SitesBLAST
Comparing Pf1N1B4_410 L-arabinose transport ATP-binding protein AraG (TC 3.A.1.2.2) 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)
46% identity, 95% coverage: 16:504/514 of query aligns to 5:492/501 of P04983
- K43 (= K54) mutation to R: Loss of transport.
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
33% identity, 40% coverage: 31:238/514 of query aligns to 25:232/233 of P75957
- G42 (= G48) mutation to D: Loss of lipoprotein release when overexpressed.
7mdyC Lolcde nucleotide-bound
33% identity, 39% coverage: 31:230/514 of query aligns to 22:221/226 of 7mdyC
- binding adp orthovanadate: G42 (= G51), S43 (≠ A52), G44 (= G53), K45 (= K54), S46 (= S55), T47 (= T56), Q91 (= Q97), H138 (≠ E147), E142 (≠ R151), S144 (= S153), G145 (≠ L154), G146 (= G155), E168 (= E177), N172 (≠ S181), H201 (= H209)
- binding magnesium ion: S46 (= S55), Q91 (= Q97)
Sites not aligning to the query:
7arlD Lolcde in complex with lipoprotein and adp (see paper)
33% identity, 39% coverage: 31:230/514 of query aligns to 22:221/222 of 7arlD
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
33% identity, 42% coverage: 16:231/514 of query aligns to 5:223/648 of P75831
- K47 (= K54) mutation to L: Lack of activity.
- D169 (= D176) mutation to N: Lack of activity.
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
32% identity, 39% coverage: 31:230/514 of query aligns to 24:223/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: S43 (≠ N50), G44 (= G51), G46 (= G53), K47 (= K54), S48 (= S55), T49 (= T56), Q93 (= Q97), R137 (≠ D144), H140 (≠ E147), E144 (≠ R151), S146 (= S153), G148 (= G155), E149 (≠ Q156), H203 (= H209)
- binding magnesium ion: S48 (= S55), Q93 (= Q97)
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
30% identity, 42% coverage: 16:231/514 of query aligns to 2:225/232 of 1f3oA
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
30% identity, 41% coverage: 19:230/514 of query aligns to 5:215/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F25), V16 (≠ A30), S36 (≠ N50), G37 (= G51), S38 (≠ A52), G39 (= G53), K40 (= K54), S41 (= S55), T42 (= T56), E162 (= E177), H194 (= H209)
- binding magnesium ion: S41 (= S55), E162 (= E177)
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
30% identity, 42% coverage: 16:231/514 of query aligns to 2:225/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F25), S40 (≠ N50), G41 (= G51), S42 (≠ A52), G43 (= G53), K44 (= K54), S45 (= S55), T46 (= T56), F138 (≠ D144), Q145 (≠ R151), S147 (= S153), G149 (= G155), Q150 (= Q156), H204 (= H209)
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)
31% identity, 43% coverage: 12:230/514 of query aligns to 390:609/1286 of P21439
- Y403 (≠ F25) 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 51:56) binding
- K435 (= K54) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (≠ S69) to G: in dbSNP:rs1189003716
- D459 (≠ Q77) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q97) binding
- P479 (≠ L99) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (= L101) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (= A132) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (= E147) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (≠ L154) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- G536 (= G155) binding ; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (≠ V160) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (= A165) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E177) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H209) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (= R210) 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
6s7pA Nucleotide bound abcb4 (see paper)
30% identity, 43% coverage: 12:230/514 of query aligns to 329:548/1128 of 6s7pA
- binding adenosine-5'-triphosphate: Y342 (≠ F25), S344 (vs. gap), R345 (vs. gap), G371 (= G51), G373 (= G53), K374 (= K54), S375 (= S55), Q416 (= Q97), Q471 (≠ R151), S473 (= S153), G475 (= G155), Q476 (= Q156)
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
7niwA Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
30% identity, 43% coverage: 12:230/514 of query aligns to 339:558/1140 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
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 46% coverage: 14:250/514 of query aligns to 2:235/371 of P68187
- A85 (≠ H100) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A132) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L133) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ C135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A140) 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.
- R228 (≠ Q243) 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, 46% coverage: 14:250/514 of query aligns to 1:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F25), S37 (≠ N50), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), Q81 (= Q97), R128 (≠ P145), A132 (≠ V149), S134 (= S153), G136 (= G155), Q137 (= Q156), E158 (= E177), H191 (= H209)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
30% identity, 46% coverage: 14:250/514 of query aligns to 1:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F25), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ P145), S134 (= S153), Q137 (= Q156)
- binding beryllium trifluoride ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (= S153), G136 (= G155), H191 (= H209)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
30% identity, 46% coverage: 14:250/514 of query aligns to 1:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ P145), A132 (≠ V149), S134 (= S153), Q137 (= Q156)
- binding tetrafluoroaluminate ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (= S153), G135 (≠ L154), G136 (= G155), E158 (= E177), H191 (= H209)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
30% identity, 46% coverage: 14:250/514 of query aligns to 1:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (≠ P145), A132 (≠ V149), S134 (= S153), Q137 (= Q156)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
30% identity, 46% coverage: 14:250/514 of query aligns to 1:234/374 of 2awnB
5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
29% identity, 42% coverage: 16:230/514 of query aligns to 5:222/650 of 5ws4A
O65934 ABC transporter ATP-binding/permease protein Rv1747; EC 7.-.-.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
32% identity, 43% coverage: 9:227/514 of query aligns to 313:528/865 of O65934
- E479 (= E177) mutation to Q: Loss of ATPase activity.
Sites not aligning to the query:
- 33 R→A: Strong decrease in phosphorylation.
- 47 S→A: Strong decrease in phosphorylation. Lack of interaction with PknF. Attenuates growth in macrophages.
- 69 N→A: Strong decrease in phosphorylation.
- 152 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-210.
- 210 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-152.
- 234 R→A: Strong decrease in phosphorylation.
- 248 S→A: Strong decrease in phosphorylation. Decreases interaction with PknF.
- 270 N→A: Strong decrease in phosphorylation.
Query Sequence
>Pf1N1B4_410 L-arabinose transport ATP-binding protein AraG (TC 3.A.1.2.2)
MHAHVQTQEQRIGGSLRFNGIGKTFPGVKALDGISFVAHPGQVHALMGENGAGKSTLLKI
LGGAYTPSSGDLQIGEQKRIFKSTADSIGSGVAVIHQELHLVPEMTVAENLFLGHLPASF
GLINRGVLRQQALACLKGLADEIDPQEKVGRLSLGQRQLVEIAKALSRGAHVIAFDEPTS
SLSAREIDRLMAIIGRLRDEGKVVLYVSHRMEEVFRICNAVTVFKDGRFVRTFEDMSALT
HDQLVTCMVGRDIQDIYDYRSRPRGAVALKVDGLLGPGLREPVSFEAHKGEILGLFGLVG
AGRTELFRMLSGLTRNTAGRLELRGRELKLHSPRDAIAAGILLCPEDRKKEGILPLASVA
ENINISARGAHSTFGCLLRGLWEKDNADKQIKALKVKTPNAAQKIMYLSGGNQQKAILGR
WLSMPMKVLLLDEPTRGIDIGAKAEIYQIIHNLAASGIAVIVVSSDLMEVMGISDRILVL
CEGAMRGELTREQANESNLLQLALPRQRVADVAN
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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