SitesBLAST
Comparing CCNA_02572 FitnessBrowser__Caulo:CCNA_02572 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)
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
50% identity, 99% coverage: 1:431/436 of query aligns to 1:428/431 of P12047
- H89 (= H92) mutation to Q: Abolishes enzyme activity.
- H141 (= H144) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q215) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N273) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R304) 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)
49% identity, 99% coverage: 1:430/436 of query aligns to 1:427/431 of Q9X0I0
- H141 (= H144) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
47% identity, 98% coverage: 2:430/436 of query aligns to 1:423/427 of 2x75A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
37% identity, 100% coverage: 1:436/436 of query aligns to 1:419/423 of 4eeiB
- active site: H67 (= H71), S140 (= S143), H141 (= H144), K256 (= K271), E263 (= E278)
- binding adenosine monophosphate: K66 (= K70), H67 (= H71), D68 (= D72), Q212 (= Q215), R289 (= R304), I291 (= I306), S294 (= S309), R298 (= R313)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
40% identity, 87% coverage: 1:379/436 of query aligns to 1:364/419 of 5hw2A
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 100% coverage: 1:435/436 of query aligns to 10:457/477 of 5nx9D
- active site: H79 (= H71), T151 (≠ S143), H152 (= H144), S283 (= S266), K288 (= K271), E295 (= E278)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (≠ S143), H152 (= H144)
- binding adenosine monophosphate: R13 (= R4), Y14 (= Y5), R78 (≠ K70), H79 (= H71), D80 (= D72), S105 (= S97), Q234 (= Q215), R296 (≠ N279), L324 (≠ I306), S327 (= S309), A328 (≠ S310), R331 (= R313)
- binding fumaric acid: H79 (= H71), S105 (= S97), Q234 (= Q215), S282 (= S265), S283 (= S266), K288 (= K271)
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 86% coverage: 3:379/436 of query aligns to 13:401/482 of Q05911
- K196 (≠ S184) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
26% identity, 100% coverage: 1:435/436 of query aligns to 17:464/484 of P30566
- M26 (≠ A10) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ W57) to V: in ADSLD; severe
- P100 (≠ G85) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D99) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A126) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (= H144) active site, Proton donor/acceptor
- R190 (≠ K175) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ A179) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D220) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (≠ E242) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S265) active site, Proton donor/acceptor
- R303 (≠ N279) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V287) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ A294) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (≠ I339) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D349) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (= S370) to R: in ADSLD; severe
- R396 (= R371) 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 (≠ R391) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (≠ F392) to V: in ADSLD; moderate
- R426 (≠ F395) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (= D399) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ T409) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ G418) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (= T421) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ N423) 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
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
27% identity, 83% coverage: 1:364/436 of query aligns to 9:376/472 of 5eytA
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
25% identity, 86% coverage: 3:379/436 of query aligns to 13:394/469 of 5vkwB
Sites not aligning to the query:
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 100% coverage: 1:435/436 of query aligns to 10:444/464 of 5nxaA
- active site: H79 (= H71), T151 (≠ S143), H152 (= H144), K275 (= K271), E282 (= E278)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R13 (= R4), Y14 (= Y5), R78 (≠ K70), H79 (= H71), D80 (= D72), T104 (= T96), S105 (= S97), Q234 (= Q215), K275 (= K271), R283 (≠ N279), L311 (≠ I306), S314 (= S309), A315 (≠ S310), R318 (= R313)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
31% identity, 70% coverage: 60:365/436 of query aligns to 77:402/476 of A0A0K2JL82
- N93 (≠ H71) mutation to A: Slight decrease in activity.
- D125 (= D99) mutation D->N,V: Almost loss of activity.
- R137 (= R111) binding
- R140 (≠ D114) binding
- R201 (≠ K175) binding
- H253 (≠ V216) mutation to A: Loss of activity.
- S302 (= S265) mutation to A: Loss of activity.
- K308 (= K271) binding ; mutation to A: Loss of activity.
- N310 (= N273) binding ; mutation to A: Loss of activity.
- R341 (≠ E296) mutation to A: Loss of activity.
