SitesBLAST
Comparing H281DRAFT_02704 FitnessBrowser__Burk376:H281DRAFT_02704 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)
43% identity, 95% coverage: 19:505/511 of query aligns to 4:491/501 of P04983
- K43 (= K58) mutation to R: Loss of transport.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
29% identity, 42% coverage: 19:234/511 of query aligns to 1:215/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F29), V16 (≠ A34), S36 (≠ N54), G37 (= G55), S38 (≠ A56), G39 (= G57), K40 (= K58), S41 (= S59), T42 (≠ S60), E162 (= E181), H194 (= H213)
- binding magnesium ion: S41 (= S59), E162 (= E181)
3c4jA Abc protein artp in complex with atp-gamma-s
30% identity, 45% coverage: 19:247/511 of query aligns to 3:238/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
30% identity, 45% coverage: 19:247/511 of query aligns to 3:238/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
30% identity, 45% coverage: 19:247/511 of query aligns to 3:238/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
30% identity, 45% coverage: 19:247/511 of query aligns to 3:238/242 of 2oljA
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
30% identity, 45% coverage: 18:247/511 of query aligns to 1:236/241 of 4u00A
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)
33% identity, 43% coverage: 13:234/511 of query aligns to 5:227/265 of P07821
- K50 (= K58) mutation to Q: Lack of activity.
- D172 (= D180) mutation to E: Lack of activity.
- E173 (= E181) mutation to A: Lack of activity.
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
28% identity, 43% coverage: 16:234/511 of query aligns to 1:229/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
28% identity, 43% coverage: 16:234/511 of query aligns to 1:229/253 of 1g9xB
7mewA E. Coli msba in complex with g247 (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 319:550/572 of 7mewA
Sites not aligning to the query:
6bppA E. Coli msba in complex with lps and inhibitor g092 (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 323:554/576 of 6bppA
Sites not aligning to the query:
- binding (2E)-3-{6-[(1S)-1-(3-amino-2,6-dichlorophenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: 168, 172, 175, 176, 179, 256, 288, 291, 292, 296
6bplA E. Coli msba in complex with lps and inhibitor g907 (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 323:554/576 of 6bplA
Sites not aligning to the query:
- binding (2E)-3-{6-[(1S)-1-(2-chloro-6-cyclopropylphenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: 154, 168, 175, 176, 179, 256, 288, 291, 292, 295, 296
8dmmA Structure of the vanadate-trapped msba bound to kdl (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 322:553/576 of 8dmmA
- binding adp orthovanadate: Y347 (≠ F29), R350 (vs. gap), S374 (≠ N54), G375 (= G55), S376 (≠ A56), G377 (= G57), K378 (= K58), S379 (= S59), T380 (≠ S60), Q420 (= Q100), L476 (vs. gap), S478 (≠ P157), G479 (≠ L158), G480 (≠ N159), H533 (= H213)
Sites not aligning to the query:
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid: 25, 79, 83, 184, 234, 239, 246, 250
7ph3A Amp-pnp bound nanodisc reconstituted msba with nanobodies, spin- labeled at position a60c (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 324:555/577 of 7ph3A
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (≠ F29), S376 (≠ N54), G377 (= G55), G379 (= G57), K380 (= K58), S381 (= S59), T382 (≠ S60), Q422 (= Q100), L478 (vs. gap), S480 (≠ P157), G482 (≠ N159), Q483 (≠ K160), H535 (= H213)
- binding magnesium ion: S381 (= S59), Q422 (= Q100)
7bcwA Structure of msba in salipro with adp vanadate (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 321:552/574 of 7bcwA
- binding adenosine-5'-diphosphate: Y346 (≠ F29), G374 (= G55), S375 (≠ A56), K377 (= K58), S378 (= S59), T379 (≠ S60), L475 (vs. gap), S477 (≠ P157), Q480 (≠ K160)
- binding magnesium ion: S378 (= S59), Q419 (= Q100)
- binding vanadate ion: S373 (≠ N54), K377 (= K58), S477 (≠ P157), A505 (= A185), H532 (= H213)
P60752 ATP-dependent lipid A-core flippase; Lipid A export ATP-binding/permease protein MsbA; Lipid flippase; EC 7.5.2.6 from Escherichia coli (strain K12) (see 7 papers)
31% identity, 45% coverage: 4:234/511 of query aligns to 326:557/582 of P60752
- E506 (= E181) mutation to Q: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
- L511 (= L186) mutation to P: Loss of ATPase activity; ATP is still bound.
