SitesBLAST
Comparing WP_013834982.1 NCBI__GCF_000214825.1:WP_013834982.1 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)
P43672 ATP-binding protein Uup; EC 3.6.1.- from Escherichia coli (strain K12) (see 3 papers)
50% identity, 100% coverage: 1:628/628 of query aligns to 1:634/635 of P43672
- D181 (= D174) mutation to N: No longer hydrolyzes ATP, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, not required to suppress bipA deletion.
- E182 (= E175) mutation to Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-464 (called EQ2).
- 294:300 (vs. 287:293, 57% identical) mutation Missing: Decreases growth at 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.
- D465 (= D458) mutation to N: No longer hydrolyzes ATP, has a high level of transposon excision. Inhibits growth at 37 and 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.
- E466 (= E459) mutation to Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-181 (EQ2).
Sites not aligning to the query:
- 551:635 C-terminal domain (CTD), binds DNA, required to complement a deletion mutant; mutation Missing: Reduces DNA binding 2-fold, no change in ATP hydrolysis, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes.
7mscx 70SIC in complex with MtbEttA at Pre_R0 state (see paper)
36% identity, 80% coverage: 6:505/628 of query aligns to 7:513/547 of 7mscx
- binding phosphoaminophosphonic acid-adenylate ester: H14 (≠ F13), N39 (= N38), G42 (= G41), K43 (= K42), S44 (= S43), S45 (≠ T44), Q74 (= Q73), N158 (≠ S149), S160 (= S151), G161 (= G152), G162 (= G153), H213 (= H204), Y330 (≠ W322), R333 (≠ K325), N355 (= N347), G356 (= G348), G358 (= G350), K359 (= K351), T360 (≠ S352), T361 (= T353), K437 (≠ Q429), S443 (= S435), G445 (= G437), E446 (= E438), H496 (= H488)
- binding magnesium ion: S44 (= S43), Q74 (= Q73), D183 (= D174)
- binding : Y28 (≠ E27), Q142 (≠ T134), R256 (≠ K247), K257 (≠ S248), K260 (≠ E251), R273 (= R264), S274 (≠ Q265), K277 (= K268), K277 (= K268), A278 (= A269), R279 (= R270), Q280 (≠ R271), S283 (≠ N274), K284 (≠ E275), A285 (≠ G276), R286 (= R277), R289 (≠ A280), R301 (= R292), R315 (≠ T307), G317 (= G309), N318 (≠ K310), T382 (≠ N374), D410 (= D402), Y411 (= Y403), R422 (≠ I414), A423 (≠ G415)
Sites not aligning to the query:
P9WQK3 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 80% coverage: 6:505/628 of query aligns to 8:514/558 of P9WQK3
- K338 (≠ Q329) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3j5sD Etta binds to ribosome exit site and regulates translation by restricting ribosome and tRNA dynamics (see paper)
36% identity, 80% coverage: 18:519/628 of query aligns to 20:529/554 of 3j5sD
- binding : S27 (≠ Q25), R63 (≠ I61), N140 (= N129), V141 (≠ Q130), Q142 (= Q131), R145 (≠ T134), A146 (≠ I135), A149 (≠ K138), R202 (≠ G190), F203 (= F191), E208 (≠ R196), W239 (= W227), Q256 (≠ S244), Q260 (≠ S248), R276 (= R264), Q277 (= Q265), G319 (= G309), D320 (≠ K310)
Sites not aligning to the query:
P0A9W3 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Escherichia coli (strain K12) (see 4 papers)
36% identity, 80% coverage: 18:519/628 of query aligns to 21:530/555 of P0A9W3
- 95:139 (vs. 92:127, 22% identical) Arm
- E188 (= E175) mutation to Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity, 47-fold decrease in translation; when associated with Q-470 (called EQ2).
- 242:322 (vs. 229:311, 27% identical) PtIM
- E470 (= E459) mutation to Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity, 47-fold decrease in translation; when associated with Q-188 (EQ2).
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
A0A0H2VFI8 Energy-dependent translational throttle protein EttA; Translational regulatory factor EttA; EC 3.6.1.- from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
36% identity, 80% coverage: 18:519/628 of query aligns to 21:530/555 of A0A0H2VFI8
- E188 (= E175) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-456 (called EQ2).
- E470 (= E459) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-188 (EQ2).
P0A9U3 Probable ATP-binding protein YbiT from Escherichia coli (strain K12) (see paper)
31% identity, 83% coverage: 3:523/628 of query aligns to 1:527/530 of P0A9U3
- E181 (= E175) mutation to Q: Causes growth defect at 37 degrees Celsius, 15-fold decrease in translation; when associated with Q-464 (called EQ2).
