SitesBLAST
Comparing WP_024771162.1 NCBI__GCF_000520995.1:WP_024771162.1 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)
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)
32% identity, 88% coverage: 32:262/264 of query aligns to 30:261/265 of P07821
- K50 (= K52) mutation to Q: Lack of activity.
- D172 (= D174) mutation to E: Lack of activity.
- E173 (= E175) mutation to A: Lack of activity.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
31% identity, 78% coverage: 32:236/264 of query aligns to 21:223/241 of 4u00A
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
28% identity, 81% coverage: 27:241/264 of query aligns to 14:223/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ N48), G36 (= G49), C37 (≠ I50), G38 (= G51), K39 (= K52), S40 (= S53), T41 (= T54), R126 (≠ K145), A130 (≠ E149), S132 (= S151), G134 (= G153), Q135 (= Q154)
Sites not aligning to the query:
P9WQK5 Uncharacterized ABC transporter ATP-binding protein Rv0073 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
30% identity, 81% coverage: 32:246/264 of query aligns to 26:238/330 of P9WQK5
- K65 (≠ M71) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
28% identity, 81% coverage: 27:241/264 of query aligns to 17:226/371 of P68187
- A85 (≠ I97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ M122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I130) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A133) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G140) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D174) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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)
28% identity, 81% coverage: 27:241/264 of query aligns to 16:225/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (≠ N48), G38 (= G49), C39 (≠ I50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), Q81 (≠ T94), R128 (≠ K145), A132 (≠ E149), S134 (= S151), G136 (= G153), Q137 (= Q154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S53), Q81 (≠ T94)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
28% identity, 81% coverage: 27:241/264 of query aligns to 16:225/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G49), C39 (≠ I50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (≠ K145), S134 (= S151), Q137 (= Q154)
- binding beryllium trifluoride ion: S37 (≠ N48), G38 (= G49), K41 (= K52), Q81 (≠ T94), S134 (= S151), G136 (= G153), H191 (= H208)
- binding magnesium ion: S42 (= S53), Q81 (≠ T94)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
28% identity, 81% coverage: 27:241/264 of query aligns to 16:225/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ I28), G38 (= G49), C39 (≠ I50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (≠ K145), A132 (≠ E149), S134 (= S151), Q137 (= Q154)
- binding tetrafluoroaluminate ion: S37 (≠ N48), G38 (= G49), K41 (= K52), Q81 (≠ T94), S134 (= S151), G135 (≠ D152), G136 (= G153), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S53), Q81 (≠ T94)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
28% identity, 81% coverage: 27:241/264 of query aligns to 16:225/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ I28), G38 (= G49), C39 (≠ I50), G40 (= G51), K41 (= K52), S42 (= S53), T43 (= T54), R128 (≠ K145), A132 (≠ E149), S134 (= S151), Q137 (= Q154)
- binding magnesium ion: S42 (= S53), Q81 (≠ T94)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
28% identity, 80% coverage: 27:236/264 of query aligns to 16:220/374 of 2awnB
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
30% identity, 78% coverage: 9:213/264 of query aligns to 1:209/232 of 1f3oA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
28% identity, 80% coverage: 27:236/264 of query aligns to 17:221/369 of P19566
- L86 (≠ A98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D181) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
30% identity, 78% coverage: 9:213/264 of query aligns to 1:209/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (= Y19), S40 (≠ N48), G41 (= G49), S42 (≠ I50), G43 (= G51), K44 (= K52), S45 (= S53), T46 (= T54), F138 (vs. gap), Q145 (≠ E149), S147 (= S151), G149 (= G153), Q150 (= Q154), H204 (= H208)
3c4jA Abc protein artp in complex with atp-gamma-s
31% identity, 78% coverage: 32:236/264 of query aligns to 22:225/242 of 3c4jA
Sites not aligning to the query:
3c41J Abc protein artp in complex with amp-pnp/mg2+
31% identity, 78% coverage: 32:236/264 of query aligns to 22:225/242 of 3c41J
Sites not aligning to the query:
2olkA Abc protein artp in complex with adp-beta-s
31% identity, 78% coverage: 32:236/264 of query aligns to 22:225/242 of 2olkA
Sites not aligning to the query:
2oljA Abc protein artp in complex with adp/mg2+
31% identity, 78% coverage: 32:236/264 of query aligns to 22:225/242 of 2oljA
Sites not aligning to the query:
Q99758 Phospholipid-transporting ATPase ABCA3; ABC-C transporter; ATP-binding cassette sub-family A member 3; ATP-binding cassette transporter 3; ATP-binding cassette 3; Xenobiotic-transporting ATPase ABCA3; EC 7.6.2.1; EC 7.6.2.2 from Homo sapiens (Human) (see 15 papers)
29% identity, 81% coverage: 10:223/264 of query aligns to 530:736/1704 of Q99758
- N568 (= N48) to D: in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport; dbSNP:rs121909184
- L579 (= L59) to P: in SMDP3; uncertain significance
- R605 (≠ A86) to Q: in SMDP3; uncertain significance; dbSNP:rs760006956
- S693 (≠ T178) mutation to L: Does not affect protein oligomerization.
