SitesBLAST
Comparing CCNA_02493 FitnessBrowser__Caulo:CCNA_02493 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)
44% identity, 88% coverage: 19:355/382 of query aligns to 36:385/476 of A0A0K2JL82
- N93 (≠ I78) mutation to A: Slight decrease in activity.
- D125 (= D105) mutation D->N,V: Almost loss of activity.
- R137 (≠ T117) binding
- R140 (≠ A120) binding
- R201 (≠ T181) binding
- H253 (= H223) mutation to A: Loss of activity.
- S302 (= S272) mutation to A: Loss of activity.
- K308 (= K278) binding ; mutation to A: Loss of activity.
- N310 (= N280) binding ; mutation to A: Loss of activity.
- R341 (= R311) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
42% identity, 88% coverage: 19:355/382 of query aligns to 22:354/439 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)
29% identity, 90% coverage: 11:355/382 of query aligns to 6:345/431 of P12047
- H89 (= H98) mutation to Q: Abolishes enzyme activity.
- H141 (≠ L150) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W222) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N280) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R311) mutation R->K,Q: Abolishes enzyme activity.
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)
29% identity, 91% coverage: 7:355/382 of query aligns to 3:345/431 of Q9X0I0
- H141 (≠ L150) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
28% identity, 90% coverage: 11:355/382 of query aligns to 5:344/427 of 2x75A
Sites not aligning to the query:
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
28% identity, 88% coverage: 12:346/382 of query aligns to 16:357/477 of 5nx9D
- active site: H79 (≠ I78), T151 (= T149), H152 (≠ L150), S283 (= S273), K288 (= K278), E295 (≠ Q285)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T149), H152 (≠ L150)
- binding adenosine monophosphate: R78 (≠ A77), H79 (≠ I78), D80 (≠ P79), S105 (= S103), Q234 (≠ E219), R296 (≠ V286), L324 (= L313), S327 (≠ W316), A328 (≠ Q317), R331 (≠ G320)
- binding fumaric acid: H79 (≠ I78), S105 (= S103), Q234 (≠ E219), S282 (= S272), S283 (= S273), K288 (= K278)
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)
28% identity, 88% coverage: 12:346/382 of query aligns to 23:364/484 of P30566
- M26 (= M15) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ V63) to V: in ADSLD; severe
- P100 (= P91) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D105) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A132) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ L150) active site, Proton donor/acceptor
- R190 (≠ T181) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ Q185) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ R226) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D249) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S272) active site, Proton donor/acceptor
- R303 (≠ V286) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (= L297) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ A304) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V346) to M: in ADSLD; severe; dbSNP:rs370851726
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
- 374 R → W: in ADSLD; severe; dbSNP:rs376533026
- 395 S → R: in ADSLD; severe
- 396 R → C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; R → H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- 422 D → Y: in ADSLD; moderate; dbSNP:rs119450943
- 423 L → V: in ADSLD; moderate
- 426 R → H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- 430 D → N: in ADSLD; mild; dbSNP:rs554254383
- 438 S → P: in ADSLD; severe; dbSNP:rs119450940
- 447 S → P: in ADSLD; severe; dbSNP:rs777821034
- 450 T → S: in ADSLD; moderate; dbSNP:rs372895468
- 452 R → P: 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)
30% identity, 67% coverage: 91:346/382 of query aligns to 97:361/482 of Q05911
- K196 (≠ G189) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
27% identity, 76% coverage: 68:357/382 of query aligns to 79:362/472 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)
27% identity, 88% coverage: 12:346/382 of query aligns to 15:345/418 of 5nxaC
- active site: H78 (≠ I78), T150 (= T149), H151 (≠ L150), K276 (= K278), E283 (≠ Q285)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ A77), H78 (≠ I78), D79 (≠ P79), Q233 (≠ E219), L312 (= L313), S315 (≠ W316), A316 (≠ Q317), R319 (≠ G320)
- binding fumaric acid: H78 (≠ I78), T103 (= T102), S104 (= S103), Q233 (≠ E219)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: T150 (= T149), H151 (≠ L150), K276 (= K278), R284 (≠ V286)