- E464 (= E459) mutation to Q: Causes growth defect at 37 degrees Celsius, 15-fold decrease in translation; when associated with Q-181 (EQ2).
P0A9U4 Probable ATP-binding protein YbiT from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
31% identity, 83% coverage: 3:523/628 of query aligns to 1:527/530 of P0A9U4
- E181 (= E175) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-464 (called EQ2).
- E464 (= E459) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-181 (EQ2).
A0A0H2VBH0 Probable ATP-binding protein YheS from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
28% identity, 93% coverage: 3:589/628 of query aligns to 1:582/637 of A0A0H2VBH0
- E175 (= E175) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-456 (called EQ2).
- E456 (= E459) mutation to Q: Causes growth defect at 18 degrees Celsius in bipA deletion strain; when associated with Q-175 (EQ2).
P63389 Probable ATP-binding protein YheS from Escherichia coli (strain K12) (see paper)
28% identity, 93% coverage: 3:589/628 of query aligns to 1:582/637 of P63389
- E175 (= E175) mutation to Q: Causes growth defect at 37 degrees Celsius, 7-fold decrease in translation; when associated with Q-456 (called EQ2).
- E456 (= E459) mutation to Q: Causes growth defect at 37 degrees Celsius, 7-fold decrease in translation; when associated with Q-175 (EQ2).
7p7q0 30S ribosomal protein S19 (see paper)
28% identity, 80% coverage: 9:512/628 of query aligns to 6:524/534 of 7p7q0
- binding adenosine-5'-triphosphate: F10 (= F13), N35 (= N38), G36 (= G39), G38 (= G41), K39 (= K42), T40 (≠ S43), T41 (= T44), Q69 (= Q73), Q154 (≠ D145), E158 (≠ S149), S160 (= S151), G161 (= G152), G162 (= G153), Q163 (≠ M154), Y339 (≠ W322), N365 (= N347), G366 (= G348), G368 (= G350), K369 (= K351), S370 (= S352), T371 (= T353), Q400 (= Q382), K441 (≠ Q429), V445 (≠ S433), S447 (= S435), G449 (= G437), E450 (= E438)
- binding magnesium ion: T40 (≠ S43), Q69 (= Q73), S370 (= S352), Q400 (= Q382)
- binding : H22 (≠ Q25), R114 (≠ G108), Y132 (≠ W126), L139 (≠ N129), K248 (≠ R237), K258 (= K247), F273 (≠ W262), Q275 (≠ R264), K276 (≠ Q265), K278 (≠ I267), Q279 (≠ K268), S281 (≠ R270), Q282 (≠ R271), Q282 (≠ R271), T283 (= T272), T283 (= T272), N284 (≠ R273), H285 (≠ N274), H285 (≠ N274), K288 (≠ R277), R289 (≠ V278), M290 (≠ R279), L292 (= L281), E293 (= E282), R294 (≠ K283), R297 (= R285), K300 (≠ R288), K310 (≠ S297), R426 (≠ I414), S430 (= S418), D436 (≠ P424)
Sites not aligning to the query:
8buu9 50S ribosomal protein L13 (see paper)
28% identity, 79% coverage: 12:504/628 of query aligns to 15:502/573 of 8buu9
- binding adenosine-5'-triphosphate: F16 (= F13), N41 (= N38), G42 (= G39), G44 (= G41), K45 (= K42), T46 (≠ S43), T47 (= T44), R116 (≠ E146), H119 (≠ S149), S121 (= S151), E124 (≠ M154), F325 (≠ W322), R328 (≠ K325), G351 (= G348), G353 (= G350), K354 (= K351), T355 (≠ S352), T356 (= T353), Q385 (= Q382), T431 (≠ S433), S433 (= S435), L434 (≠ G436), G435 (= G437), E436 (= E438)
- binding magnesium ion: T46 (≠ S43), T355 (≠ S352), Q385 (= Q382), L434 (≠ G436)
- binding : E28 (≠ Q25), K30 (≠ E27), H95 (≠ L98), Q99 (≠ H102), S102 (≠ A105), N214 (vs. gap), H217 (≠ A240), Q218 (= Q241), Q232 (≠ K255), Q235 (= Q258), W239 (= W262), K242 (vs. gap), A243 (vs. gap), H244 (vs. gap), R245 (vs. gap), S254 (vs. gap), E255 (vs. gap), R257 (vs. gap), Q258 (vs. gap), I259 (vs. gap), G260 (vs. gap), K262 (vs. gap), E263 (vs. gap), Y264 (vs. gap), R266 (vs. gap), K268 (= K268), K270 (≠ R270), K271 (≠ R271), D273 (≠ R273), N274 (= N274), K277 (≠ R277), S278 (≠ V278), K279 (≠ R279), R282 (vs. gap), R302 (≠ N299), K310 (≠ T307), R311 (≠ S308), R314 (≠ K311), W373 (≠ E370), S375 (≠ G372), S377 (≠ N374), L409 (≠ N407), R412 (= R410), T413 (≠ K411), A416 (≠ S418), N417 (≠ D419), K421 (≠ A423)
Sites not aligning to the query:
P39115 Ribosome protection protein VmlR; Multidrug resistance system ATP-binding protein VmlR from Bacillus subtilis (strain 168) (see 2 papers)
28% identity, 81% coverage: 3:508/628 of query aligns to 4:481/547 of P39115
- E129 (= E175) mutation to Q: Probably has no ATPase activity, does not confer lincomycin resistance, cells enter stationary phase at lower cell density, almost all protein is bound to ribosomes; when associated with Q-432 (called EQ2). Used for electron microscopy.
