SitesBLAST
Comparing 5207683 FitnessBrowser__PV4:5207683 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
P59846 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
53% identity, 97% coverage: 12:404/407 of query aligns to 2:392/400 of P59846
- 6:14 (vs. 16:24, 100% identical) binding
- A33 (= A44) binding
- G114 (= G126) binding
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
53% identity, 97% coverage: 12:404/407 of query aligns to 2:383/386 of 1j20A
- active site: D12 (= D22), R92 (= R104), D121 (= D133), S168 (= S185)
- binding adenosine monophosphate: A6 (= A16), T13 (= T23), A33 (= A44), R92 (= R104), H113 (= H125), G114 (= G126), F125 (= F137)
- binding argininosuccinate: Y84 (= Y96), T88 (= T100), A115 (≠ C127), T116 (= T128), G119 (= G131), N120 (= N132), D121 (= D133), R124 (= R136), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
53% identity, 97% coverage: 12:404/407 of query aligns to 2:383/386 of 1j1zA
- active site: D12 (= D22), R92 (= R104), D121 (= D133), S168 (= S185)
- binding aspartic acid: A115 (≠ C127), T116 (= T128), G119 (= G131), N120 (= N132), D121 (= D133)
- binding adenosine-5'-triphosphate: A6 (= A16), T13 (= T23), A33 (= A44), R92 (= R104), I95 (= I107), H113 (= H125), G114 (= G126), F125 (= F137)
- binding citrulline: Y84 (= Y96), T88 (= T100), R124 (= R136), S168 (= S185), M169 (≠ R186), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
53% identity, 97% coverage: 12:404/407 of query aligns to 2:377/380 of 1kh3A
- active site: D12 (= D22), R92 (= R104), D121 (= D133), S168 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A16), T13 (= T23), T32 (≠ C43), A33 (= A44), H113 (= H125), G114 (= G126), F125 (= F137), S168 (= S185), M169 (≠ R186)
- binding arginine: Y84 (= Y96), T88 (= T100), R124 (= R136), S168 (= S185), M169 (≠ R186), D170 (= D187), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
- binding aspartic acid: A115 (≠ C127), T116 (= T128), G119 (= G131), N120 (= N132), D121 (= D133)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
44% identity, 96% coverage: 10:401/407 of query aligns to 3:379/390 of 7k5zA
- active site: D15 (= D22), R95 (= R104), D124 (= D133), S176 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A16), Y10 (= Y17), S11 (= S18), C37 (≠ A44), G117 (= G126), F128 (= F137)
- binding arginine: Y88 (= Y96), T92 (= T100), D124 (= D133), R127 (= R136), S185 (= S194), E187 (= E196), E261 (= E270), Y273 (= Y282)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
44% identity, 96% coverage: 8:397/407 of query aligns to 2:397/412 of P00966
- V64 (≠ L73) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y96) binding
- T91 (= T100) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S101) binding
- R95 (= R104) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P105) to H: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; to L: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity; to S: in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity
- G117 (= G126) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (≠ C127) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T128) binding ; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N132) binding ; binding
- D124 (= D133) binding ; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R136) binding ; to L: increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to Q: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to W: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs771794639
- R157 (vs. gap) to C: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770585183; to H: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908637
- K165 (≠ A170) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.