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 79% coverage: 90:435/436 of query aligns to 36:395/415 of 5nxaB
- active site: T89 (≠ S143), H90 (= H144), S221 (= S266), K226 (= K271), E233 (= E278)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ I275), R234 (≠ N279)
- binding fumaric acid: S220 (= S265), S221 (= S266), M223 (= M268), K226 (= K271), N228 (= N273)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S97), T89 (≠ S143), H90 (= H144), Q172 (= Q215), L262 (≠ I306), S265 (= S309), A266 (≠ S310), R269 (= R313)
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, 100% coverage: 1:435/436 of query aligns to 9:433/441 of 5nx9C
- active site: H78 (= H71), T150 (≠ S143), H151 (= H144), E280 (= E278)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R12 (= R4), Y13 (= Y5), R77 (≠ K70), H78 (= H71), D79 (= D72), T103 (= T96), S104 (= S97), Q233 (= Q215), M277 (≠ I275), R281 (≠ N279), L309 (≠ I306), S312 (= S309), A313 (≠ S310), R316 (= R313)
- binding fumaric acid: T150 (≠ S143), H151 (= H144)
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 83% coverage: 1:364/436 of query aligns to 9:370/418 of 5nxaC
- active site: H78 (= H71), T150 (≠ S143), H151 (= H144), K276 (= K271), E283 (= E278)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ K70), H78 (= H71), D79 (= D72), Q233 (= Q215), L312 (≠ I306), S315 (= S309), A316 (≠ S310), R319 (= R313)
- binding fumaric acid: H78 (= H71), T103 (= T96), S104 (= S97), Q233 (= Q215)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R12 (= R4), Y13 (= Y5), T150 (≠ S143), H151 (= H144), K276 (= K271), R284 (≠ N279)
5xnzA Crystal structure of cred complex with fumarate (see paper)
31% identity, 70% coverage: 60:365/436 of query aligns to 63:371/439 of 5xnzA
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
28% identity, 75% coverage: 25:349/436 of query aligns to 55:379/456 of P0AB89
- NHD 90:92 (≠ KHD 70:72) binding ; binding
- H91 (= H71) binding
- K94 (≠ I74) modified: N6-acetyllysine
- TS 122:123 (= TS 96:97) binding ; binding
- H171 (= H144) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (= Q215) binding ; binding ; binding
- S295 (= S265) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S266) binding ; binding
- KVN 301:303 (≠ KRN 271:273) binding ; binding
- N309 (= N279) binding ; binding
- R335 (= R304) binding ; binding
- STVLR 340:344 (≠ SSVER 309:313) binding ; binding
- K366 (≠ R336) modified: N6-acetyllysine
Sites not aligning to the query:
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
29% identity, 67% coverage: 25:316/436 of query aligns to 68:360/469 of 3gzhA
- active site: H104 (= H71), T183 (≠ S143), H184 (= H144), S309 (= S266), K314 (= K271), E321 (= E278)
- binding phosphate ion: H104 (= H71), T135 (= T96), S136 (= S97), S353 (= S309), T354 (≠ S310), R357 (= R313)
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
28% identity, 75% coverage: 25:349/436 of query aligns to 55:379/459 of 2ptqA
- active site: H91 (= H71), T170 (≠ S143), N171 (≠ H144), S296 (= S266), K301 (= K271), E308 (= E278)
- binding adenosine monophosphate: N90 (≠ K70), H91 (= H71), Q247 (= Q215), N309 (= N279), R335 (= R304), L337 (≠ I306), S340 (= S309), T341 (≠ S310), R344 (= R313)
- binding fumaric acid: H91 (= H71), T122 (= T96), S123 (= S97), Q247 (= Q215), S295 (= S265), S296 (= S266), M298 (= M268), K301 (= K271), N303 (= N273)
Sites not aligning to the query:
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
28% identity, 75% coverage: 25:349/436 of query aligns to 55:379/454 of 2ptrA
- active site: H91 (= H71), T170 (≠ S143), A171 (≠ H144), K301 (= K271), E308 (= E278)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: H91 (= H71), D92 (= D72), T122 (= T96), S123 (= S97), Q247 (= Q215), S295 (= S265), S296 (= S266), M298 (= M268), K301 (= K271), N303 (= N273), N309 (= N279), R335 (= R304), L337 (≠ I306), S340 (= S309), T341 (≠ S310), R344 (= R313)
Sites not aligning to the query:
Query Sequence
>CCNA_02572 FitnessBrowser__Caulo:CCNA_02572
MISRYARPEAAAIWSSQTKYKIWFEIEAHAADAMAELGVIPKLAAETIWEKGRDAVWDSD
RIDEIERVTKHDVIAFLTHVSEIVGPEARFLHQGMTSSDVLDTCFAVQLSRATDLLLEDV
DLVLAALKRRALEHKMTVCVGRSHGIHAEPITFGLKLAGYYAEFQRAKERLAMAKFEIAT
CAISGAVGTFANVDPRVEQHVADKMGLAVEPVSTQVIPRDRHAAYFAALGVVASSVERLA
TEIRHLQRTEVLEAEEPFDPGQKGSSAMPHKRNPILTENLTGLARLVRSAVVPAMENVAL
WHERDISHSSVERGIGPDATIHLDFALRRLAGVIERFNIYPDNMAKNLDKLGGLVFSQRV
MLALTHKDVSREDAYAAVQGNAMKVWRGEGRFLDFLKADPVVSKALTETELEELFDLGYH
TKNVDVIFQRVFGEQG
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