- 183:289 (vs. 229:310, 19% identical) Antibiotic resistance domain (ARD)
- F237 (≠ Q258) mutation to A: No longer confers resistance to virginiamycin M, still confers resistance to lincomycin and tiamycin.; mutation to V: Still confers resistance to virginiamycin M, lincomycin and tiamycin.
- E432 (= E459) mutation to Q: Probably has no ATPase activity, does not confer lincomycin resistance, cells enter stationary phase at lower cell density, almost all protein is bound to ribosomes; when associated with Q-129 (called EQ2). Used for electron microscopy.
Sites not aligning to the query:
- 483:547 C-terminal extension (CTE)
- 492:547 mutation Missing: No longer confers resistance to virginiamycin M.
6ha8V 50S ribosomal protein L1 (see paper)
28% identity, 81% coverage: 3:508/628 of query aligns to 3:480/541 of 6ha8V
- binding adenosine-5'-triphosphate: V13 (≠ F13), N38 (= N38), G39 (= G39), A40 (≠ E40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q102 (≠ S149), S104 (= S151), G105 (= G152), G106 (= G153), F300 (≠ W322), R303 (≠ K325), N325 (= N347), G326 (= G348), S327 (≠ C349), G328 (= G350), K329 (= K351), T330 (≠ S352), T331 (= T353), Q359 (= Q382), Q398 (≠ R426), E401 (≠ Q429), M406 (≠ L434), S407 (= S435), G409 (= G437), H460 (= H488)
- binding : P84 (≠ Q112), K88 (≠ T134), E91 (≠ S137), K92 (= K138), H147 (≠ N194), K181 (≠ D228), K193 (vs. gap), T197 (vs. gap), R200 (vs. gap), Q215 (= Q241), W222 (vs. gap), K225 (= K247), A226 (≠ S248), H227 (≠ N249), T231 (≠ D253), G235 (≠ A257), F236 (≠ Q258), K237 (≠ E259), E238 (= E260), Y239 (≠ V261), R241 (≠ G266), K243 (= K268), K245 (≠ R270), R246 (= R271), D248 (≠ E275), S253 (≠ A280), K254 (≠ L281), K256 (= K283), R257 (= R285), K260 (≠ R288), K285 (≠ T307), G287 (= G309), R289 (≠ K311), W347 (≠ E370), S349 (≠ G372), S351 (≠ N374), R382 (= R410), H384 (= H412), N387 (≠ G415), L388 (≠ Y416), H391 (≠ D419)
Sites not aligning to the query:
7nhn0 50S ribosomal protein L31 type B (see paper)
32% identity, 57% coverage: 148:504/628 of query aligns to 75:451/461 of 7nhn0
- binding adenosine-5'-triphosphate: T76 (≠ S149), S78 (= S151), E81 (≠ M154), I278 (≠ W322), N303 (= N347), A304 (≠ G348), S305 (≠ C349), G306 (= G350), K307 (= K351), T308 (≠ S352), T309 (= T353), Q334 (= Q382), K376 (≠ Q429), M380 (≠ S433), S382 (= S435), G384 (= G437), E385 (= E438)
- binding magnesium ion: T308 (≠ S352), Q334 (= Q382)
- binding : R84 (= R157), Q88 (≠ A161), R92 (≠ I165), H114 (≠ W187), R117 (≠ G190), H123 (≠ R196), K177 (≠ S250), E178 (= E251), Q185 (= Q258), S189 (vs. gap), H192 (vs. gap), I195 (vs. gap), R199 (vs. gap), I200 (vs. gap), K202 (vs. gap), P203 (vs. gap), R206 (vs. gap), K210 (vs. gap), E211 (= E259), A212 (≠ E260), S213 (≠ V261), F215 (≠ I263), G218 (= G266), K219 (≠ I267), T221 (≠ A269), Q222 (≠ R270), K224 (≠ T272), K225 (≠ R273), H227 (≠ E275), K231 (≠ R279), K235 (= K283), R236 (= R285), R239 (= R288), K245 (≠ Q294), H247 (≠ G296), T248 (≠ S297), K250 (≠ N299), P251 (vs. gap), K253 (≠ Q301), K263 (vs. gap), N266 (≠ K310), T267 (≠ K311), R361 (≠ K411), E362 (≠ H412), G365 (= G415), H368 (≠ S418), E371 (≠ P424)
