SitesBLAST
Comparing AO353_17225 FitnessBrowser__pseudo3_N2E3:AO353_17225 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)
42% identity, 94% coverage: 21:448/453 of query aligns to 35:471/476 of A0A0K2JL82
- N93 (= N79) mutation to A: Slight decrease in activity.
- D125 (= D111) mutation D->N,V: Almost loss of activity.
- R137 (≠ Q123) binding
- R140 (≠ H126) binding
- R201 (≠ K187) binding
- H253 (= H230) mutation to A: Loss of activity.
- S302 (= S279) mutation to A: Loss of activity.
- K308 (= K285) binding ; mutation to A: Loss of activity.
- N310 (= N287) binding ; mutation to A: Loss of activity.
- R341 (= R318) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
42% identity, 94% coverage: 21:446/453 of query aligns to 21:438/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
31% identity, 95% coverage: 13:444/453 of query aligns to 4:424/427 of 2x75A
Sites not aligning to the query:
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, 95% coverage: 13:443/453 of query aligns to 5:427/431 of P12047
- H89 (= H104) mutation to Q: Abolishes enzyme activity.
- H141 (≠ W156) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q232) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N287) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R318) 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)
27% identity, 94% coverage: 18:443/453 of query aligns to 10:427/431 of Q9X0I0
- H141 (≠ W156) active site, Proton donor/acceptor
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
23% identity, 94% coverage: 18:445/453 of query aligns to 10:415/423 of 4eeiB
- active site: H67 (≠ N79), S140 (≠ T155), H141 (≠ W156), K256 (= K285), E263 (≠ A292)
- binding adenosine monophosphate: K66 (≠ G78), H67 (≠ N79), D68 (≠ S80), Q212 (= Q232), R289 (= R318), I291 (≠ L320), S294 (≠ W323), R298 (≠ W327)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
27% identity, 72% coverage: 20:343/453 of query aligns to 12:314/419 of 5hw2A
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
26% identity, 96% coverage: 13:449/453 of query aligns to 21:465/484 of P30566
- M26 (= M18) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ Y65) to V: in ADSLD; severe
- P100 (≠ A93) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D111) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A138) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ W156) active site, Proton donor/acceptor
- R190 (≠ K187) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L191) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ Q232) 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 (= S279) active site, Proton donor/acceptor
- R303 (≠ V293) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V301) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ T307) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V353) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D363) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R384) 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 (≠ V408) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L409) to V: in ADSLD; moderate
- R426 (≠ E412) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ T416) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ A422) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A431) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L434) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ Q436) 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)
25% identity, 96% coverage: 13:449/453 of query aligns to 14:458/477 of 5nx9D
- active site: H79 (≠ N79), T151 (= T155), H152 (≠ W156), S283 (= S280), K288 (= K285), E295 (≠ A292)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T155), H152 (≠ W156)
- binding adenosine monophosphate: Y14 (≠ F13), R78 (≠ G78), H79 (≠ N79), D80 (≠ S80), S105 (= S109), Q234 (= Q227), R296 (≠ V293), L324 (= L320), S327 (≠ W323), A328 (≠ H324), R331 (≠ W327)
- binding fumaric acid: H79 (≠ N79), S105 (= S109), Q234 (= Q227), S282 (= S279), S283 (= S280), K288 (= K285)
Sites not aligning to the query:
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
26% identity, 77% coverage: 85:435/453 of query aligns to 141:486/488 of P08417
- H154 (≠ D98) mutation to R: Abolished fumarate hydratase activity and ability to participate in DNA repair.
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 24 M→S: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.; mutation M->V,I: Abolishes processing by the mitochondrial processing peptidase. Mainly localizes in the cytosol, with a small fraction in the mitochondrion. Reduced fumarate hydratase activity.
- 24:25 MN→SF: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.
- 29:44 mutation Missing: Does not affect subcellular location.
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 77% coverage: 102:449/453 of query aligns to 36:396/415 of 5nxaB
- active site: T89 (= T155), H90 (≠ W156), S221 (= S280), K226 (= K285), E233 (≠ A292)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V289), R234 (≠ V293)
- binding fumaric acid: S220 (= S279), S221 (= S280), M223 (= M282), K226 (= K285), N228 (= N287)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S109), T89 (= T155), H90 (≠ W156), Q172 (= Q227), L262 (= L320), S265 (≠ W323), A266 (≠ H324), R269 (≠ W327)
Sites not aligning to the query:
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)
27% identity, 57% coverage: 103:362/453 of query aligns to 109:366/468 of P24058
- N116 (≠ Q110) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D111) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T155) 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 (≠ W156) mutation to E: Loss of activity.
