SitesBLAST

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)
31% identity, 48% coverage: 4:247/504 of query aligns to 11:246/265 of P07821

query
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P07821

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K50 (= K43) mutation to Q: Lack of activity.
D172 (= D165) mutation to E: Lack of activity.
E173 (= E166) mutation to A: Lack of activity.

7niwA Nanodisc reconstituted human abcb4 in complex with 4b1-fab (posaconazole-bound, inward-open conformation) (see paper)
27% identity, 57% coverage: 1:286/504 of query aligns to 339:629/1140 of 7niwA

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binding 1,2-dilinoleoyl-sn-glycero-3-phosphocholine: F617 (= F274)

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, 882
binding posaconazole: 250, 291, 294, 658, 661, 726, 841, 871, 874, 878, 882

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)
30% identity, 48% coverage: 1:242/504 of query aligns to 390:637/1286 of P21439

query
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P21439

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Y403 (≠ F14) 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 (≠ GAGKST 40:45) binding ATP
K435 (= K43) mutation to M: Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.
E450 (≠ S58) to G: in dbSNP:rs1189003716
D459 (≠ E67) to H: in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression
Q477 (= Q86) binding ATP
P479 (≠ Q89) to L: in PFIC3; greatly reduced expression; alters efflux activity for PC; dbSNP:rs748657435
L481 (≠ V91) to R: in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol
A511 (≠ V121) to T: in PFIC3 and GBD1; dbSNP:rs1257887155
E528 (≠ L138) to D: in GBD1; uncertain significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location; dbSNP:rs8187797
G535 (≠ I143) to D: in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location
G536 (≠ A144) binding ATP; to R: in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location
I541 (≠ V149) to F: in PFIC3 and GBD1; dbSNP:rs66904256
A546 (= A154) to D: in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface; dbSNP:rs121918441
E558 (= E166) mutation to Q: Loss of floppase activity. Strongly reduce the ATPase activity.
H589 (= H198) to T: in GBD1; requires 2 nucleotide substitutions
R590 (= R199) 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

Q00748 Multidrug resistance protein homolog 65; P-glycoprotein 65; EC 7.6.2.2 from Drosophila melanogaster (Fruit fly) (see paper)
27% identity, 44% coverage: 15:237/504 of query aligns to 1072:1295/1302 of Q00748

query
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Q00748

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D

N

G

G

R

Q

K

V

V

V

A

E

S

Q

H

G

P

N

S

H

L

M

E

Q

G

L

V

I

S

S

R

Q

D

G

T

G

I

I

V

Y

S

A

E

K

M

L

Sites not aligning to the query:

103 modified: carbohydrate, N-linked (GlcNAc...) asparagine

P34358 ABC transporter ced-7; Cell death protein 7 from Caenorhabditis elegans (see 2 papers)
32% identity, 42% coverage: 9:221/504 of query aligns to 550:758/1704 of P34358

query
sites
P34358

N

N

I

L

G

V

K

K

V

I

F

W

-

S

-

T

P

T

G

G

V

E

R

R

A

A

L

V

D

D

G

G

I

L

S

S

F

L

D

R

V

A

H

V

A

R

G

G

Q

Q

V

C

H

S

G

I

L

L

M

L

G

G

E

H

N

N

G

G

A

A

G

G

K
|
K

S

S

T

T

L

T

L

F

K

S

I

S

L

I

G

A

G

G

E

I

Y

I

Q

R

P

P

D

T

S

N

G

G

R

R

V

I

L

T

I

I

D

C

E

G

N

Y

E

D

V

V

R

-

F

-

A

G

N

N

A

E

G

P

A

G

S

E

I

T

A

R

G

H

I

I

A

G

V

M

I

C

H

P

Q

Q

E

Y

L

N

Q

P

Y

L

V

Y

P

D

D

Q

L

L

T

T

V

V

S

S

E
|
E

N

H

L

L

L

-

G

-

R

K

L

L

P

V

N

Y

T

G

I

L

G

K

F

G

V

A

K

R

K

E

G

K

D

D

A

F

K

K

R

Q

F

D

V

M

R

K

E

R

Q

L

L

L

A

S

A

D

M

V

G

K

V

L

D

D

L

F

D

K

P

E

N

N

A

E

K

K

L

A

R

V

K

N

L

L

S

S

I

G

A

G

Q

M

R

K

Q

R

M

K

V

L

E

C

I

V

C

C

K

M

A

A

L

L

M

I

R

G

N

D

A

S

R

E

V

V

I

V

A

L

L

L

D

D

E

E

P

P

T

T

S

A

S

G

L

M

S

D

H

P

R

G

E

A

T

R

E

Q

V

D

L

V

F

Q

K

K

L

L

V

V

R

E

D

R

L

E

R

K

A

A

D

-

N

N

R

R

A

T

L

I

I

L

Y

L

I

T

S

T

H

H

R

Y

M

M

D

D

E

E

I

A

Y

E

Q

R

L

L

C

G

D

D

A

W

C

V

T

F

I

I

F

M

R

S

D

H

G

G

R

K

K

L

V

V

A

A

S

S

K586 (= K43) mutation to R: Cell corpses not engulfed.
E639 (= E98) mutation to G: Cell corpses not engulfed.

Sites not aligning to the query:

126 modified: carbohydrate, N-linked (GlcNAc...) asparagine
1012 modified: carbohydrate, N-linked (GlcNAc...) asparagine
1045 modified: carbohydrate, N-linked (GlcNAc...) asparagine
1417 K→R: Some cell corpses not engulfed.

