SitesBLAST
Comparing WP_097030541.1 NCBI__GCF_900207575.1:WP_097030541.1 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
38% identity, 88% coverage: 1:226/258 of query aligns to 1:218/501 of P04983
- K43 (= K43) mutation to R: Loss of transport.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
33% identity, 84% coverage: 3:219/258 of query aligns to 1:206/241 of 4u00A
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 79% coverage: 17:221/258 of query aligns to 18:213/343 of P30750
- 40:46 (vs. 39:45, 71% identical) binding ATP
- E166 (= E175) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
34% identity, 79% coverage: 17:221/258 of query aligns to 19:214/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: I19 (≠ V17), S41 (≠ N39), G42 (= G40), A43 (= A41), G44 (= G42), K45 (= K43), S46 (= S44), T47 (≠ S45), N141 (≠ T149), S143 (= S151), Q146 (= Q154), H200 (= H207)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
34% identity, 79% coverage: 17:221/258 of query aligns to 19:214/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
34% identity, 79% coverage: 17:221/258 of query aligns to 19:214/344 of 3tuiC
Sites not aligning to the query:
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)
31% identity, 86% coverage: 5:225/258 of query aligns to 11:228/257 of P0AAH0
- G48 (= G42) mutation to I: Loss of phosphate transport.
- K49 (= K43) mutation to Q: Loss of phosphate transport.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3c4jA Abc protein artp in complex with atp-gamma-s
31% identity, 84% coverage: 4:219/258 of query aligns to 3:208/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
31% identity, 84% coverage: 4:219/258 of query aligns to 3:208/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
31% identity, 84% coverage: 4:219/258 of query aligns to 3:208/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
31% identity, 84% coverage: 4:219/258 of query aligns to 3:208/242 of 2oljA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
28% identity, 84% coverage: 4:221/258 of query aligns to 4:222/253 of 1g9xB
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
27% identity, 84% coverage: 4:221/258 of query aligns to 4:222/254 of 1g6hA
Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
29% identity, 84% coverage: 19:235/258 of query aligns to 19:223/276 of Q5M243
- Q90 (≠ M100) mutation to A: No effect on ATPase, 10-fold decrease in riboflavin uptake; when associated with A-97 in EcfA2.
- E163 (= E175) mutation to Q: 10-fold decrease in ATPase and riboflavin uptake; when associated with Q-171 in EcfA2.
6z4wA Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
30% identity, 86% coverage: 4:226/258 of query aligns to 3:216/230 of 6z4wA
A0A0H2ZM82 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see paper)
30% identity, 86% coverage: 4:226/258 of query aligns to 3:216/230 of A0A0H2ZM82
- K43 (= K43) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.
- D164 (= D174) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.
- E165 (= E175) mutation to A: Growth cessation and formation of spherical cells with aberrant division planes.
6z67B Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution (see paper)
30% identity, 84% coverage: 4:219/258 of query aligns to 3:209/229 of 6z67B
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 88% coverage: 1:226/258 of query aligns to 14:225/378 of P69874
- C26 (≠ R13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y14) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A41) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L135) mutation to M: Loss of ATPase activity and transport.
- D172 (= D174) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
29% identity, 86% coverage: 5:225/258 of query aligns to 7:219/375 of 2d62A
O95477 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein; EC 7.6.2.1 from Homo sapiens (Human) (see 35 papers)
30% identity, 86% coverage: 8:230/258 of query aligns to 902:1112/2261 of O95477
- D917 (≠ N21) to Y: in a colorectal cancer sample; somatic mutation
- T929 (≠ L33) to I: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane
- N935 (= N39) to S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs28937313
- K939 (= K43) mutation to M: Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952.
- S1042 (≠ A159) modified: Phosphoserine; by PKA
- P1065 (≠ V182) natural variant: P -> S
- M1091 (= M209) to T: in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux
- C1110 (≠ L228) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1111.
- C1111 (= C229) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1110.
Sites not aligning to the query:
- 3 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111.
- 23 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111.
- 74 I→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.; I→K: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-371.
