SitesBLAST
Comparing 353259 FitnessBrowser__Btheta:353259 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)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
37% identity, 81% coverage: 28:390/446 of query aligns to 20:383/451 of 1tj7B
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
37% identity, 81% coverage: 28:390/446 of query aligns to 16:380/450 of 2e9fB
- active site: E71 (= E83), T146 (= T156), H147 (= H157), S268 (= S279), S269 (= S280), K274 (= K285), E281 (= E292)
- binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y308 (= Y319), Q313 (= Q324), K316 (= K327)
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)
33% identity, 94% coverage: 28:445/446 of query aligns to 33:444/468 of P24058
- D33 (= D28) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D84) mutation to N: Loss of activity.
- N116 (= N111) 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 (= H157) mutation to E: Loss of activity.
- R238 (= R233) mutation to Q: Loss of activity.
- T281 (= T277) 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 (= D289) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E292) mutation to D: Loss of activity.
- Y323 (= Y319) binding in chain A
- K325 (≠ R321) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q324) binding in chain A
- D330 (≠ I326) mutation to N: Loss of activity.
- K331 (= K327) 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.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
32% identity, 94% coverage: 28:445/446 of query aligns to 16:427/450 of 1k7wD
- active site: E71 (= E83), T144 (= T156), H145 (= H157), A266 (≠ S279), S267 (= S280), K272 (= K285), E279 (= E292)
- binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
31% identity, 93% coverage: 31:445/446 of query aligns to 17:425/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
32% identity, 88% coverage: 31:423/446 of query aligns to 34:416/466 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)
32% identity, 81% coverage: 28:390/446 of query aligns to 31:392/464 of P04424
- D31 (= D28) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ S48) mutation to N: 2-fold reduction in activity.
- K69 (≠ T66) modified: N6-acetyllysine
- E73 (≠ S70) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D84) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H86) mutation to Q: 10-fold reduction in activity.
- R94 (≠ L91) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ M92) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R110) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D117) to E: in ARGINSA; severe
- V178 (≠ E175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ V178) to S: in a breast cancer sample; somatic mutation
- R182 (≠ D179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (≠ F183) 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 (= 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 (≠ G234) 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 (= K286) 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 (= R295) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ L304) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q324) to L: in ARGINSA; severe
- V335 (≠ A333) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L358) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M380) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R383) to L: in ARGINSA; severe
- H388 (≠ Y386) to Q: in ARGINSA; severe
Sites not aligning to the query:
- 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- 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
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 84% coverage: 28:401/446 of query aligns to 15:388/418 of 6ienC
- binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
- binding argininosuccinate: T144 (= T156), H145 (= H157), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285)
- binding fumaric acid: S97 (= S109), R98 (= R110), N99 (= N111)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 81% coverage: 28:387/446 of query aligns to 15:375/454 of 6ienB
- binding argininosuccinate: S97 (= S109), R98 (= R110), N99 (= N111), T144 (= T156), H145 (= H157), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 81% coverage: 28:387/446 of query aligns to 15:373/452 of 6ienA
- binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y304 (= Y319), Q309 (= Q324), K312 (= K327)
- binding fumaric acid: S266 (= S279), S267 (= S280), K270 (= K285), N272 (= N287)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 57% coverage: 41:295/446 of query aligns to 45:292/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
31% identity, 57% coverage: 41:295/446 of query aligns to 45:292/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
31% identity, 57% coverage: 41:295/446 of query aligns to 45:292/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
31% identity, 57% coverage: 41:295/446 of query aligns to 45:292/496 of 6g3iA
Sites not aligning to the query:
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)
24% identity, 57% coverage: 131:386/446 of query aligns to 115:372/431 of Q9X0I0
- H141 (= H157) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 76% coverage: 49:389/446 of query aligns to 36:374/427 of 2x75A
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)
29% identity, 37% coverage: 122:288/446 of query aligns to 152:327/474 of P9WN93
- T186 (= T156) binding
- S318 (= S279) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S280) binding
- KVN 324:326 (≠ KKN 285:287) binding
Sites not aligning to the query:
- 104:106 binding
- 138:140 binding
4adlA Crystal structures of rv1098c in complex with malate (see paper)
29% identity, 38% coverage: 122:292/446 of query aligns to 144:323/459 of 4adlA
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)
23% identity, 52% coverage: 93:323/446 of query aligns to 77:303/431 of P12047
- H89 (= H105) mutation to Q: Abolishes enzyme activity.
- H141 (= H157) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ V227) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N287) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R321) mutation R->K,Q: Abolishes enzyme activity.
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
28% identity, 38% coverage: 122:292/446 of query aligns to 144:323/462 of 4apbD
Sites not aligning to the query:
Query Sequence
>353259 FitnessBrowser__Btheta:353259
MAQKLWEKSVQVNKDIERFTVGRDREMDLYLAKHDVLGSMAHITMLESIGLLTKEELEQL
LAELKTIYASVERGEFIIEEGVEDVHSQVELMLTRRLGDVGKKIHSGRSRNDQVLLDLKL
FTRTQIREIAEAVEQLFHVLILQSERYKNVLMPGYTHLQIAMPSSFGLWFGAYAESLVDD
MQFLQAAFRMCNRNPLGSAAGYGSSFPLNRTMTTDLLGFDSLNYNVVYAQMGRGKLERNV
AFALATIAGTISKLAFDACMFNSQNFGFVKLPDDCTTGSSIMPHKKNPDVFELTRAKCNK
LQSLPQQIMMIANNLPSGYFRDLQIIKEVFLPAFQELKDCLQMTTYIMNEIKVNEHILDD
DKYLFIFSVEEVNRLAREGMPFRDAYKKVGLDIEAGKFTHDKQVHHTHEGSIGNLCNDEI
SALMQQVVDGFNFCGMEQAEKALLGR
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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