SitesBLAST
Comparing PfGW456L13_4586 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4586 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)
42% identity, 94% coverage: 22:449/454 of query aligns to 35:471/476 of A0A0K2JL82
- N93 (= N80) mutation to A: Slight decrease in activity.
- D125 (= D112) mutation D->N,V: Almost loss of activity.
- R137 (= R124) binding
- R140 (≠ E127) binding
- R201 (≠ K188) binding
- H253 (= H231) mutation to A: Loss of activity.
- S302 (= S280) mutation to A: Loss of activity.
- K308 (= K286) binding ; mutation to A: Loss of activity.
- N310 (= N288) binding ; mutation to A: Loss of activity.
- R341 (= R319) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
41% identity, 94% coverage: 22:447/454 of query aligns to 21:438/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
31% identity, 95% coverage: 14:445/454 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: 14:444/454 of query aligns to 5:427/431 of P12047
- H89 (= H105) mutation to Q: Abolishes enzyme activity.
- H141 (≠ W157) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W230) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N288) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R319) 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, 96% coverage: 14:448/454 of query aligns to 5:431/431 of Q9X0I0
- H141 (≠ W157) active site, Proton donor/acceptor
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
24% identity, 92% coverage: 14:432/454 of query aligns to 5:414/423 of 4eeiB
- active site: H67 (≠ N80), S140 (≠ T156), H141 (≠ W157), K256 (= K286), E263 (≠ A293)
- binding adenosine monophosphate: K66 (≠ G79), H67 (≠ N80), D68 (≠ S81), Q212 (= Q233), R289 (= R319), I291 (≠ L321), S294 (≠ W324), R298 (≠ W328)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
24% identity, 92% coverage: 14:432/454 of query aligns to 5:410/419 of 5hw2A
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
25% identity, 96% coverage: 14:448/454 of query aligns to 21:463/484 of P30566
- M26 (= M19) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ Y66) to V: in ADSLD; severe
- P100 (≠ A94) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D112) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ T139) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ W157) active site, Proton donor/acceptor
- R190 (≠ K188) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L192) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ Q233) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D257) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S280) active site, Proton donor/acceptor
- R303 (≠ V294) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V302) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ T308) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V354) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D364) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R385) 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 (≠ V409) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L410) to V: in ADSLD; moderate
- R426 (≠ E413) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ T417) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ A423) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A432) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L435) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ Q437) 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: 14:448/454 of query aligns to 14:456/477 of 5nx9D
- active site: H79 (≠ N80), T151 (= T156), H152 (≠ W157), S283 (= S281), K288 (= K286), E295 (≠ A293)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T156), H152 (≠ W157)
- binding adenosine monophosphate: Y14 (≠ F14), R78 (≠ G79), H79 (≠ N80), D80 (≠ S81), S105 (= S110), Q234 (= Q228), R296 (≠ V294), L324 (= L321), S327 (≠ W324), A328 (≠ H325), R331 (≠ W328)
- binding fumaric acid: H79 (≠ N80), S105 (= S110), Q234 (= Q228), S282 (= S280), S283 (= S281), K288 (= K286)
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)
28% identity, 57% coverage: 104:363/454 of query aligns to 109:366/468 of P24058
- N116 (≠ Q111) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D112) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T156) 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 (≠ W157) mutation to E: Loss of activity.
- R238 (= R234) mutation to Q: Loss of activity.
- T281 (≠ G278) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S280) 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 (= N288) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V290) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A293) mutation to D: Loss of activity.
- Y323 (≠ H317) binding in chain A
- K325 (≠ R319) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ H325) binding in chain A
- D330 (≠ E327) mutation to N: Loss of activity.
- K331 (≠ W328) 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: 104:363/454 of query aligns to 92:349/450 of 1k7wD
- active site: T144 (= T156), H145 (≠ W157), A266 (≠ S280), S267 (= S281), K272 (= K286), E279 (≠ A293)
- binding argininosuccinate: R98 (≠ S110), N99 (≠ Q111), V102 (≠ M114), T144 (= T156), H145 (≠ W157), Y306 (≠ H317), Q311 (≠ H325), K314 (≠ W328)
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: 104:363/454 of query aligns to 90:347/447 of 1hy0A
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 76% coverage: 103:448/454 of query aligns to 36:394/415 of 5nxaB
- active site: T89 (= T156), H90 (≠ W157), S221 (= S281), K226 (= K286), E233 (≠ A293)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V290), R234 (≠ V294)
- binding fumaric acid: S220 (= S280), S221 (= S281), M223 (= M283), K226 (= K286), N228 (= N288)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S110), T89 (= T156), H90 (≠ W157), Q172 (= Q228), L262 (= L321), S265 (≠ W324), A266 (≠ H325), R269 (≠ W328)
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)
29% identity, 48% coverage: 86:304/454 of query aligns to 141:367/488 of P08417
- H154 (≠ E99) 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.
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
29% identity, 55% coverage: 116:363/454 of query aligns to 119:364/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
28% identity, 57% coverage: 104:363/454 of query aligns to 107:364/464 of P04424
- R113 (≠ S110) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ G117) to E: in ARGINSA; severe
- V178 (≠ G175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (= T178) to S: in a breast cancer sample; somatic mutation
- R182 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G197) to V: in a breast cancer sample; somatic mutation
- R236 (= R234) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D235) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ H285) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R287) 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 (≠ I296) 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 (≠ H325) to L: in ARGINSA; severe
- V335 (≠ I334) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M359) 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
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, 76% coverage: 104:446/454 of query aligns to 103:458/482 of Q05911
- K196 (≠ G197) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
29% identity, 52% coverage: 71:304/454 of query aligns to 106:342/461 of Q9ZCQ4
Sites not aligning to the query:
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
28% identity, 52% coverage: 71:304/454 of query aligns to 103:339/456 of 1fuqA
- active site: N104 (≠ G72), T184 (= T156), H185 (≠ W157), S315 (= S280), K321 (= K286), E328 (≠ A293)
- binding citric acid: S136 (≠ T109), S137 (= S110), N138 (≠ Q111)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ K91), H126 (≠ A94), P127 (≠ A95), N128 (≠ T96), D129 (= D97)
Sites not aligning to the query:
1fuoA FumarasE C with bound citrate (see paper)
28% identity, 52% coverage: 71:304/454 of query aligns to 103:339/456 of 1fuoA
Sites not aligning to the query:
Query Sequence
>PfGW456L13_4586 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4586
MNQRPGNQLFDAYFTARDMREVFCDQGRVQAMLDFEAALARAEARVGMIPSSAVAPIEAA
CRAGLYDFAMLGEAIATAGNSAIPLVKALGKQIAATDAEAERYVHLGATSQDVMDSGLVL
QLRRALELIESDLAQLGQTLASQAQRYATTPLAGRTWLQHATPVTLGMKIAGWLGAVTRS
RQRLAELKPRLLVLQFGGASGTLAALGEQAMPIAQALAEELQLTLPDQPWHTQRDRVVEF
GAALGLIAGSLGKLGRDISLLMQTEAAEVFEPSAPGKGGSSTMPHKRNPVGAAVLIGAAT
RVPGLLSTLFSAMPQEHERSLGLWHAEWETLPEICCLVSGSLHQALLIVQGLEVDAERMA
RNLDLTQGLVLAEAVSIVLAQRVGRNTAHHLLEQCCKRAVAEQRHLRAVLGDEPQVTAEL
SAAELDHLLDSAHYLGQAKTWVERAVAEHSALTA
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