- D512 (≠ Q187) mutation to G: Loss of ATPase activity; ATP is still bound.
- H537 (= H213) mutation to A: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
Sites not aligning to the query:
- 88 C→S: Does not affect ATPase activity.
- 208 E→A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates. Inhibits formation of outward-facing conformation.; E→C: Exhibits ATPase activity. Forms intermolecular cross-links.; E→Q: Improves basal ATPase activity and increases transport activity.
- 212 K→A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates.
- 270 A→T: Temperature-sensitive. Loss of lipid export to the outer membrane. Significantly decreases ATPase activity at 42 degrees Celsius but not at 30 degrees Celsius.
- 315 C→S: Does not affect ATPase activity.
7ph2A Nanodisc reconstituted msba in complex with nanobodies, spin-labeled at position a60c (see paper)
31% identity, 45% coverage: 4:234/511 of query aligns to 315:546/569 of 7ph2A
Sites not aligning to the query:
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,5-bis(oxidanyl)oxan-2-yl]oxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-4-[(3~{R})-3-nonanoyloxytetradecanoyl]oxy-5-[[(3~{R})-3-octanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{S},5~{S},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanylnonanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-oxan-2-yl]methoxy]-5-oxidanyl-oxane-2-carboxylic acid: 30, 37, 277, 282, 285
4zirA Crystal structure of ecfaa' heterodimer bound to amppnp (see paper)
29% identity, 48% coverage: 33:278/511 of query aligns to 21:243/263 of 4zirA
- binding phosphoaminophosphonic acid-adenylate ester: T42 (≠ N54), G45 (= G57), K46 (= K58), S47 (= S59), T48 (≠ S60), Q83 (≠ I98), R132 (≠ S146), F136 (≠ W150), S138 (≠ R152), G139 (≠ L153), G140 (= G154), E141 (≠ D155)
- binding magnesium ion: S47 (= S59), Q83 (≠ I98), D161 (= D180)
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)
31% identity, 43% coverage: 20:241/511 of query aligns to 394:616/1286 of P21439
- Y403 (≠ F29) 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 (≠ GAGKSS 55:60) binding
- K435 (= K58) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (= E73) to G: in dbSNP:rs1189003716
- D459 (≠ P82) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q100) binding
- P479 (≠ L102) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (= L104) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (= A140) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (vs. gap) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (≠ L158) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- G536 (≠ N159) binding ; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (≠ V164) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (= A169) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E181) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H213) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (≠ H214) 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
Query Sequence
>H281DRAFT_02704 FitnessBrowser__Burk376:H281DRAFT_02704
MTVQAEERERAPVNRSVPLLRMQGIVKSFPGVKALRGVSLELRAGHVMAIVGENGAGKSS
LVKTLSGAYEPDEGTIEIDGVPLARGTNAAIDAGVAVIYQELSLINDMTVAENLFLGRMP
ARKGFIMQREANQLAREALARVGLDSVPPWMRLGDLPLNKRQLVEVAKAIARDARILVMD
EPTAALQSQDIVNLYAVVRRLRAAGMGIIFISHHLEEVFELADSAVVMRDGATVGARPMS
EWTEAALVQAMVARNLESFYPWEPRDYGDVVLEVRNLVSAPLLRNASFKVRAGEIVGIAG
IAGAGRTELLKTIFGALPATGGEILIKGKKIANHSPTEGVRHGLVYTSEDRKLEGLVLDA
NIEENIALSSLKALANGGFVSGARKRKLARDASTRFGVRASSVLQVTRTLSGGNQQKVIL
GRATATQPVVIMLDEPTRGIDVGAKTEIYAHMVAMARAGGAVVMVSSELPELLGMSDRVL
VMYRGSIVTEIPREKAHSEAVIQWATTGAGA
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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