SitesBLAST
Comparing GFF2282 FitnessBrowser__WCS417:GFF2282 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
37% identity, 98% coverage: 5:446/451 of query aligns to 17:471/476 of A0A0K2JL82
- N93 (≠ Y81) mutation to A: Slight decrease in activity.
- D125 (= D109) mutation D->N,V: Almost loss of activity.
- R137 (≠ A121) binding
- R140 (≠ A124) binding
- R201 (= R185) binding
- H253 (= H228) mutation to A: Loss of activity.
- S302 (= S277) mutation to A: Loss of activity.
- K308 (= K283) binding ; mutation to A: Loss of activity.
- N310 (= N285) binding ; mutation to A: Loss of activity.
- R341 (= R316) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
36% identity, 98% coverage: 5:445/451 of query aligns to 3:439/439 of 5xnzA
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
31% identity, 93% coverage: 13:432/451 of query aligns to 3:418/431 of Q9X0I0
- H141 (= H154) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
30% identity, 96% coverage: 13:447/451 of query aligns to 2:425/427 of 2x75A
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
29% identity, 96% coverage: 15:447/451 of query aligns to 5:429/431 of P12047
- H89 (= H102) mutation to Q: Abolishes enzyme activity.
- H141 (= H154) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W227) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N285) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R316) mutation R->K,Q: Abolishes enzyme activity.
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
27% identity, 94% coverage: 15:439/451 of query aligns to 14:450/477 of 5nx9D
- active site: H79 (≠ Y81), T151 (= T153), H152 (= H154), S283 (= S278), K288 (= K283), E295 (= E290)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T153), H152 (= H154)
- binding adenosine monophosphate: Y14 (≠ F15), R78 (≠ G80), H79 (≠ Y81), D80 (≠ P82), S105 (≠ T107), Q234 (≠ W227), R296 (≠ L291), L324 (≠ T318), S327 (≠ W321), A328 (≠ Q322), R331 (≠ W325)
- binding fumaric acid: H79 (≠ Y81), S105 (≠ T107), Q234 (≠ W227), S282 (= S277), S283 (= S278), K288 (= K283)
Sites not aligning to the query:
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
27% identity, 94% coverage: 15:439/451 of query aligns to 21:457/484 of P30566
- M26 (= M20) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ L67) to V: in ADSLD; severe
- P100 (≠ G95) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D109) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ L136) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (= H154) active site, Proton donor/acceptor
- R190 (= R185) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ E189) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D232) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D254) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S277) active site, Proton donor/acceptor
- R303 (≠ L291) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ H302) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (vs. gap) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V351) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D361) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R382) to C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; to H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- D422 (≠ A406) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L407) to V: in ADSLD; moderate
- R426 (≠ Q410) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ T414) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ A420) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A429) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L432) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ L434) to P: in ADSLD; severe
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine; A → V: in ADSLD; severe; dbSNP:rs143083947
- 3 A → V: in ADSLD; severe
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 94% coverage: 15:440/451 of query aligns to 15:455/482 of Q05911
- K196 (≠ A194) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
27% identity, 75% coverage: 15:352/451 of query aligns to 5:325/419 of 5hw2A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
27% identity, 75% coverage: 15:352/451 of query aligns to 5:325/423 of 4eeiB
- active site: H67 (≠ T76), S140 (≠ T153), H141 (= H154), K256 (= K283), E263 (= E290)
- binding adenosine monophosphate: K66 (≠ E75), H67 (≠ T76), D68 (≠ E77), Q212 (≠ W227), R289 (= R316), I291 (≠ T318), S294 (≠ W321), R298 (≠ W325)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
25% identity, 94% coverage: 15:440/451 of query aligns to 15:448/469 of 5vkwB
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 94% coverage: 15:439/451 of query aligns to 14:437/464 of 5nxaA
- active site: H79 (≠ Y81), T151 (= T153), H152 (= H154), K275 (= K283), E282 (= E290)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y14 (≠ F15), R78 (≠ G80), H79 (≠ Y81), D80 (≠ P82), T104 (= T106), S105 (≠ T107), Q234 (≠ W227), K275 (= K283), R283 (≠ L291), L311 (≠ T318), S314 (≠ W321), A315 (≠ Q322), R318 (≠ W325)
Sites not aligning to the query:
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
26% identity, 95% coverage: 15:443/451 of query aligns to 13:449/472 of 5eytA
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 80% coverage: 15:376/451 of query aligns to 13:370/418 of 5nxaC
- active site: H78 (≠ Y81), T150 (= T153), H151 (= H154), K276 (= K283), E283 (= E290)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ G80), H78 (≠ Y81), D79 (≠ P82), Q233 (≠ W227), L312 (≠ T318), S315 (≠ W321), A316 (≠ Q322), R319 (≠ W325)
- binding fumaric acid: H78 (≠ Y81), T103 (= T106), S104 (≠ T107), Q233 (≠ W227)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y13 (≠ F15), T150 (= T153), H151 (= H154), K276 (= K283), R284 (≠ L291)
Sites not aligning to the query:
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
