SitesBLAST
Comparing HSERO_RS05175 FitnessBrowser__HerbieS:HSERO_RS05175 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)
39% identity, 97% coverage: 12:514/516 of query aligns to 4:494/501 of P04983
- K43 (= K51) mutation to R: Loss of transport.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
32% identity, 42% coverage: 11:228/516 of query aligns to 1:218/241 of 4u00A
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
29% identity, 41% coverage: 12:225/516 of query aligns to 1:213/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F22), V16 (≠ A27), S36 (≠ N47), G37 (= G48), S38 (≠ A49), G39 (= G50), K40 (= K51), S41 (= S52), T42 (= T53), E162 (= E174), H194 (= H206)
- binding magnesium ion: S41 (= S52), E162 (= E174)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 41% coverage: 11:224/516 of query aligns to 16:224/378 of P69874
- C26 (≠ A21) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A49) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L136) mutation to M: Loss of ATPase activity and transport.
- D172 (= D173) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
3c4jA Abc protein artp in complex with atp-gamma-s
28% identity, 45% coverage: 12:243/516 of query aligns to 3:228/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
28% identity, 45% coverage: 12:243/516 of query aligns to 3:228/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
28% identity, 45% coverage: 12:243/516 of query aligns to 3:228/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
28% identity, 45% coverage: 12:243/516 of query aligns to 3:228/242 of 2oljA
3d31A Modbc from methanosarcina acetivorans (see paper)
30% identity, 41% coverage: 12:224/516 of query aligns to 1:204/348 of 3d31A
Sites not aligning to the query:
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 53% coverage: 12:283/516 of query aligns to 1:262/343 of P30750
- 40:46 (vs. 47:53, 86% identical) binding
- E166 (= E174) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
29% identity, 53% coverage: 12:283/516 of query aligns to 2:263/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F22), Q14 (vs. gap), I19 (≠ V25), S41 (≠ N47), G42 (= G48), A43 (= A49), G44 (= G50), K45 (= K51), S46 (= S52), T47 (= T53), N141 (≠ A152), S143 (vs. gap), Q146 (vs. gap), H200 (= H206)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
29% identity, 53% coverage: 12:283/516 of query aligns to 2:263/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
29% identity, 53% coverage: 12:283/516 of query aligns to 2:263/344 of 3tuiC
5x40A Structure of a cbio dimer bound with amppcp (see paper)
30% identity, 41% coverage: 11:224/516 of query aligns to 3:216/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (= F22), V18 (= V25), A20 (= A27), N40 (= N47), G41 (= G48), G43 (= G50), K44 (= K51), S45 (= S52), T46 (= T53), Q88 (vs. gap), H139 (≠ Q131), M140 (≠ L132), L141 (= L133), S142 (≠ Q134), G144 (≠ L136), Q145 (= Q137), Q166 (≠ E174), H198 (= H206)
- binding magnesium ion: S45 (= S52), Q88 (vs. gap)
Q5SSE9 ATP-binding cassette sub-family A member 13; EC 7.6.2.- from Mus musculus (Mouse) (see paper)
28% identity, 41% coverage: 11:224/516 of query aligns to 3808:4018/5034 of Q5SSE9
- K3849 (= K51) mutation to M: Does not affect intracellular vesicle localization. Affects cholesterol internalization.
- T3999 (= T205) mutation to A: Does not affect protein expression. Affects intracellular vesicles localization. Impairs intracellular cholesterol accumulation in the vesicle.
Sites not aligning to the query:
- 3577 H→P: Does not affect protein expression. Decreases intracellular cholesterol accumulation in the vesicle.
- 4735 K→M: Does not affect intracellular vesicle localization.Affects cholesterol internalization.
- 4818 R→C: Does not affect protein expression. Decreases intracellular cholesterol accumulation in the vesicle.
1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
29% identity, 45% coverage: 12:243/516 of query aligns to 6:234/240 of 1ji0A
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
31% identity, 41% coverage: 13:224/516 of query aligns to 4:214/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F22), Q14 (≠ A23), T16 (≠ V25), V18 (≠ A27), S38 (≠ N47), G39 (= G48), C40 (≠ A49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53), R133 (≠ S148), E137 (≠ A152), S139 (≠ Q154), G141 (vs. gap), Q142 (vs. gap)
- binding calcium ion: T43 (≠ S52), Q86 (= Q94)
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
28% identity, 41% coverage: 11:224/516 of query aligns to 3:219/648 of P75831
- K47 (= K51) mutation to L: Lack of activity.
- D169 (= D173) mutation to N: Lack of activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
27% identity, 41% coverage: 13:224/516 of query aligns to 7:219/375 of 2d62A
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)
28% identity, 38% coverage: 27:224/516 of query aligns to 548:739/1704 of Q99758
- N568 (= N47) 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 (= L58) to P: in SMDP3; uncertain significance
- R605 (≠ A84) to Q: in SMDP3; uncertain significance; dbSNP:rs760006956
- S693 (= S177) 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
Query Sequence
>HSERO_RS05175 FitnessBrowser__HerbieS:HSERO_RS05175
MTMSVGTQARPMLELSGIHKAFAGVKALTDVGLRLFPGEVHTLMGQNGAGKSTLIKVLTG
VHEPDGGKIELDGRAIAPASTLEAQALGISTVYQEVNLCPNLSVAENIFVGRYPTRFGRI
DWKSVHTQSRQLLQQLQIDIDVAAPLSSYPLAIQQMVAISRALSVSAKVLILDEPTSSLD
EAEVQQLFKVLRRLREQGMAILFVTHFLDQTYEISDRITVLRNGVREGEYLVSELSRLDL
VNKMVGVTAVDHRKVEAGAEALASELSTDAAAAGAVFLQAEGFGRRGVLAPQDLQLRRGE
VFGLCGLLGSGRTEMARLLFGADRADCGQLRIEGKEVRLNVPRDAIAAGIGFCSEDRKKE
GAILELSVRENIILALQARQGLFRVLPRKRQNQIAADYVKWLGIKTADLETPIGLLSGGN
QQKALLARWLATDPGMLILDEPTRGIDVRAKQEIMDFVIAMCRKGMSILFISSEIPEVLR
CSDRMLVLRDRRACGEYRRGELDEQSVLQVIAGETA
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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