Sites not aligning to the query:
7nhl0 50S ribosomal protein L32 (see paper)
31% identity, 57% coverage: 148:504/628 of query aligns to 77:454/465 of 7nhl0
- binding adenosine-5'-triphosphate: T78 (≠ S149), S80 (= S151), G81 (= G152), E83 (≠ M154), I281 (≠ W322), R284 (≠ K325), L286 (≠ I327), N306 (= N347), G307 (= G348), T308 (≠ C349), G309 (= G350), K310 (= K351), T311 (≠ S352), K379 (≠ Q429), V383 (≠ S433), S385 (= S435), G387 (= G437), E388 (= E438)
- binding magnesium ion: T311 (≠ S352), Q337 (= Q382)
- binding : N112 (≠ P183), K116 (≠ W187), N123 (= N194), H125 (≠ R196), R173 (vs. gap), K180 (vs. gap), R187 (vs. gap), R201 (≠ S248), A202 (≠ N249), K204 (≠ E251), K207 (= K254), S210 (≠ A257), S212 (≠ E259), E213 (= E260), K215 (≠ W262), K217 (≠ R264), V218 (≠ Q265), T219 (≠ G266), Y222 (vs. gap), F223 (≠ I267), A224 (≠ K268), S225 (≠ A269), K226 (≠ R270), K228 (≠ T272), R231 (≠ E275), K232 (≠ G276), S236 (≠ A280), T239 (≠ K283), R240 (≠ L284), N251 (≠ S293), D259 (≠ Q301), N268 (≠ G309), R269 (≠ K310), E360 (= E405), T361 (≠ I406), L362 (≠ H412), R364 (≠ I414), T365 (≠ G415), A368 (≠ S418), R369 (≠ D419), R374 (≠ P424)
Sites not aligning to the query:
- binding adenosine-5'-triphosphate: 13, 16, 38, 39, 41, 42, 43, 44
- binding magnesium ion: 43, 71
- binding : 2, 23, 25, 27
7p486 ABC-F type ribosomal protection protein (see paper)
25% identity, 79% coverage: 3:496/628 of query aligns to 2:463/510 of 7p486
- binding adenosine-5'-triphosphate: I12 (≠ F13), E13 (≠ G14), N37 (= N38), G38 (= G39), G40 (= G41), K41 (= K42), S42 (= S43), T100 (≠ S149), S102 (= S151), G104 (= G153), E105 (≠ M154), Y294 (≠ W322), N319 (= N347), G320 (= G348), G322 (= G350), K323 (= K351), S324 (= S352), T325 (= T353), Q354 (= Q382), Q400 (≠ S433), S402 (= S435), M403 (≠ G436), G404 (= G437)
- binding magnesium ion: S42 (= S43), Q61 (= Q73), S324 (= S352), Q354 (= Q382)
- binding : H24 (≠ Q25), Q188 (vs. gap), T195 (≠ R237), K202 (≠ S244), K215 (≠ A257), Y217 (≠ E259), W220 (= W262), Y221 (≠ I263), S229 (≠ R271), R231 (= R273), P233 (≠ E275), Y234 (≠ G276), Q236 (≠ V278), K237 (≠ R279), Q238 (≠ A280), S240 (≠ E282), K241 (= K283), K244 (vs. gap), R245 (vs. gap), H251 (vs. gap), R255 (= R288), F272 (≠ L300), S273 (≠ Q301), H282 (≠ K310), K342 (≠ E370), T378 (≠ I406), R381 (≠ Q409), T382 (≠ G415), A385 (≠ S418), S386 (≠ D419)
P40024 ABC transporter ATP-binding protein ARB1; ATP-binding cassette protein involved in ribosome biogenesis 1; EC 3.6.5.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 79% coverage: 6:504/628 of query aligns to 84:586/610 of P40024
- GG 229:230 (= GG 152:153) mutation to DE: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity; when associated with D-519.