- R238 (= R233) mutation to Q: Loss of activity.
- T281 (≠ G277) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S279) 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 (= N287) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V289) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A292) mutation to D: Loss of activity.
- Y323 (≠ H316) binding in chain A
- K325 (≠ R318) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ H324) binding in chain A
- D330 (≠ E326) mutation to N: Loss of activity.
- K331 (≠ W327) 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.
- 33 D→N: 99% decrease in catalytic efficiency.
- 89 D→N: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
27% identity, 57% coverage: 103:362/453 of query aligns to 92:349/450 of 1k7wD
- active site: T144 (= T155), H145 (≠ W156), A266 (≠ S279), S267 (= S280), K272 (= K285), E279 (≠ A292)
- binding argininosuccinate: R98 (≠ S109), N99 (≠ Q110), V102 (≠ M113), T144 (= T155), H145 (≠ W156), Y306 (≠ H316), Q311 (≠ H324), K314 (≠ W327)
Sites not aligning to the query:
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
27% identity, 57% coverage: 103:362/453 of query aligns to 90:347/447 of 1hy0A
Sites not aligning to the query:
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 96% coverage: 13:449/453 of query aligns to 15:462/482 of Q05911
- K196 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
29% identity, 57% coverage: 103:362/453 of query aligns to 107:364/464 of P04424
- R113 (≠ S109) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ G116) to E: in ARGINSA; severe
- V178 (≠ G174) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (= T177) to S: in a breast cancer sample; somatic mutation
- R182 (= R178) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R182) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G196) to V: in a breast cancer sample; somatic mutation
- R236 (= R233) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D234) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ H284) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R286) 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 (≠ I295) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (vs. gap) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ H324) to L: in ARGINSA; severe
- V335 (≠ I333) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M358) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
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
- 95 R → C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- 382 M → R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- 385 R → L: in ARGINSA; severe
- 388 H → Q: in ARGINSA; severe
- 398 A → D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 96% coverage: 13:449/453 of query aligns to 14:445/464 of 5nxaA
- active site: H79 (≠ N79), T151 (= T155), H152 (≠ W156), K275 (= K285), E282 (≠ A292)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y14 (≠ F13), R78 (≠ G78), H79 (≠ N79), D80 (≠ S80), T104 (= T108), S105 (= S109), Q234 (= Q227), K275 (= K285), R283 (≠ V293), L311 (= L320), S314 (≠ W323), A315 (≠ H324), R318 (≠ W327)
Sites not aligning to the query:
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
28% identity, 55% coverage: 115:362/453 of query aligns to 119:364/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
Q9ZCQ4 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Rickettsia prowazekii (strain Madrid E) (see paper)
31% identity, 52% coverage: 70:303/453 of query aligns to 106:342/461 of Q9ZCQ4
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, 96% coverage: 13:449/453 of query aligns to 13:434/441 of 5nx9C
- active site: H78 (≠ N79), T150 (= T155), H151 (≠ W156), E280 (≠ A292)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: Y13 (≠ F13), R77 (≠ G78), H78 (≠ N79), D79 (≠ S80), T103 (= T108), S104 (= S109), Q233 (= Q227), M277 (≠ V289), R281 (≠ V293), L309 (= L320), S312 (≠ W323), A313 (≠ H324), R316 (≠ W327)
- binding fumaric acid: T150 (= T155), H151 (≠ W156)
Sites not aligning to the query:
Query Sequence
>AO353_17225 FitnessBrowser__pseudo3_N2E3:AO353_17225
MQRPGNQLFDAYFTARNMREVFSDQGRVQAMLDFEAALARAEARVGLIPASAVAPIEAAC
RAEHYDFAALGEAIAIAGNSAIPLVKALGKQIAAHDQDAERYVHLGATSQDVMDTGLVLQ
VRQALHLIDSDLARLGEALAIQARHHVLTPLAGRTWLQHATPVTLGMKVAGWLGAVTRSR
QRLHALKPRLLVLQFGGASGTLAALGEQAMPIAEALAQELQLTLPEQPWHTQRDRLVEFG
AALGLIAGSLGKLGRDISLLMQTEAAEVFEPSAPGKGGSSTMPHKRNPVGAAVLIGAATR
VPGLLSTLFSAMPQEHERSLGLWHAEWETLPEICCLVSGALQQALLITEGLEVDAERMAQ
NLDLTQGLVLAEAVSIVLAQRIGRDKAHHLLELCCKRAVAEQRHLRAVLGDEPQVTAELS
SAELDQLMNPAHYLGQAQTWVERALAEHVALTA
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