SitesBLAST
Comparing GFF3532 FitnessBrowser__WCS417:GFF3532 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)
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)
44% identity, 90% coverage: 18:255/263 of query aligns to 26:264/265 of P07821
- K50 (= K42) mutation to Q: Lack of activity.
- D172 (= D164) mutation to E: Lack of activity.
- E173 (= E165) mutation to A: Lack of activity.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
30% identity, 86% coverage: 3:228/263 of query aligns to 2:225/241 of 4u00A
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)
32% identity, 89% coverage: 2:235/263 of query aligns to 9:248/257 of P0AAH0
- G48 (= G41) mutation to I: Loss of phosphate transport.
- K49 (= K42) mutation to Q: Loss of phosphate transport.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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, 83% coverage: 14:230/263 of query aligns to 407:621/1286 of P21439
- GCGKST 432:437 (= GCGKST 39:44) binding
- K435 (= K42) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
- E450 (≠ Q57) to G: in dbSNP:rs1189003716
- D459 (≠ A66) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
- Q477 (= Q84) binding
- P479 (= P87) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
- L481 (≠ P89) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
- A511 (≠ V120) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
- E528 (≠ R135) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
- G535 (= G142) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
- G536 (= G143) binding ; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
- I541 (≠ A148) to F: in PFIC3 and GBD1; dbSNP:rs66904256
- A546 (≠ V153) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
- E558 (= E165) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
- H589 (= H197) to T: in GBD1; requires 2 nucleotide substitutions
- R590 (≠ D198) 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
- 403 Y → H: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol; dbSNP:rs121918443
- 406 binding ; R → Q: found in patients with cholangitis; uncertain significance; dbSNP:rs763807769
- 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
Q9JI39 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein from Mus musculus (Mouse) (see 2 papers)
33% identity, 78% coverage: 18:221/263 of query aligns to 474:678/715 of Q9JI39
- G497 (= G41) mutation to A: Decreases ATP binding about 50%.
- K498 (= K42) mutation to R: Decreases ATP binding about 50%.
- C547 (≠ V92) modified: S-glutathionyl cysteine; mutation to A: Does not affect ABCB10 glutathionylation.
- G602 (= G143) mutation to D: Affects ATP hydrolysis but not binding.; mutation to V: Affects ATP hydrolysis but not binding.
- E624 (= E165) mutation to Q: Affects ATP hydrolysis but not binding.
- C675 (≠ V218) mutation to A: Prevents ABCB10 glutathionylation.
Sites not aligning to the query:
- 1:82 modified: transit peptide, Mitochondrion
5x40A Structure of a cbio dimer bound with amppcp (see paper)
33% identity, 86% coverage: 3:228/263 of query aligns to 4:229/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y13), V18 (≠ T16), A20 (≠ I18), N40 (= N38), G41 (= G39), G43 (= G41), K44 (= K42), S45 (= S43), T46 (= T44), Q88 (= Q84), H139 (≠ A138), M140 (≠ D139), L141 (= L140), S142 (= S141), G144 (= G143), Q145 (= Q144), Q166 (≠ E165), H198 (= H197)
- binding magnesium ion: S45 (= S43), Q88 (= Q84)
4f4cA The crystal structure of the multi-drug transporter (see paper)
30% identity, 80% coverage: 18:228/263 of query aligns to 1038:1248/1250 of 4f4cA
Sites not aligning to the query:
4ayxA Structure of the human mitochondrial abc transporter, abcb10 (rod form b) (see paper)
32% identity, 78% coverage: 18:221/263 of query aligns to 356:560/571 of 4ayxA
Sites not aligning to the query:
7niwA Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
28% identity, 83% coverage: 14:230/263 of query aligns to 356:570/1140 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, 83% coverage: 14:230/263 of query aligns to 346:560/1128 of 6s7pA
Sites not aligning to the query:
- binding adenosine-5'-triphosphate: 342, 344, 345, 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
O65934 ABC transporter ATP-binding/permease protein Rv1747; EC 7.-.-.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 81% coverage: 14:226/263 of query aligns to 330:540/865 of O65934
- E479 (= E165) 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.
