SitesBLAST
Comparing BWI76_RS16130 FitnessBrowser__Koxy:BWI76_RS16130 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)
40% identity, 98% coverage: 2:444/450 of query aligns to 21:472/476 of A0A0K2JL82
- N93 (= N74) mutation to A: Slight decrease in activity.
- D125 (= D106) mutation D->N,V: Almost loss of activity.
- R137 (≠ G118) binding
- R140 (≠ A121) binding
- R201 (= R182) binding
- H253 (= H225) mutation to A: Loss of activity.
- S302 (= S274) mutation to A: Loss of activity.
- K308 (= K280) binding ; mutation to A: Loss of activity.
- N310 (= N282) binding ; mutation to A: Loss of activity.
- R341 (= R313) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
39% identity, 98% coverage: 2:442/450 of query aligns to 7:439/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
27% identity, 91% coverage: 17:425/450 of query aligns to 13:410/427 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)
27% identity, 92% coverage: 13:424/450 of query aligns to 10:413/431 of P12047
- H89 (= H99) mutation to Q: Abolishes enzyme activity.
- H141 (≠ W151) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W224) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N282) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R313) 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, 92% coverage: 11:424/450 of query aligns to 8:413/431 of Q9X0I0
- H141 (≠ W151) active site, Proton donor/acceptor
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
23% identity, 75% coverage: 10:348/450 of query aligns to 7:324/419 of 5hw2A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
23% identity, 75% coverage: 10:348/450 of query aligns to 7:324/423 of 4eeiB
- active site: H67 (≠ G66), S140 (≠ T150), H141 (≠ W151), K256 (= K280), E263 (≠ A287)
- binding adenosine monophosphate: K66 (≠ L65), H67 (≠ G66), D68 (≠ Q67), Q212 (= Q227), R289 (= R313), I291 (≠ L315), S294 (≠ W318), R298 (≠ W322)
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, 78% coverage: 93:442/450 of query aligns to 98:460/482 of Q05911
- K196 (≠ G191) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
26% identity, 78% coverage: 93:442/450 of query aligns to 98:457/469 of 5vkwB
Sites not aligning to the query:
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
30% identity, 45% coverage: 95:298/450 of query aligns to 94:295/451 of 1tj7B
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
30% identity, 48% coverage: 86:303/450 of query aligns to 95:310/464 of P04424
- R95 (= R86) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (≠ S104) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ G111) to E: in ARGINSA; severe
- V178 (≠ D169) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L172) to S: in a breast cancer sample; somatic mutation
- R182 (= R173) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R177) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G191) to V: in a breast cancer sample; somatic mutation
- R236 (= R228) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D229) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ H279) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R281) 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 (≠ L290) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ L299) to W: in ARGINSA; severe; dbSNP:rs868834862
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
- 326 Q → L: in ARGINSA; severe
- 335 V → L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- 360 M → T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- 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
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, 48% coverage: 86:303/450 of query aligns to 97:312/468 of P24058
- N116 (≠ Q105) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D106) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T150) 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 (≠ W151) mutation to E: Loss of activity.
- R238 (= R228) mutation to Q: Loss of activity.
- T281 (≠ R271) 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 (≠ I284) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A287) mutation to D: 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.
- 323 binding in chain A
- 325 K→N: 99% decrease in catalytic efficiency.
- 328 binding in chain A
- 330 D→N: Loss of activity.
- 331 binding in chain A; K→Q: Loss of activity.
4adlA Crystal structures of rv1098c in complex with malate (see paper)
25% identity, 72% coverage: 103:424/450 of query aligns to 130:451/459 of 4adlA
Sites not aligning to the query:
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
27% identity, 48% coverage: 86:303/450 of query aligns to 80:295/450 of 1k7wD
Sites not aligning to the query:
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
27% identity, 48% coverage: 86:303/450 of query aligns to 95:310/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
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)
25% identity, 72% coverage: 103:424/450 of query aligns to 138:459/474 of P9WN93
- SSN 138:140 (≠ TSQ 103:105) binding
- T186 (= T150) binding
- S318 (= S274) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S275) binding
- KVN 324:326 (≠ KRN 280:282) binding
Sites not aligning to the query:
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
29% identity, 46% coverage: 103:311/450 of query aligns to 139:355/464 of 7c18B
Sites not aligning to the query:
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
31% identity, 41% coverage: 127:311/450 of query aligns to 163:354/462 of 7lubB
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
31% identity, 41% coverage: 127:311/450 of query aligns to 211:402/510 of P07954
- K230 (≠ M146) to R: in FMRD and HLRCC; dbSNP:rs752232718
- R233 (= R149) to H: in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair; dbSNP:rs121913123
- T236 (≠ M152) modified: Phosphothreonine; by PRKDC; mutation to A: Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage.; mutation to D: Phosphomimetic mutant; promotes interaction with H2AZ1, leading to increased localization to chromatin in response to DNA damage.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 1:43 modified: Variant sequence, Missing (in isoform Cytoplasmic)
- 46 S→A: Does not affect phosphorylation by PRKDC.
- 147 T→A: Does not affect phosphorylation by PRKDC.
- 187 S→A: Does not affect phosphorylation by PRKDC.
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
25% identity, 72% coverage: 103:424/450 of query aligns to 130:451/462 of 4apbD
- active site: H179 (≠ W151), C310 (≠ S274), K316 (= K280), E323 (≠ A287)
- binding fumaric acid: S130 (≠ T103), S131 (= S104), N132 (≠ Q105), T178 (= T150), H179 (≠ W151), C310 (≠ S274), S311 (= S275), M313 (= M277), K316 (= K280), N318 (= N282)
Sites not aligning to the query:
Query Sequence
>BWI76_RS16130 FitnessBrowser__Koxy:BWI76_RS16130
MSLLTPMMRTSPLTAWFSDAQRVQGMLDFEAALARAQVECGLVPQAALTPILETCRHENI
DFAALGQAAASAGNLAIPLVKQLTARVRERDEAAARYLHWGATSQDAIDTGFILQLRGAL
AETESLLQRLLDALASQAQRYQDTVMPGRTWMQHALPVTFGLKLAGTLDALLRWQTRLRE
MRSRVLALQFGGAAGTLDSLKTQAPQVAIALAKTLDLQLPDTPWHSQRDRLLEVGAWYAG
VCGTLGKFANDFSLLMQSEVAEVAEPVAEGRGGSSTMPHKRNPIACAAILTAAQRTPGLV
ATLYTGQIQQHERALGGWQAEWETLPELMTLVGGALAQSEALVRDMQVFPPKMRADLEIT
HGLIMAEAVTLALAEFIGKADAHHRIEALCRQALDTSCSLQSVLENDPQVSEHLSADRLT
QLLDPTTATGSAALFVRQVVARYKEQLHEC
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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