SitesBLAST
Comparing GFF445 FitnessBrowser__Phaeo:GFF445 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
33% identity, 91% coverage: 5:414/449 of query aligns to 17:439/476 of A0A0K2JL82
- N93 (≠ V81) mutation to A: Slight decrease in activity.
- D125 (= D111) mutation D->N,V: Almost loss of activity.
- R137 (≠ Q123) binding
- R140 (≠ A126) binding
- R201 (= R187) binding
- H253 (= H230) mutation to A: Loss of activity.
- S302 (= S276) mutation to A: Loss of activity.
- K308 (= K282) binding ; mutation to A: Loss of activity.
- N310 (= N284) binding ; mutation to A: Loss of activity.
- R341 (= R315) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
33% identity, 91% coverage: 5:414/449 of query aligns to 3:408/439 of 5xnzA
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 87% coverage: 15:406/449 of query aligns to 5:393/431 of P12047
- H89 (= H104) mutation to Q: Abolishes enzyme activity.
- H141 (≠ Y156) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ V223) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N284) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R315) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 87% coverage: 15:405/449 of query aligns to 4:391/427 of 2x75A
Sites not aligning to the query:
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)
24% identity, 94% coverage: 15:437/449 of query aligns to 5:430/431 of Q9X0I0
- H141 (≠ Y156) active site, Proton donor/acceptor
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
23% identity, 89% coverage: 15:414/449 of query aligns to 5:391/419 of 5hw2A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
25% identity, 70% coverage: 15:328/449 of query aligns to 5:302/423 of 4eeiB
- active site: H67 (≠ V81), S140 (≠ T155), H141 (≠ Y156), K256 (= K282), E263 (≠ S289)
- binding adenosine monophosphate: K66 (≠ G80), H67 (≠ V81), D68 (≠ P82), Q212 (≠ D232), R289 (= R315), I291 (≠ G317), S294 (≠ W320), R298 (≠ W324)
2qgaC Plasmodium vivax adenylosuccinate lyase pv003765 with amp bound
26% identity, 41% coverage: 101:286/449 of query aligns to 112:298/455 of 2qgaC
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)
23% identity, 95% coverage: 12:437/449 of query aligns to 18:462/484 of P30566
- M26 (≠ V20) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ G70) to V: in ADSLD; severe
- P100 (= P97) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D111) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ Q138) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ Y156) active site, Proton donor/acceptor
- R190 (= R187) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L191) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ S234) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D256) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S276) active site, Proton donor/acceptor
- R303 (≠ A290) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (vs. gap) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ A304) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (≠ P350) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ H360) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (≠ R380) to R: in ADSLD; severe
- R396 (= R381) 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 (vs. gap) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (vs. gap) to V: in ADSLD; moderate
- R426 (≠ L402) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ A406) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (vs. gap) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ T422) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L425) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ S427) 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
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
22% identity, 95% coverage: 12:437/449 of query aligns to 11:455/477 of 5nx9D
- active site: H79 (≠ D92), T151 (= T155), H152 (≠ Y156), S283 (= S277), K288 (= K282), E295 (≠ S289)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T155), H152 (≠ Y156)
- binding adenosine monophosphate: R13 (≠ L14), Y14 (≠ F15), R78 (= R91), H79 (≠ D92), D80 (≠ E93), S105 (= S109), Q234 (≠ L220), R296 (≠ A290), L324 (≠ G317), S327 (≠ W320), A328 (≠ F321), R331 (≠ W324)
