SitesBLAST
Comparing SM_b21429 FitnessBrowser__Smeli:SM_b21429 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)
31% identity, 89% coverage: 3:228/253 of query aligns to 11:245/265 of P07821
- K50 (= K43) mutation to Q: Lack of activity.
- D172 (= D155) mutation to E: Lack of activity.
- E173 (= E156) mutation to A: Lack of activity.
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
27% identity, 89% coverage: 4:228/253 of query aligns to 3:233/240 of 6mjpA
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
28% identity, 89% coverage: 3:228/253 of query aligns to 2:233/233 of 6b8bA
- binding adenosine-5'-diphosphate: Y12 (= Y13), R15 (= R16), V17 (= V18), G38 (≠ A40), G40 (= G42), K41 (= K43), T42 (≠ S44), T43 (= T45)
- binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (≠ N82), R90 (≠ A83), R91 (≠ V84)
6b89A E. Coli lptb in complex with adp and novobiocin (see paper)
28% identity, 89% coverage: 3:228/253 of query aligns to 2:233/234 of 6b89A
- binding adenosine-5'-diphosphate: Y12 (= Y13), R15 (= R16), V17 (= V18), N37 (= N39), G38 (≠ A40), G40 (= G42), K41 (= K43), T42 (≠ S44), T43 (= T45)
- binding magnesium ion: T42 (≠ S44), Q84 (= Q77)
- binding novobiocin: L71 (≠ D64), H72 (≠ T65), P83 (= P76), A86 (≠ T79), S87 (≠ G80), F89 (≠ N82), R90 (≠ A83), R91 (≠ V84), L92 (= L85), V101 (≠ G100), Q135 (≠ G129), R149 (≠ Q143)
4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium (see paper)
28% identity, 89% coverage: 3:228/253 of query aligns to 2:233/234 of 4p31A
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
29% identity, 89% coverage: 3:228/253 of query aligns to 2:233/238 of 6s8nB
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
29% identity, 89% coverage: 3:228/253 of query aligns to 2:233/238 of 6s8gA
- binding phosphoaminophosphonic acid-adenylate ester: Y12 (= Y13), R15 (= R16), N37 (= N39), G40 (= G42), K41 (= K43), T42 (≠ S44), T43 (= T45), Q84 (= Q77), S136 (≠ E130), S138 (= S132), E141 (≠ Q135)
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
29% identity, 89% coverage: 3:228/253 of query aligns to 2:233/235 of 6mhzA
- binding adp orthovanadate: Y12 (= Y13), N37 (= N39), G38 (≠ A40), G40 (= G42), K41 (= K43), T42 (≠ S44), T43 (= T45), Q84 (= Q77), S136 (≠ E130), S138 (= S132), G139 (= G133), G140 (= G134), E162 (= E156), G166 (≠ A160), H194 (= H189)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
32% identity, 85% coverage: 1:216/253 of query aligns to 4:215/353 of 1vciA
1l7vC Bacterial abc transporter involved in b12 uptake (see paper)
28% identity, 81% coverage: 24:228/253 of query aligns to 19:229/231 of 1l7vC
6mbnA Lptb e163q in complex with atp (see paper)
28% identity, 89% coverage: 3:228/253 of query aligns to 3:234/241 of 6mbnA
4fi3C Structure of vitamin b12 transporter btucd-f in a nucleotide-bound state (see paper)
28% identity, 83% coverage: 24:233/253 of query aligns to 19:234/248 of 4fi3C
- binding phosphoaminophosphonic acid-adenylate ester: N34 (= N39), G35 (≠ A40), G37 (= G42), K38 (= K43), S39 (= S44), T40 (= T45), R121 (= R126), Q125 (≠ E130), S127 (= S132), G129 (= G134), E130 (≠ Q135), Q158 (≠ E156)
- binding magnesium ion: S39 (= S44), Q79 (= Q77)
Sites not aligning to the query:
7r8eA The structure of human abcg1 e242q complexed with atp (see paper)
32% identity, 86% coverage: 2:219/253 of query aligns to 4:225/548 of 7r8eA
Sites not aligning to the query:
1g291 Malk (see paper)
30% identity, 86% coverage: 1:218/253 of query aligns to 1:227/372 of 1g291
- binding magnesium ion: D69 (≠ N67), E71 (≠ A69), K72 (≠ E70), K79 (≠ Q77), D80 (= D78)
- binding pyrophosphate 2-: S38 (≠ N39), G39 (≠ A40), C40 (≠ A41), G41 (= G42), K42 (= K43), T43 (≠ S44), T44 (= T45)
Sites not aligning to the query:
P45844 ATP-binding cassette sub-family G member 1; ATP-binding cassette transporter 8; White protein homolog; EC 7.6.2.- from Homo sapiens (Human) (see 6 papers)
34% identity, 81% coverage: 14:219/253 of query aligns to 96:305/678 of P45844
- K124 (= K43) mutation to M: Affects ATP binding. Does not affect efflux of 7beta-hydroxycholesterol. Does not affect localization at plasma membrane. Does not affect homodimerization. Decreases cholesterol and phospholipids efflux. Does not affect heretodimerization with ABCG4.
