosphorylation-dependent manner; R → Q: found in patients with cholangitis; uncertain significance; dbSNP:rs372685632
- 49 S→A: Reduces efflux activity for PC. Does not alter apical membrane location.
- 68 G → R: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression; dbSNP:rs1343667900
- 73 L → V: in PFIC3 and GBD1; dbSNP:rs8187788
- 87 natural variant: D -> E
- 95 P → S: in dbSNP:rs377268767
- 175 T → A: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs58238559
- 201 T → M: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs753318087
- 238 L → V: in dbSNP:rs45596335
- 263 I → V: in dbSNP:rs45547936
- 286 A → V: in PFIC3 and GBD1; does not alter plasma membrane location; inhibits efflux activity for PC; dbSNP:rs765478923
- 320 S → F: in ICP3, GBD1 and PFIC3; uncertain significance; does not alter plasma membrane location; does not inhibit efflux activity for PC; dbSNP:rs72552778
- 367 I → V: in dbSNP:rs1168923653
- 651 T → N: in dbSNP:rs45476795
- 652 R → G: in dbSNP:rs2230028
- 726 P → L: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs141677867
- 742 natural variant: G -> S
- 764 I → L: in a heterozygous patient with risperidone-induced cholestasis
- 775 T → M: found in patients with cholangitis; uncertain significance; dbSNP:rs148052192
- 788 R → Q: in GBD1; benign; dbSNP:rs8187801
- 934 A → T: found in patients with gallbladder and cholestasis; uncertain significance; dbSNP:rs61730509
- 953 A→D: Accumulates predominantly in intracellular compartments with only a small fraction at the plasma membrane and inhibits partially the efflux activity for PC.
- 964 V → T: found in patients with cholangitis; uncertain significance; requires 2 nucleotide substitutions
- 978 S → P: in PFIC3; alters efflux activity for PC; dbSNP:rs1051861187
- 985 V→M: Significantly reduces phosphatidylcholine floppase activity; when associated with Q-989 and V-990.
- 989 H→Q: Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and V-990.
- 990 A→V: Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and Q-989.
- 1046 binding
- 1071:1077 binding
- 1075 K→M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- 1082 L → Q: in a heterozygous patient with amoxicillin/clavulanic acid-induced cholestasis; dbSNP:rs1214110864
- 1124 binding
- 1125 E → K: in PFIC3; alters efflux activity for PC
- 1168 P → S: in GBD1; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs121918442
- 1183 S → L: in GBD1; severely reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- 1184:1186 binding
- 1185 G → S: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
30% identity, 47% coverage: 4:240/500 of query aligns to 1:234/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 47% coverage: 4:240/500 of query aligns to 2:235/371 of P68187
- A85 (≠ H90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ K120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ C125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A130) 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 (≠ Q233) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
30% identity, 47% coverage: 4:240/500 of query aligns to 1:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F15), S37 (≠ N40), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), Q81 (= Q87), R128 (≠ E137), A132 (≠ R141), S134 (= S143), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H199)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
30% identity, 47% coverage: 4:240/500 of query aligns to 1:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F15), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ E137), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q87), S134 (= S143), G136 (= G145), H191 (= H199)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
30% identity, 47% coverage: 4:240/500 of query aligns to 1:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A20), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ E137), A132 (≠ R141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q87), S134 (= S143), G135 (≠ L144), G136 (= G145), E158 (= E167), H191 (= H199)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
30% identity, 47% coverage: 4:240/500 of query aligns to 1:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A20), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ E137), A132 (≠ R141), S134 (= S143), Q137 (= Q146)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
7niwA Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
28% identity, 42% coverage: 6:217/500 of query aligns to 343:555/1140 of 7niwA
Sites not aligning to the query:
- binding cholesterol: 70, 152, 160, 266, 641, 645, 648, 839
- binding 1,2-dilinoleoyl-sn-glycero-3-phosphocholine: 173, 183, 250, 254, 257, 261, 286, 294, 298, 617, 882
- binding posaconazole: 250, 291, 294, 658, 661, 726, 841, 871, 874, 878, 882
6s7pA Nucleotide bound abcb4 (see paper)
28% identity, 42% coverage: 6:217/500 of query aligns to 333:545/1128 of 6s7pA
- binding adenosine-5'-triphosphate: Y342 (≠ F15), S344 (vs. gap), R345 (vs. gap), G371 (= G41), G373 (= G43), K374 (= K44), S375 (= S45), Q416 (= Q87), Q471 (≠ R141), S473 (= S143), G475 (= G145), Q476 (= Q146)
Sites not aligning to the query:
- binding adenosine-5'-triphosphate: 920, 922, 923, 948, 949, 951, 952, 953, 954, 994, 1033, 1053, 1054, 1056
- binding cholesterol: 25, 32, 35, 65, 824, 834, 834, 838
- binding magnesium ion: 953, 994
Query Sequence
>GFF2162 FitnessBrowser__WCS417:GFF2162
MTAAALRFDGIGKTFPGVKALDGISFSAHPGQVHALMGENGAGKSTLLKILGGAYIPNSG
TLHIGEQVMAFKSAADSIASGVAVIHQELHLVPEMSVAENLFLGHLPSRFGVVNRGLLRK
QALACLKGLADEIDPAEKLGRLSLGQRQLVEIAKALSRGAHVIAFDEPTSSLSAREIDRL
MAIIARLRDEGKVVLYVSHRMEEVFRICNAVTVFKDGRYVRTFEDMSALTHDQLVTCMVG
RDIQDIYDYRPREHGEVALKVDGLLGPGLREPVSFNVRKGEILGLFGLVGAGRTELFRLL
SGLERASAGQLELCGEPLHLQSPRDAIAAGVLLCPEDRKKEGIIPLSSVAENINISARGA
HSTFGWLLREGWEKGNADQQINAMKVKTPNAAQKIMYLSGGNQQKSILGRWLSMPMKVLL
LDEPTRGIDIGAKAEIYQIIHNLAAQGIAVIVVSSDLMEVMGIADRILVLCEGALRGEQT
REHATESNLLQLALPRSVAN
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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