- Y346 (vs. gap) mutation to A: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity.
- G519 (= G437) mutation to D: Abolished ATPase activity, leading to impaired ability to stimulate VMS1 activity; when associated with 229-D-E-230.
6r84A Protein VMS1,Vms1,Protein VMS1,Vms1 (see paper)
29% identity, 57% coverage: 150:504/628 of query aligns to 81:429/446 of 6r84A
- binding : K178 (≠ S250), E185 (= E259), E186 (= E260), F193 (≠ G266), T199 (= T272), Y200 (vs. gap), A201 (vs. gap), N202 (vs. gap), V204 (vs. gap), K205 (vs. gap), Q206 (≠ R273), S209 (≠ G276), R210 (= R277), K216 (= K283)
Q8NE71 ATP-binding cassette sub-family F member 1; ATP-binding cassette 50; TNF-alpha-stimulated ABC protein from Homo sapiens (Human) (see 2 papers)
27% identity, 82% coverage: 6:522/628 of query aligns to 306:830/845 of Q8NE71
- K342 (= K42) mutation to M: Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-664. Shows an enhanced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664.
- Q367 (= Q73) mutation to E: Does not inhibit ribosome binding.
- G454 (= G152) mutation to D: Does not inhibit ribosome binding.
- E477 (= E175) mutation to Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768.
- H506 (= H204) mutation to L: Does not inhibit ribosome binding.
- K664 (= K351) mutation to M: Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-342. Shows a reduced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664.
- Q695 (= Q382) mutation to E: Does not inhibit ribosome binding.
- G745 (= G436) mutation to D: Does not inhibit ribosome binding.
- E768 (= E459) mutation to Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477.
- H797 (= H488) mutation to L: Does not inhibit ribosome binding.
Sites not aligning to the query:
- 109 modified: Phosphoserine; by CK2; S→A: Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-140. Does not inhibit interaction with EIF2; when associated with S-140. Does not inhibit association with ribosomes; when associated with S-140. Reduces EIF2 interaction with ribosomes; when associated with S-140. Does not inhibit protein synthesis; when associated with A-140.
- 140 modified: Phosphoserine; by CK2; S→A: Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-109. Does not inhibits interaction with EIF2; when associated with S-109. Does not inhibit association with ribosomes; when associated with S-109. Reduces EIF2 interaction with ribosomes; when associated with S-109. Does not inhibit protein synthesis; when associated with A-109.
Query Sequence
>WP_013834982.1 NCBI__GCF_000214825.1:WP_013834982.1
MALLFLRDISLSFGAAPLLNKIHFQVETGERVCIVGRNGEGKSTLLKVIEGIQPADEGSR
IVQDGVKIAKLQQDVPHDIQGSVFDVVALGLGDIGETLKAYHHAALEGDMDQLEKLQHKI
EAQNGWDMNQQVDTILSKLDLPADDEFASLSGGMKRRVLLAQALIQKPDILLLDEPTNHL
DIPSIQWLEGFVKNLRCALVFITHDRAFLQALATRIVEVDRGQLYSWDCDYATYLERKQA
QLESEAKSNSEFDKKLAQEEVWIRQGIKARRTRNEGRVRALEKLRLERQARRSQQGSANL
QVNVADTSGKKVIKIEHLCFGWPDKTIVQDFSTVIMRGDKVGLIGPNGCGKSTLLKLLLG
QEQPQQGKVELGTNLQIAYFDQHRAKLNEELSVAENVMDSSDYVEINGQRKHIIGYLSDF
LFAPDRARQPVKSLSGGERNRLLLAQVFAKPSNLLILDEPTNDLDVETLELLEDLLLNYQ
GTVLIVSHDRAFLNNVVTSSIVFDAPGLVNEYVGGYDDWLRQRPNLEANAGANKSSANKQ
TKNATQAPAPKTEKKLSYKDQREYDALPGLIEQLETQLETLSGQIAEPDFYQQEQTKIDK
HLAKIQHKEQELEQAFERWEELEGLVNG
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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