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
29% identity, 65% coverage: 100:346/382 of query aligns to 40:295/415 of 5nxaB
- active site: T89 (= T149), H90 (≠ L150), S221 (= S273), K226 (= K278), E233 (≠ Q285)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ T282), R234 (≠ V286)
- binding fumaric acid: S220 (= S272), S221 (= S273), M223 (= M275), K226 (= K278), N228 (= N280)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S103), T89 (= T149), H90 (≠ L150), Q172 (≠ E219), L262 (= L313), S265 (≠ W316), A266 (≠ Q317), R269 (≠ G320)
Sites not aligning to the query:
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
25% identity, 68% coverage: 92:349/382 of query aligns to 83:327/419 of 5hw2A
Sites not aligning to the query:
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
25% identity, 68% coverage: 92:349/382 of query aligns to 83:327/423 of 4eeiB
Sites not aligning to the query:
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 88% coverage: 12:346/382 of query aligns to 16:344/464 of 5nxaA
- active site: H79 (≠ I78), T151 (= T149), H152 (≠ L150), K275 (= K278), E282 (≠ Q285)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R78 (≠ A77), H79 (≠ I78), D80 (≠ P79), T104 (= T102), S105 (= S103), Q234 (≠ E219), K275 (= K278), R283 (≠ V286), L311 (= L313), S314 (≠ W316), A315 (≠ Q317), R318 (≠ G320)
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, 88% coverage: 12:346/382 of query aligns to 15:342/441 of 5nx9C
- active site: H78 (≠ I78), T150 (= T149), H151 (≠ L150), E280 (≠ Q285)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R77 (≠ A77), H78 (≠ I78), D79 (≠ P79), T103 (= T102), S104 (= S103), Q233 (≠ E219), M277 (≠ T282), R281 (≠ V286), L309 (= L313), S312 (≠ W316), A313 (≠ Q317), R316 (≠ G320)
- binding fumaric acid: T150 (= T149), H151 (≠ L150)
Sites not aligning to the query:
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
27% identity, 67% coverage: 91:346/382 of query aligns to 97:354/469 of 5vkwB
Sites not aligning to the query:
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
28% identity, 54% coverage: 97:301/382 of query aligns to 133:348/462 of 7lubB
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
28% identity, 54% coverage: 97:301/382 of query aligns to 181:396/510 of P07954
- S187 (= S103) mutation to A: Does not affect phosphorylation by PRKDC.
- K230 (≠ M145) to R: in FMRD and HLRCC; dbSNP:rs752232718
- R233 (= R148) to H: in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair; dbSNP:rs121913123
- T236 (≠ L151) modified: Phosphothreonine; by PRKDC; mutation to A: Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage.; mutation to D: Phosphomimetic mutant; promotes interaction with H2AZ1, leading to increased localization to chromatin in response to DNA damage.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 1:43 modified: Variant sequence, Missing (in isoform Cytoplasmic)
- 46 S→A: Does not affect phosphorylation by PRKDC.
- 147 T→A: Does not affect phosphorylation by PRKDC.
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
27% identity, 53% coverage: 83:285/382 of query aligns to 99:308/454 of 2ptrA
- active site: T170 (= T149), A171 (≠ L150), K301 (= K278), E308 (≠ Q285)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T122 (= T102), S123 (= S103), Q247 (≠ W222), S295 (= S272), S296 (= S273), M298 (= M275), K301 (= K278), N303 (= N280)
Sites not aligning to the query:
- active site: 91
- 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
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
27% identity, 53% coverage: 83:285/382 of query aligns to 99:308/459 of 2ptqA
- active site: T170 (= T149), N171 (≠ L150), S296 (= S273), K301 (= K278), E308 (≠ Q285)
- binding adenosine monophosphate: Q247 (≠ W222)
- binding fumaric acid: T122 (= T102), S123 (= S103), Q247 (≠ W222), S295 (= S272), S296 (= S273), M298 (= M275), K301 (= K278), N303 (= N280)
Sites not aligning to the query:
Query Sequence
>CCNA_02493 FitnessBrowser__Caulo:CCNA_02493
MSCLLRDRPASTPEMLTAFSDEALLRAALTFETMLARAQADVGLIPSDAAETIAIACAEL
PDVVSLAEAAAHAGTLAIPLVALIRERIADPEVAKLVHKGATSQDLADTALMLQAKTGAA
LVLRDASRLAQALAVLAQRHAATPMLGRTLLQAAQPITFGLKAAGWLQGVASALARFERE
TGAIQMQLGGATGSLAGLDGRAGDVAERLAARLGLPAPETPWHARREGLAGLASSLAILT
GAVGKIAGDIALMAQTEVAEAFEPKVVGRGGSSTMAHKRNPTGCQVALSASIRAPHLAAT
ILSALPQQHERGLGGWQVEGPVLAELFELAHGALAAMAIVVEGLEVDADRMAVNLAAARV
GSDIGEAERLVARALNAYPKDR
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