- K176 (≠ T181) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
- W179 (≠ Y184) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S185) binding ; to I: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs121908638; to N: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908638
- S189 (= S194) binding
- E191 (= E196) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G197) to V: in CTLN1; decreased protein abundance
- V263 (= V263) to M: in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs192838388
- R265 (= R265) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E270) binding ; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R272) to C: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs762387914; to H: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008; to L: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008
- G280 (= G280) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y282) binding
- T284 (= T284) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L302) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (≠ K304) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G324) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G347) to R: in CTLN1; severe clinical course
- Y359 (≠ Q359) to D: in CTLN1; mild clinical course
- G362 (≠ K362) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G390) to R: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908641
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
44% identity, 95% coverage: 13:397/407 of query aligns to 4:392/402 of 2nz2A
- active site: D13 (= D22), R92 (= R104), D121 (= D133), S176 (= S185)
- binding aspartic acid: A115 (≠ C127), T116 (= T128), G119 (= G131), N120 (= N132), D121 (= D133)
- binding citrulline: Y84 (= Y96), T88 (= T100), N120 (= N132), R124 (= R136), D178 (= D187), S185 (= S194), E187 (= E196), E266 (= E270), Y278 (= Y282)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
40% identity, 97% coverage: 11:403/407 of query aligns to 2:392/397 of 4xfjB
- active site: D13 (= D22), R94 (= R104), D123 (= D133), S174 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A16), Y8 (= Y17), S9 (= S18), T14 (= T23), I34 (≠ A44), G116 (= G126), C117 (= C127), F127 (= F137)
- binding arginine: Y86 (= Y96), S90 (≠ T100), R126 (= R136), A183 (≠ S194), E185 (= E196), E259 (= E270), E269 (≠ G280), Y271 (= Y282)
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
30% identity, 91% coverage: 2:373/407 of query aligns to 2:384/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
30% identity, 91% coverage: 2:373/407 of query aligns to 6:388/445 of 5us8A
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
27% identity, 92% coverage: 11:385/407 of query aligns to 11:396/439 of 1kp3A
- active site: D22 (= D22), R106 (= R104), D135 (= D133), S191 (= S185)
- binding adenosine-5'-triphosphate: A16 (= A16), S18 (= S18), G20 (= G20), D22 (= D22), T23 (= T23), T41 (≠ C43), A42 (= A44), D127 (≠ H125), G128 (= G126), S129 (≠ C127), F139 (= F137), D193 (= D187)
- binding citrulline: Y98 (= Y96), T102 (= T100), P103 (≠ S101), T130 (= T128), G133 (= G131), N134 (= N132), D135 (= D133), R138 (= R136), D193 (= D187), T200 (≠ S194), E202 (= E196), E202 (= E196), E279 (= E270), S287 (= S278), Y291 (= Y282)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 95% coverage: 11:397/407 of query aligns to 12:410/447 of P0A6E4
- 17:25 (vs. 16:24, 89% identical) binding
- A43 (= A44) binding
- Y99 (= Y96) binding
- G129 (= G126) binding
- T131 (= T128) binding ; binding
- N135 (= N132) binding ; binding
- D136 (= D133) binding ; binding
- R139 (= R136) binding
- S192 (= S185) binding
- D194 (= D187) binding
- T201 (≠ S194) binding
- E203 (= E196) binding
- E280 (= E270) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
27% identity, 92% coverage: 11:385/407 of query aligns to 11:395/432 of 1k97A
- active site: D22 (= D22), R106 (= R104), D135 (= D133), S191 (= S185)
- binding aspartic acid: S129 (≠ C127), T130 (= T128), G133 (= G131), N134 (= N132), D135 (= D133)
- binding citrulline: Y98 (= Y96), T102 (= T100), P103 (≠ S101), R138 (= R136), S191 (= S185), T192 (≠ R186), D193 (= D187), T200 (≠ S194), E202 (= E196), E279 (= E270), Y291 (= Y282), Y331 (= Y322)
Query Sequence
>5207683 FitnessBrowser__PV4:5207683
MSIENNKASVKKVVLAYSGGLDTSAIIPWLKETYDNCEIVAFCADVGQGEAELEGLHEKA
IASGASECYIVDLKEELVADYIYPTIATGAIYEGTYLLGTSMARPIIAKAQVEVARKVGA
DAVCHGCTGKGNDQVRFEGCFAALAPDLTVIAPWREWSMVSREDLLDYLAERNIKTTASA
TKIYSRDANAWHISHEGGELEDPWNEPSKEVWTMTVAPEDAPDEPEYVSVEMEAGRITKV
NGQSYTPYGALMALNEIAGAHGVGRIDITENRLVGMKSRGCYETPGGTVMFAALRAIEEL
VLDKTSREWREQVGAKMAHLVYDGRWFTPLCESLLGASQPLANLLNGEVVLKLYKGQAQA
VKKRSPNSLYSEEFATFGEDEVYNQKDAEGFIRLYSLASRIRALNVK
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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