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
30% identity, 78% coverage: 17:222/263 of query aligns to 21:225/226 of 5xu1B
Q9NRK6 ATP-binding cassette sub-family B member 10, mitochondrial; ABC-mitochondrial erythroid protein; ABC-me protein; ATP-binding cassette transporter 10; ABC transporter 10 protein; Mitochondrial ATP-binding cassette 2; M-ABC2 from Homo sapiens (Human) (see 5 papers)
32% identity, 78% coverage: 18:221/263 of query aligns to 509:713/738 of Q9NRK6
- K533 (= K42) mutation to E: Increases hemoglobin biosynthetic process.
- D545 (≠ K54) to N: in dbSNP:rs35698797
- C582 (≠ V92) mutation to G: Does not affect ATPase activity; when associated with S-215 and L-224. Activated by Zn (II) mesoporphyrin; when associated with S-215 and L-224.
- S635 (= S141) mutation to R: Does not rescue hemoglobin and heme biosynthetic process.
- Q638 (= Q144) mutation to H: Does not rescue hemoglobin and heme biosynthetic process.
- D658 (= D164) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
- E659 (= E165) mutation to A: Does not rescue hemoglobin and heme biosynthetic process.
Sites not aligning to the query:
- 150 A → S: in dbSNP:rs4148756
- 215 C→S: Does not affect ATPase activity; when associated with L-224 and G-582. Activated by Zn (II) mesoporphyrin; when associated with L-224 and G-582.
- 224 C→L: Does not affect ATPase activity; when associated withS-215 and G-582. Activated by Zn (II) mesoporphyrin; when associated with S-215 and G-582.
- 471 R → T: in a breast cancer sample; somatic mutation
8hf4A Cryo-em structure of nucleotide-bound coma at outward-facing state with ec gate closed conformation (see paper)
31% identity, 80% coverage: 12:221/263 of query aligns to 340:545/563 of 8hf4A
Sites not aligning to the query:
2ixfA Crystal structure of the atpase domain of tap1 with atp (d645q, q678h mutant) (see paper)
33% identity, 79% coverage: 15:221/263 of query aligns to 30:237/255 of 2ixfA
- binding adenosine-5'-triphosphate: V33 (≠ I18), N53 (= N38), G54 (= G39), S55 (≠ C40), G56 (= G41), K57 (= K42), S58 (= S43), T59 (= T44), N154 (≠ A138), S157 (= S141), G159 (= G143), Q160 (= Q144), H214 (= H197)
Sites not aligning to the query:
6q81A Structure of p-glycoprotein(abcb1) in the post-hydrolytic state (see paper)
30% identity, 83% coverage: 17:234/263 of query aligns to 372:582/1182 of 6q81A
Sites not aligning to the query:
7otgA Structure of abcb1/p-glycoprotein in the presence of the cftr potentiator ivacaftor (see paper)
30% identity, 83% coverage: 17:234/263 of query aligns to 372:582/1179 of 7otgA
Sites not aligning to the query:
1jj7A Crystal structure of thE C-terminal atpase domain of human tap1 (see paper)
32% identity, 80% coverage: 18:227/263 of query aligns to 29:239/251 of 1jj7A
Sites not aligning to the query:
4xwkA P-glycoprotein co-crystallized with bde-100 (see paper)
30% identity, 83% coverage: 17:234/263 of query aligns to 375:585/1182 of 4xwkA
Sites not aligning to the query:
7zdaC If(apo/asym) conformation of cyddc in adp+pi(cydc)/atp(cydd) bound state (dataset-2) (see paper)
29% identity, 79% coverage: 19:227/263 of query aligns to 356:560/572 of 7zdaC
Sites not aligning to the query:
Query Sequence
>GFF3532 FitnessBrowser__WCS417:GFF3532
MSILQARELDIGYGTTRIVQGLSFVPPTGKVTALIGPNGCGKSTLLKAFARILKPTQGEL
TLDGHAYTSLSARQLARQIAFLPQVLPVPEGVSVRQLVAYGRSPHNSLWGRLSGNDQAHV
TQAMQRLELDTLADRALADLSGGQRQRAWLAMVLAQNAPVVLLDEPTTYLDISHQVELLD
LMGELAGEGKTVITVLHDINQACRYAHHLAVMHGGKLVADGAPGQVITAELMRQVFEVQV
QVMSEPVAGTPMCLIKKSTRPHT
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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