SitesBLAST
Comparing GFF334 FitnessBrowser__Phaeo:GFF334 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)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
51% identity, 96% coverage: 9:447/456 of query aligns to 1:440/450 of 2e9fB
- active site: E71 (= E79), T146 (= T152), H147 (= H153), S268 (= S274), S269 (= S275), K274 (= K280), E281 (= E287)
- binding arginine: R98 (= R106), N99 (= N107), V102 (= V110), Y308 (= Y314), Q313 (= Q319), K316 (= K322)
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)
44% identity, 100% coverage: 1:454/456 of query aligns to 10:461/468 of P24058
- W11 (= W2) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
- S29 (= S20) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D24) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D80) mutation to N: Loss of activity.
- N116 (= N107) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D108) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T152) 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 (= H153) mutation to E: Loss of activity.
- R238 (= R229) mutation to Q: Loss of activity.
- T281 (= T272) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S274) 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 (= N282) binding in chain B; mutation to L: Loss of activity.
- D293 (= D284) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E287) mutation to D: Loss of activity.
- Y323 (= Y314) binding in chain A
- K325 (= K316) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q319) binding in chain A
- D330 (= D321) mutation to N: Loss of activity.
- K331 (= K322) binding in chain A; mutation to Q: Loss of activity.
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
48% identity, 97% coverage: 5:448/456 of query aligns to 1:444/451 of 1tj7B
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 97% coverage: 11:454/456 of query aligns to 3:444/450 of 1k7wD
- active site: E71 (= E79), T144 (= T152), H145 (= H153), A266 (≠ S274), S267 (= S275), K272 (= K280), E279 (= E287)
- binding argininosuccinate: R98 (= R106), N99 (= N107), V102 (= V110), T144 (= T152), H145 (= H153), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 97% coverage: 11:454/456 of query aligns to 1:442/447 of 1hy0A
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 98% coverage: 1:447/456 of query aligns to 8:452/464 of P04424
- R12 (= R5) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D24) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ A44) mutation to N: 2-fold reduction in activity.
- K69 (≠ T62) modified: N6-acetyllysine
- E73 (= E66) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D80) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H82) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A87) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R88) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R106) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D113) to E: in ARGINSA; severe
- V178 (≠ E171) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ G174) to S: in a breast cancer sample; somatic mutation
- R182 (= R175) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G193) to V: in a breast cancer sample; somatic mutation
- R236 (= R229) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D230) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q279) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K281) 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 (= R290) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A299) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q319) to L: in ARGINSA; severe
- V335 (≠ A328) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L353) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V377) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R380) to L: in ARGINSA; severe
- H388 (= H383) to Q: in ARGINSA; severe
- A398 (= A393) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
Sites not aligning to the query:
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 100% coverage: 1:454/456 of query aligns to 8:459/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 96% coverage: 10:447/456 of query aligns to 1:438/454 of 6ienB
- binding argininosuccinate: S97 (= S105), R98 (= R106), N99 (= N107), T144 (= T152), H145 (= H153), S266 (= S274), S267 (= S275), M269 (= M277), K272 (= K280), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 96% coverage: 10:447/456 of query aligns to 1:436/452 of 6ienA
- binding argininosuccinate: R98 (= R106), N99 (= N107), V102 (= V110), T144 (= T152), H145 (= H153), Y304 (= Y314), Q309 (= Q319), K312 (= K322)
- binding fumaric acid: S266 (= S274), S267 (= S275), K270 (= K280), N272 (= N282)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 96% coverage: 10:447/456 of query aligns to 1:402/418 of 6ienC
- binding arginine: R98 (= R106), N99 (= N107), V102 (= V110), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
- binding argininosuccinate: T144 (= T152), H145 (= H153), S266 (= S274), S267 (= S275), M269 (= M277), K272 (= K280)
- binding fumaric acid: S97 (= S105), R98 (= R106), N99 (= N107)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
33% identity, 90% coverage: 36:447/456 of query aligns to 44:454/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
33% identity, 90% coverage: 36:447/456 of query aligns to 44:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
33% identity, 90% coverage: 36:447/456 of query aligns to 44:454/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
33% identity, 90% coverage: 36:447/456 of query aligns to 44:454/496 of 6g3iA
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
25% identity, 59% coverage: 32:298/456 of query aligns to 33:339/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
25% identity, 59% coverage: 32:298/456 of query aligns to 32:338/462 of 3r6qA
Sites not aligning to the query:
P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
28% identity, 49% coverage: 82:303/456 of query aligns to 109:347/474 of P9WN93
- SSN 138:140 (≠ ATD 111:113) binding
- T186 (= T152) binding
- S318 (= S274) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S275) binding
- KVN 324:326 (≠ KKN 280:282) binding
Sites not aligning to the query:
4adlA Crystal structures of rv1098c in complex with malate (see paper)
28% identity, 49% coverage: 82:303/456 of query aligns to 101:339/459 of 4adlA
Sites not aligning to the query:
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
28% identity, 49% coverage: 82:303/456 of query aligns to 101:339/462 of 4apbD
- active site: H179 (= H153), C310 (≠ S274), K316 (= K280), E323 (= E287)
- binding fumaric acid: S130 (≠ A111), S131 (≠ T112), N132 (≠ D113), T178 (= T152), H179 (= H153), C310 (≠ S274), S311 (= S275), M313 (= M277), K316 (= K280), N318 (= N282)
Sites not aligning to the query:
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
23% identity, 51% coverage: 88:318/456 of query aligns to 75:302/427 of 2x75A
Sites not aligning to the query:
Query Sequence
>GFF334 FitnessBrowser__Phaeo:GFF334
MWGGRFAAGPDAIMEAINASIGFDKRMAAQDIAGSRAHAAMLAATGVITDNDAEAIREGL
LTVLSEIEGGTFQFSTALEDIHMNVEARLKDIIGEPAGRLHTGRSRNDQVATDFKLWVRD
QLDAAESGLLALIRALLSQAEAGADWVMPGFTHLQTAQPVTWGHHMMAYVEMFGRDLSRV
RDARKRMNESPLGAAALAGTSFPIDREMTASALGFDRPAANSLDAVSDRDFALEFLSVAS
ISAVHLSRFAEELVIWSSAQFRFVTLSDRFSTGSSIMPQKKNPDAAELIRAKVGRIFGAN
TALMMVMKGLPLAYSKDMQEDKEQVFDAADNWMLALAAMEGMVKDMTGNRAELAAAAGSG
FSTATDLADWMVRVLKVPFRDAHHVTGTLVAMAESRGCDLPDLTLADMQGVHEGITEDIF
SVLGVENSVNSRMSYGGTAPAQVRAQIARWQDVLSD
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