Sites not aligning to the query:
- 43 R → L: in SMDP3; uncertain significance
- 53 N→Q: Does not affect N-glycosylation. Does not affect protein expression. Does not affect lamellar body membrane location.
- 101 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; dbSNP:rs121909182
- 124 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-140. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.
- 140 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N → H: in dbSNP:rs45447801; N→Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-124. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.
- 173:174 LK→AA: Loss of proteolytic processing.
- 174:175 Cleavage; by CTSL
- 215 Q → K: in SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization; dbSNP:rs879159551
- 280 R → C: in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs201299260
- 288 R → K: in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs117603931
- 290 L → M: in a breast cancer sample; somatic mutation
- 292 E → V: in SMDP3; uncertain significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death; dbSNP:rs149989682
- 766 P → S: in dbSNP:rs45592239
- 801 E → D: in a breast cancer sample; somatic mutation
- 945 N→Q: Does not affect lamellar body membrane location. Does not affect protein expression. Does not affect proteolytic processing.
- 982 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs1402761450
- 1069 H → Q: in a breast cancer sample; somatic mutation
- 1076 N → K: in SMDP3; uncertain significance
- 1221 G → S: in SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; G→A: Decreases ATP hydrolysis activity of 15% compared to the wild-type.; G→T: Decreases ATP hydrolysis activity of 36% compared to the wild-type.; G→V: Decreases ATP hydrolysis activity of 18% compared to the wild-type.
- 1302 G → E: in SMDP3; uncertain significance
- 1388 K → N: in SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport
- 1553 L → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs121909183
- 1580 L → P: in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport; L→A: Decreases ATP hydrolysis activity of 13% compared to the wild-type.; L→F: Decreases ATP hydrolysis activity of 13% compared to the wild-type.; L→V: Decreases ATP hydrolysis activity of 56% compared to the wild-type.
- 1591 Q → P: in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs28936691
7w02A Cryo-em structure of atp-bound abca3 (see paper)
29% identity, 81% coverage: 10:223/264 of query aligns to 495:701/1566 of 7w02A
- binding adenosine-5'-triphosphate: F504 (≠ Y19), N533 (= N48), G534 (= G49), G536 (= G51), K537 (= K52), T538 (≠ S53), T539 (= T54), Q578 (≠ T94), L630 (= L150), S631 (= S151)
- binding magnesium ion: T538 (≠ S53), Q578 (≠ T94)
Sites not aligning to the query:
- binding adenosine-5'-triphosphate: 1277, 1305, 1306, 1307, 1308, 1309, 1310, 1344, 1395, 1398
- binding magnesium ion: 1310, 1344
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
30% identity, 83% coverage: 19:236/264 of query aligns to 8:223/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ K22), V16 (= V27), S36 (≠ N48), G37 (= G49), S38 (≠ I50), G39 (= G51), K40 (= K52), S41 (= S53), T42 (= T54), E162 (= E175), H194 (= H208)
- binding magnesium ion: S41 (= S53), E162 (= E175)
Query Sequence
>WP_024771162.1 NCBI__GCF_000520995.1:WP_024771162.1
MNREALNIVLKTEDLSIGYRTKKELNVIAADINLKLHEGELVGLVGANGIGKSTLLRTLS
RVQPALHGKIMLSDIELQSYKSVELASQLSIVLTEQIASKNLTVQELVALGRQPYTNWVG
KMAEEDIEQIRKAIEVTHIGDLVAKRCFELSDGQLQKVLIARAIAQDTPFIMLDEPTTHL
DVYHKAYILKLLKRLAFETRKTILFSTHEIDFAIQLCDKMIVMNEDGFEFGRPKELVQCR
AFSSLFPEDLILFDSKSGRYKVRN
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