- C154 (≠ N67) modified: S-palmitoyl cysteine; mutation to A: No significant effect.
Sites not aligning to the query:
- 30 modified: S-palmitoyl cysteine; C→A: No significant effect.
- 315 modified: S-palmitoyl cysteine; mutation C->A,S: Significantly decreases ABCG1-mediated cholesterol efflux.
- 394 modified: S-palmitoyl cysteine; C→A: No significant effect.
- 406 modified: S-palmitoyl cysteine; C→A: No significant effect.
- 491 Y→A: Significantly reduces interaction with CAV1; when associated with A-493. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-493.
- 493 Y→A: Significantly reduces interaction with CAV1; when associated with A-491. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-491.
- 498 Y→A: Significantly reduces interaction with CAV1; when associated with A-499. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-499. Affects subcellular location at plasma membrane; when associated with A-499. Affects ABCG1 traffincking to the plasma membrane; when associated with A-499.; Y→F: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-499.; Y→I: Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-499.; Y→W: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-499.
- 499 Y→A: Significantly reduces interaction with CAV1; when associated with A-498. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-498. Affects subcellular location at plasma membrane; when associated with A-498. Affects ABCG1 traffincking to the plasma membrane; when associated with A-498.; Y→F: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-498.; Y→I: Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-498.; Y→W: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-498.
- 668 natural variant: F -> L
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
31% identity, 86% coverage: 4:220/253 of query aligns to 3:225/241 of 4u00A
7oz1A Cryo-em structure of abcg1 e242q mutant with atp and cholesteryl hemisuccinate bound (see paper)
32% identity, 86% coverage: 2:219/253 of query aligns to 2:225/544 of 7oz1A
Sites not aligning to the query:
- binding cholesterol hemisuccinate: 335, 335, 367, 431, 431, 434, 435, 438, 438, 439, 441, 463, 466, 466, 467, 525, 526, 527, 529, 530, 531, 532, 533, 535
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 84% coverage: 1:213/253 of query aligns to 1:216/371 of P68187
- A85 (≠ G80) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ W101) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V114) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A116) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ N121) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G134) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D155) 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.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
32% identity, 85% coverage: 4:218/253 of query aligns to 2:223/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y13), V16 (= V18), S36 (≠ N39), G37 (≠ A40), S38 (≠ A41), G39 (= G42), K40 (= K43), S41 (= S44), T42 (= T45), E162 (= E156), H194 (= H189)
- binding magnesium ion: S41 (= S44), E162 (= E156)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
27% identity, 84% coverage: 1:213/253 of query aligns to 4:225/375 of 2d62A
Query Sequence
>SM_b21429 FitnessBrowser__Smeli:SM_b21429
MVSLALKDVGATYGRRVVLSDINTGTLKGGHLTAVIGPNAAGKSTLFKRIAGLAAGPGLV
HLSDTANGAEAICYMPQDTGANAVLTVYESVLLSAKQGSGWKVKDGELAEIDRVLAALKI
NDLAFRGLGELSGGQRQLVSIAQALVRKPEVLLMDEPTSALDLFRQIEVLGFMKRLAAQS
GMAVLIALHDLNHALRYCEDTIVISGGSVVASGPTHTVVTADMLKSVYRVEARVEACSRG
RPVIIVDDSITFG
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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