- 75 modified: Disulfide link with 309
- 85 P → L: in FHA1; Alabama; dbSNP:rs145183203
- 98 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 100 S→C: Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
- 210 E → D: in a colorectal cancer sample; somatic mutation
- 219 R → K: in dbSNP:rs2230806
- 230 R → C: in dbSNP:rs9282541
- 244 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 248 P → A: in dbSNP:rs142625938
- 255 A → T: in TGD; deficient cellular cholesterol efflux; dbSNP:rs758100110
- 304 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-308.
- 308 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-304.
- 309 modified: Disulfide link with 75
- 364 S → C: in dbSNP:rs775035559
- 371 I→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane. 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-74 or C-375.; I→E: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-74.
- 375 L→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.
- 399 V → A: in dbSNP:rs9282543
- 401 K → Q: in dbSNP:rs138487227
- 496 R → W: in dbSNP:rs147675550
- 568 K→A: 60-65% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane.
- 573 Y→F: No effect on phospholipid and cholesterol efflux and on localization to cell membrane.
- 581 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-584 and K-585.
- 583 F→K: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-590.
- 584 E→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-585.
- 585 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-584.
- 590 W → S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs137854496; W→E: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-583.
- 593 F→L: Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
- 638 R → Q: in dbSNP:rs374190304
- 771 V → M: in dbSNP:rs2066718
- 774 T → P: in dbSNP:rs35819696; natural variant: T -> S
- 776 K → N: in dbSNP:rs138880920
- 815 E → G: in dbSNP:rs145582736
- 825 V → I: in dbSNP:rs2066715
- 883 I → M: in dbSNP:rs2066714
- 1172 E → D: in dbSNP:rs33918808
- 1181 S → F: in dbSNP:rs76881554
- 1216 G → V: in dbSNP:rs562403512
- 1341 R → T: in dbSNP:rs147743782
- 1376 S → G: in dbSNP:rs145689805
- 1379 L → F: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane
- 1407 A → T: in a colorectal cancer sample; somatic mutation; dbSNP:rs189206655
- 1463 modified: Disulfide link with 1477
- 1477 modified: Disulfide link with 1463; C → R: in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs137854494
- 1512 T→M: Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity.
- 1555 I → T: in dbSNP:rs1997618
- 1587 K → R: in dbSNP:rs2230808
- 1611 N → D: in FHA1; deficient cellular cholesterol efflux
- 1615 R → Q: in dbSNP:rs1251839800
- 1648 L → P: in dbSNP:rs1883024
- 1670 A → T: in dbSNP:rs1203589782
- 1680 R → Q: in dbSNP:rs150125857
- 1704 V → D: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane
- 1731 S → C: in dbSNP:rs760507032
- 1897 R → W: in FHA1; uncertain significance; dbSNP:rs760768125
- 1925 R → Q: in Scott syndrome; shows impaired trafficking of the mutant protein to the plasma membrane; dbSNP:rs142688906
- 1952 K→M: Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939.
- 2054 modified: Phosphoserine; by PKA
- 2081 R → W: in TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane; dbSNP:rs137854501
- 2109 A → T: in a colorectal cancer sample; somatic mutation
- 2150 P → L: in FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs369098049
- 2163 natural variant: F -> S
- 2168 L → P: in dbSNP:rs2853577
- 2243 D → E: in dbSNP:rs34879708
- 2244 V → I: in dbSNP:rs144588452
Query Sequence
>WP_097030541.1 NCBI__GCF_900207575.1:WP_097030541.1
MEPILKARGLVKRYGKVTALNNCDFDLYPGEILAVIGDNGAGKSSLIKALSGAVKVDEGT
IELDGRPMSFVSPLDAREAGIETVYQNLALSPALSIADNMFLGREIRKPGIMGKWFRALD
RAEMERRAREKLTELGLMTIQNIGQAVETLSGGQRQGVAVARAAAFGSKVVIMDEPTAAL
GVKESRRVLELILDVKRRGLPIVLISHNMPHVFEVADRIHVHRLGRRLCVIDPRRHSMSD
AVALMTGAMAPEKLNEFA
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