SitesBLAST
Comparing WP_082126415.1 NCBI__GCF_001013305.1:WP_082126415.1 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)
P0AAH0 Phosphate import ATP-binding protein PstB; ABC phosphate transporter; Phosphate-transporting ATPase; EC 7.3.2.1 from Escherichia coli (strain K12) (see paper)
56% identity, 90% coverage: 29:283/283 of query aligns to 4:257/257 of P0AAH0
- G48 (= G73) mutation to I: Loss of phosphate transport.
- K49 (= K74) mutation to Q: Loss of phosphate transport.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
35% identity, 86% coverage: 36:278/283 of query aligns to 3:236/241 of 4u00A
3c4jA Abc protein artp in complex with atp-gamma-s
35% identity, 84% coverage: 45:282/283 of query aligns to 13:242/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
35% identity, 84% coverage: 45:282/283 of query aligns to 13:242/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
35% identity, 84% coverage: 45:282/283 of query aligns to 13:242/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
35% identity, 84% coverage: 45:282/283 of query aligns to 13:242/242 of 2oljA
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
35% identity, 85% coverage: 40:279/283 of query aligns to 6:237/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y45), V16 (≠ A50), S36 (= S70), G37 (= G71), S38 (≠ C72), G39 (= G73), K40 (= K74), S41 (= S75), T42 (= T76), E162 (= E205), H194 (= H236)
- binding magnesium ion: S41 (= S75), E162 (= E205)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
34% identity, 76% coverage: 63:278/283 of query aligns to 54:263/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
34% identity, 76% coverage: 63:278/283 of query aligns to 54:263/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 81% coverage: 49:278/283 of query aligns to 19:241/343 of P30750
- 40:46 (vs. 70:76, 86% identical) binding ATP
- E166 (= E205) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
7ahdC Opua (e190q) occluded (see paper)
35% identity, 76% coverage: 63:278/283 of query aligns to 54:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S70), G62 (= G71), G64 (= G73), K65 (= K74), S66 (= S75), T67 (= T76), Q111 (= Q123), K161 (≠ D175), Q162 (≠ S176), S164 (= S181), G166 (= G183), M167 (≠ Q184), Q188 (≠ E205), H221 (= H236)
Sites not aligning to the query:
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
33% identity, 81% coverage: 49:278/283 of query aligns to 20:242/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: S41 (= S70), G42 (= G71), A43 (≠ C72), G44 (= G73), K45 (= K74), S46 (= S75), T47 (= T76), N141 (≠ A179), S143 (= S181), Q146 (= Q184), H200 (= H236)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
33% identity, 81% coverage: 49:278/283 of query aligns to 20:242/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
33% identity, 81% coverage: 49:278/283 of query aligns to 20:242/344 of 3tuiC
Sites not aligning to the query:
P02915 Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP; EC 7.4.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 87% coverage: 35:280/283 of query aligns to 6:255/258 of P02915
- S41 (= S70) binding ATP
- G42 (= G71) binding ATP
- G44 (= G73) binding ATP
- K45 (= K74) binding ATP
- S46 (= S75) binding ATP
- T47 (= T76) binding ATP
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
34% identity, 87% coverage: 35:280/283 of query aligns to 2:251/258 of 1b0uA
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)
33% identity, 83% coverage: 30:265/283 of query aligns to 388:617/1286 of P21439
- Y403 (= Y45) 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 ATP; to Q: found in patients with cholangitis; uncertain significance; dbSNP:rs763807769
- GCGKST 432:437 (= GCGKST 71:76) binding ATP
- K435 (= K74) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (= E94) to G: in dbSNP:rs1189003716
- D459 (= D103) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q123) binding ATP
- P479 (= P125) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (≠ P127) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (≠ L165) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (≠ D175) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (= G182) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs1810849139
- G536 (= G183) binding ATP; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (≠ L188) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (= A193) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E205) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H236) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (≠ S237) 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 ATP
- 1071:1077 binding ATP
- 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 ATP
- 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 ATP
- 1185 G → S: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
5x40A Structure of a cbio dimer bound with amppcp (see paper)
34% identity, 80% coverage: 44:268/283 of query aligns to 14:230/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y44), V18 (≠ K48), A20 (= A50), N40 (≠ S70), G41 (= G71), G43 (= G73), K44 (= K74), S45 (= S75), T46 (= T76), Q88 (= Q123), H139 (≠ T178), M140 (≠ A179), L141 (= L180), S142 (= S181), G144 (= G183), Q145 (= Q184), Q166 (≠ E205), H198 (= H236)
- binding magnesium ion: S45 (= S75), Q88 (= Q123)
7niwA Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
32% identity, 83% coverage: 30:265/283 of query aligns to 337:566/1140 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)
32% identity, 83% coverage: 30:265/283 of query aligns to 327:556/1128 of 6s7pA
- binding adenosine-5'-triphosphate: Y342 (= Y45), S344 (vs. gap), R345 (vs. gap), G371 (= G71), G373 (= G73), K374 (= K74), S375 (= S75), Q416 (= Q123), Q471 (≠ A179), S473 (= S181), G475 (= G183), Q476 (= Q184)
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
>WP_082126415.1 NCBI__GCF_001013305.1:WP_082126415.1
MHSELNPPTEPGSPLADQTQVGAPSAENVESAKVKMRARDVSVYYGNKKAIDEVSVDVFS
EYVTAFIGPSGCGKSTFLRALNRMNDTIPSARVEGTIELDGEDIYSSGMDVVQLRARVGM
VFQKPNPFPKSIYDNVAYGPKIHGLAEGKTELDAIVEKSLTRAGLWEEVKDRLQDSGTAL
SGGQQQRLCIARAIAVDPEVILMDEPCSALDPIATARIEELIDDLRGRYAIVIVTHSMQQ
AARVSQRTAFFHLGHLVEYGHTSDIFTNPKQQRTQDYITGRYG
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