1g291 Malk (see paper)
27% identity, 68% coverage: 3:343/504 of query aligns to 2:326/372 of 1g291

query
sites
1g291

A

A

T

G

L

V

R

R

F

L

D

V

N

D

I

V

G

W

K

K

V

V

F

F

P

G

G

E

V

V

R

T

A

A

L

V

D

R

G

E

I

M

S

S

F

L

D

E

V

V

H

K

A

D

G

G

Q

E

V

F

H

M

G

I

L

L

M

L

G

G

E

P

N
x
S

G
|
G

A
x
C

G
|
G

K
|
K

S
x
T

T
|
T

L

T

L

L

K

R

I

M

L

I

G

A

G

G

E

L

Y

E

Q

E

P

P

D

S

S

R

G

G

R

Q

V

I

L

Y

I

I

D

G

E

D

N

K

E

L

V

V

R

A

F
x
D

A

P

N
x
E

A
x
K

G

G

A

I

S

F

I

V

A

P

-
x
K

-
x
D

-

R

G

D

I

I

A

A

V

M

I

V

H

F

Q

Q

E

S

L

Y

Q

A

Y

L

V

Y

P

P

D

H

L

M

T

T

V

V

S

Y

E

D

N

N

L

I

L

A

L

-

G

-

R

-

L

F

P

P

N

L

T

K

I

L

G

R

F

K

V

V

K

P

K

R

G

Q

D

E

A

I

K

D

R

Q

F

R

V

V

R

R

E

E

Q

V

L

A

A

E

A

L

M

L

G

G

V

L

D

T

L

E

D

L

P

L

N

N

A

R

K

K

L

P

R

R

K

E

L

L

S

S

I

G

A

G

Q

Q

R

R

Q

Q

M

R

V

V

E

A

I

L

C

G

K

R

A

A

L

I

M

V

R

R

N

K

A

P

R

Q

V

V

I

F

A

L

L

M

D

D

E

E

P

P

T

L

S

S

S

N

L

L

S

-

H

-

R

-

E

D

T

A

E

K

V

L

L

R

F

V

K

R

L

M

V

R

R

A

D

E

L

L

R

K

A

K

D

L

N

Q

R

R

A

Q

L

L

-

G

-

V

-

T

I

I

Y

Y

I

V

S

T

H

H

R

D

M

Q

D

V

E

E

I

A

Y

M

Q

T

L

M

C

G

D

D

A

R

C

I

T

A

I

V

F

M

R

N

D

R

G

G

-

V

-

L

R

Q

K

Q

V

V

A

G

S

S

H

P

P

D

S

E

L

V

E

Y

G

D

V

K

S

P

R

A

D

N

T

T

I

F

V

V

S

A

E

G

M

F

V

I

G

G

R

S

E

P

I

P

S

M

D

N

I

F

Y

L

G

D

Y

A

R

I

P

V

R

T

E

E

L

D

G

G

E

F

V

V

R

D

F

F

S

G

A

E

K

F

R

R

I

L

E

K

G

-

P

-

L

-

T

L

E

L

P

P

A

D

S

Q

F

F

E

E

V

V

R

-

G

-

E

-

I

-

V

L

G

G

F

E

F

L

G

G

L

Y

V

V

G

G

A

R

G

-

R

-

S

-

E

-

L

-

M

-

H

E

L

V

I

I

Y

F

G

G

D

I

D

R

P

P

K

-

G

-

E
|
E

L
x
D

V

L

L

Y

D

D

G

A

K

M

P

F

I

A

K

Q

V

V

K

R

S

V

A

P

G

G

E

E

A

N

I

L

R

V

Q

R

G

A

I

V

V

V

L

E

C

I

P

V

E

E

D

N

R

L

K

G

E

S

E

E

G

R

I

I

V

V

binding magnesium ion: D69 (≠ F70), E71 (≠ N72), K72 (≠ A73), K79 (vs. gap), D80 (vs. gap), E292 (= E309), D293 (≠ L310)
binding pyrophosphate 2-: S38 (≠ N39), G39 (= G40), C40 (≠ A41), G41 (= G42), K42 (= K43), T43 (≠ S44), T44 (= T45)

Sites not aligning to the query:

binding magnesium ion: 359

Query Sequence

>WP_012401988.1 NCBI__GCF_000020045.1:WP_012401988.1
MSATLRFDNIGKVFPGVRALDGISFDVHAGQVHGLMGENGAGKSTLLKILGGEYQPDSGR
VLIDENEVRFANAGASIAAGIAVIHQELQYVPDLTVSENLLLGRLPNTIGFVKKGDAKRF
VREQLAAMGVDLDPNAKLRKLSIAQRQMVEICKALMRNARVIALDEPTSSLSHRETEVLF
KLVRDLRADNRALIYISHRMDEIYQLCDACTIFRDGRKVASHPSLEGVSRDTIVSEMVGR
EISDIYGYRPRELGEVRFSAKRIEGGPLTEPASFEVRRGEIVGFFGLVGAGRSELMHLIY
GDDPKKGGELVLDGKPIKVKSAGEAIRQGIVLCPEDRKEEGIVAIASVAENINISCRRHF
LKAGLFLDRKKEAETADRFIKLLKIKTPSRRQKIRFLSGGNQQKAILSRWLAEPDLRVVI
LDEPTRGIDVGAKHEIYNVIYELAERGCAIVMISSELPEVLGVSDRIVVMRQGRISGELA
RGAATEQSVLSLALPKSSTTAQAA

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