24% identity, 94% coverage: 15:439/451 of query aligns to 13:426/441 of 5nx9C
- active site: H78 (≠ Y81), T150 (= T153), H151 (= H154), E280 (= E290)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: Y13 (≠ F15), R77 (≠ G80), H78 (≠ Y81), D79 (≠ P82), T103 (= T106), S104 (≠ T107), Q233 (≠ W227), M277 (≠ I287), R281 (≠ L291), L309 (≠ T318), S312 (≠ W321), A313 (≠ Q322), R316 (≠ W325)
- binding fumaric acid: T150 (= T153), H151 (= H154)
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 75% coverage: 104:439/451 of query aligns to 40:388/415 of 5nxaB
- active site: T89 (= T153), H90 (= H154), S221 (= S278), K226 (= K283), E233 (= E290)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ I287), R234 (≠ L291)
- binding fumaric acid: S220 (= S277), S221 (= S278), M223 (= M280), K226 (= K283), N228 (= N285)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (≠ T107), T89 (= T153), H90 (= H154), Q172 (≠ W227), L262 (≠ T318), S265 (≠ W321), A266 (≠ Q322), R269 (≠ W325)
Sites not aligning to the query:
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
28% identity, 75% coverage: 89:426/451 of query aligns to 95:417/464 of P04424
- R95 (≠ Q89) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (≠ T107) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ A114) to E: in ARGINSA; severe
- V178 (≠ S172) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ D175) to S: in a breast cancer sample; somatic mutation
- R182 (= R176) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R180) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (≠ A194) to V: in a breast cancer sample; somatic mutation
- R236 (= R231) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D232) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q282) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R284) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
- R297 (≠ Y293) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ Q301) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q322) to L: in ARGINSA; severe
- V335 (≠ A331) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M356) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L376) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R382) to L: in ARGINSA; severe
- H388 (= H386) to Q: in ARGINSA; severe
- A398 (= A396) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
Sites not aligning to the query:
- 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- 31 D → N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- 51 K→N: 2-fold reduction in activity.
- 69 modified: N6-acetyllysine
- 73 E → K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- 87 D → G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- 89 H→Q: 10-fold reduction in activity.
- 94 R → C: in ARGINSA; severe; dbSNP:rs374304304
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
26% identity, 84% coverage: 26:403/451 of query aligns to 33:407/468 of P24058
- D33 (= D26) mutation to N: 99% decrease in catalytic efficiency.
- D89 (≠ E77) mutation to N: Loss of activity.
- N116 (≠ Q108) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D109) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T153) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
- H162 (= H154) mutation to E: Loss of activity.
- R238 (= R231) mutation to Q: Loss of activity.
- T281 (≠ K272) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S277) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
- N291 (= N285) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ I287) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E290) mutation to D: Loss of activity.
- Y323 (≠ F314) binding in chain A
- K325 (≠ R316) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q322) binding in chain A
- D330 (≠ E324) mutation to N: Loss of activity.
- K331 (≠ W325) binding in chain A; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 11 W→A: 98% decrease in catalytic efficiency.; W→F: 90% decrease in catalytic efficiency.; W→M: 99% decrease in catalytic efficiency.; W→R: 97% decrease in catalytic efficiency.; W→Y: 50% decrease in catalytic efficiency.
- 29 binding in chain A; S→A: 10% decrease in catalytic efficiency.
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
27% identity, 60% coverage: 20:290/451 of query aligns to 23:308/456 of P0AB89
- NHD 90:92 (≠ -HE 74:75) binding ; binding
- H91 (= H74) binding
- K94 (≠ E77) modified: N6-acetyllysine
- TS 122:123 (≠ TT 106:107) binding ; binding
- H171 (= H154) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (≠ W227) binding ; binding ; binding
- S295 (= S277) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S278) binding ; binding
- KVN 301:303 (≠ KRN 283:285) binding ; binding
Sites not aligning to the query:
- 15:16 binding ; binding
- 309 binding ; binding
- 335 binding ; binding
- 340:344 binding ; binding
- 366 modified: N6-acetyllysine
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
26% identity, 84% coverage: 26:403/451 of query aligns to 16:390/450 of 1k7wD
- active site: E71 (≠ T76), T144 (= T153), H145 (= H154), A266 (≠ S277), S267 (= S278), K272 (= K283), E279 (= E290)
- binding argininosuccinate: R98 (≠ T107), N99 (≠ Q108), V102 (≠ M111), T144 (= T153), H145 (= H154), Y306 (≠ F314), Q311 (= Q322), K314 (≠ W325)
Query Sequence
>GFF2282 FitnessBrowser__WCS417:GFF2282
MSSTVFDSALFRDMFGTAEMRGVFSDKALIERYIEVEVALARAEARCGVIPTDAAEQIAT
LSQYEALDLALMQHETEIVGYPILPLVEQLSKICGEAGRYVHWGATTQDIMDTAVVLQVR
AALAIVERDIQTVRGLLAGLAERYRDTPMAGRTHLQHALPITFGYKCAVWLSMFDRHAER
LVELRPRVEIGQFAGAAGTLASLGDKGLEVQEALMSELGLGVPQATWHVARDGLAETLNF
LGLVTGSLGKIALDIMMMMTSELGEVYEPFVKGRGASSTMPQKRNPISCELMYAAAKGVR
QHAGLMLDAMIQDFERSTGPWQAEWIAIPEAFALSAASLGQATFMLAGLEVRPERMRKNL
DMTQGLIVAEAVMMGLAPALGRQVAHDVVYAACRMANDQGTSLLDALLAQGEATAQLDLA
ELQRLTDPANYLGLAPQMVDIALARQGAVKR
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