- binding fumaric acid: H79 (≠ D92), S105 (= S109), Q234 (≠ L220), S282 (= S276), S283 (= S277), K288 (= K282)
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
22% identity, 89% coverage: 40:437/449 of query aligns to 40:459/482 of Q05911
- K196 (≠ S196) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
23% identity, 78% coverage: 96:443/449 of query aligns to 96:460/469 of 5vkwB
Sites not aligning to the query:
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
26% identity, 42% coverage: 100:286/449 of query aligns to 127:318/469 of 3gzhA
Sites not aligning to the query:
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
26% identity, 42% coverage: 100:286/449 of query aligns to 114:305/456 of P0AB89
- TS 122:123 (= TS 108:109) binding ; binding
- H171 (≠ Y156) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (≠ W229) binding ; binding ; binding
- S295 (= S276) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S277) binding ; binding
- KVN 301:303 (≠ KQN 282:284) binding ; binding
Sites not aligning to the query:
- 15:16 binding ; binding
- 90:92 binding ; binding
- 91 binding
- 94 modified: N6-acetyllysine
- 309 binding ; binding
- 335 binding ; binding
- 340:344 binding ; binding
- 366 modified: N6-acetyllysine
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 43% coverage: 12:205/449 of query aligns to 11:201/464 of 5nxaA
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 43% coverage: 12:205/449 of query aligns to 10:200/418 of 5nxaC
Sites not aligning to the query:
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 43% coverage: 12:205/449 of query aligns to 10:200/441 of 5nx9C
- active site: H78 (≠ D92), T150 (= T155), H151 (≠ Y156)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R12 (≠ L14), Y13 (≠ F15), R77 (= R91), H78 (≠ D92), D79 (≠ E93), T103 (= T108), S104 (= S109)
- binding fumaric acid: T150 (= T155), H151 (≠ Y156)
Sites not aligning to the query:
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
26% identity, 42% coverage: 100:286/449 of query aligns to 114:305/459 of 2ptqA
- active site: T170 (= T155), N171 (≠ Y156), S296 (= S277), K301 (= K282)
- binding adenosine monophosphate: Q247 (≠ W229)
- binding fumaric acid: T122 (= T108), S123 (= S109), Q247 (≠ W229), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
- active site: 91, 308
- binding adenosine monophosphate: 15, 16, 90, 91, 309, 335, 337, 340, 341, 344
- binding fumaric acid: 91
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
26% identity, 42% coverage: 100:286/449 of query aligns to 114:305/454 of 2ptrA
- active site: T170 (= T155), A171 (≠ Y156), K301 (= K282)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T122 (= T108), S123 (= S109), Q247 (≠ W229), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
- active site: 91, 308
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: 15, 16, 91, 92, 309, 335, 337, 340, 341, 344
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
22% identity, 79% coverage: 84:437/449 of query aligns to 17:393/415 of 5nxaB
- active site: T89 (= T155), H90 (≠ Y156), S221 (= S277), K226 (= K282), E233 (≠ S289)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V286), R234 (≠ A290)
- binding fumaric acid: S220 (= S276), S221 (= S277), M223 (= M279), K226 (= K282), N228 (= N284)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S109), T89 (= T155), H90 (≠ Y156), Q172 (≠ L220), L262 (≠ G317), S265 (≠ W320), A266 (≠ F321), R269 (≠ W324)
Sites not aligning to the query:
Query Sequence
>GFF445 FitnessBrowser__Phaeo:GFF445
MAASLFDSQLYASLFSAGDVSRLFSDSAEIRAMLLVEGALAKAQGKLGLIPEDSAAAIGR
AVMEVALDPGALTQAAGQNGVPVPGLVSALRDEMNAPEHAQYVHWGATSQDIMDSALMLR
LRQALAAVETDLLILLTQLSDMADTHANLPMAARTYGQLATPTSFGAVVAAWGQPLAALL
EELPTLRQTCLLVSLSGAAGTSSALGPKASELRAELAAGLSLVDPHRSWHTDRSPVLRIA
DWLTRACTSLSKLGTDCLALRQSGIDELTTITAGASSTMPQKQNPVAASALIALASQATA
QLSALHHAAAHQHQRDGASWFGEWLSLPQIVFCAASAARTAVSMTKGLAPDAKQMLRNLH
AANGTIYAEALSFALAEQMRRGEAQAAVKDLCVKAAQQGVPLQEVAALQFPELDHATLFD
ATRQLGSATYEAQRFVKIVAALKGRKEST
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