SitesBLAST
Comparing GFF2423 FitnessBrowser__Marino:GFF2423 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)
63% identity, 96% coverage: 11:402/408 of query aligns to 2:391/400 of P59846
- 6:14 (vs. 15:23, 100% identical) binding
- A33 (= A42) binding
- G114 (= G123) binding
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
62% identity, 96% coverage: 11:402/408 of query aligns to 2:382/386 of 1j20A
- active site: D12 (= D21), R92 (= R101), D121 (= D130), S168 (= S183)
- binding adenosine monophosphate: A6 (= A15), T13 (= T22), A33 (= A42), R92 (= R101), H113 (= H122), G114 (= G123), F125 (= F134)
- binding argininosuccinate: Y84 (= Y93), T88 (= T97), A115 (= A124), T116 (= T125), G119 (= G128), N120 (= N129), D121 (= D130), R124 (= R133), S177 (= S192), E179 (= E194), E253 (= E268), Y265 (= Y280)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
62% identity, 96% coverage: 11:402/408 of query aligns to 2:382/386 of 1j1zA
- active site: D12 (= D21), R92 (= R101), D121 (= D130), S168 (= S183)
- binding aspartic acid: A115 (= A124), T116 (= T125), G119 (= G128), N120 (= N129), D121 (= D130)
- binding adenosine-5'-triphosphate: A6 (= A15), T13 (= T22), A33 (= A42), R92 (= R101), I95 (= I104), H113 (= H122), G114 (= G123), F125 (= F134)
- binding citrulline: Y84 (= Y93), T88 (= T97), R124 (= R133), S168 (= S183), M169 (= M184), S177 (= S192), E179 (= E194), E253 (= E268), Y265 (= Y280)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
62% identity, 96% coverage: 11:402/408 of query aligns to 2:376/380 of 1kh3A
- active site: D12 (= D21), R92 (= R101), D121 (= D130), S168 (= S183)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A15), T13 (= T22), T32 (= T41), A33 (= A42), H113 (= H122), G114 (= G123), F125 (= F134), S168 (= S183), M169 (= M184)
- binding arginine: Y84 (= Y93), T88 (= T97), R124 (= R133), S168 (= S183), M169 (= M184), D170 (= D185), S177 (= S192), E179 (= E194), E253 (= E268), Y265 (= Y280)
- binding aspartic acid: A115 (= A124), T116 (= T125), G119 (= G128), N120 (= N129), D121 (= D130)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
46% identity, 97% coverage: 6:399/408 of query aligns to 1:400/412 of P00966
- V64 (≠ L70) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y93) binding
- T91 (= T97) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S98) binding
- R95 (= R101) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P102) 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 (= G123) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A124) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T125) binding ; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N129) binding ; binding
- D124 (= D130) binding ; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R133) 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 (≠ E167) 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 (= K179) 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 (≠ Y182) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S183) 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 (= S192) binding
- E191 (= E194) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G195) to V: in CTLN1; decreased protein abundance
- V263 (≠ I261) 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 (= R263) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E268) binding ; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R270) 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 (= G278) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y280) binding
- T284 (= T282) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L300) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R302) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G322) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G345) to R: in CTLN1; severe clinical course
- Y359 (≠ D357) to D: in CTLN1; mild clinical course
- G362 (= G360) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G389) 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)
46% identity, 95% coverage: 12:399/408 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D21), R92 (= R101), D121 (= D130), S176 (= S183)
- binding aspartic acid: A115 (= A124), T116 (= T125), G119 (= G128), N120 (= N129), D121 (= D130)
- binding citrulline: Y84 (= Y93), T88 (= T97), N120 (= N129), R124 (= R133), D178 (= D185), S185 (= S192), E187 (= E194), E266 (= E268), Y278 (= Y280)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
45% identity, 96% coverage: 9:400/408 of query aligns to 3:379/390 of 7k5zA
- active site: D15 (= D21), R95 (= R101), D124 (= D130), S176 (= S183)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A15), Y10 (= Y16), S11 (= S17), C37 (≠ A42), G117 (= G123), F128 (= F134)
- binding arginine: Y88 (= Y93), T92 (= T97), D124 (= D130), R127 (= R133), S185 (= S192), E187 (= E194), E261 (= E268), Y273 (= Y280)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
40% identity, 96% coverage: 10:402/408 of query aligns to 2:392/397 of 4xfjB
- active site: D13 (= D21), R94 (= R101), D123 (= D130), S174 (= S183)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A15), Y8 (= Y16), S9 (= S17), T14 (= T22), I34 (≠ A42), G116 (= G123), C117 (≠ A124), F127 (= F134)
- binding arginine: Y86 (= Y93), S90 (≠ T97), R126 (= R133), A183 (≠ S192), E185 (= E194), E259 (= E268), E269 (≠ G278), Y271 (= Y280)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
27% identity, 85% coverage: 10:355/408 of query aligns to 15:371/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
27% identity, 85% coverage: 10:355/408 of query aligns to 11:367/438 of 6e5yA
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
25% identity, 95% coverage: 10:396/408 of query aligns to 12:410/447 of P0A6E4
- 17:25 (vs. 15:23, 89% identical) binding
- A43 (= A42) binding
- Y99 (= Y93) binding
- G129 (= G123) binding
- T131 (= T125) binding ; binding
- N135 (= N129) binding ; binding
- D136 (= D130) binding ; binding
- R139 (= R133) binding
- S192 (= S183) binding
- D194 (= D185) binding
- T201 (≠ S192) binding
- E203 (= E194) binding
- E280 (= E268) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
26% identity, 90% coverage: 10:378/408 of query aligns to 11:391/439 of 1kp3A
- active site: D22 (= D21), R106 (= R101), D135 (= D130), S191 (= S183)
- binding adenosine-5'-triphosphate: A16 (= A15), S18 (= S17), G20 (= G19), D22 (= D21), T23 (= T22), T41 (= T41), A42 (= A42), D127 (≠ H122), G128 (= G123), S129 (≠ A124), F139 (= F134), D193 (= D185)
- binding citrulline: Y98 (= Y93), T102 (= T97), P103 (≠ S98), T130 (= T125), G133 (= G128), N134 (= N129), D135 (= D130), R138 (= R133), D193 (= D185), T200 (≠ S192), E202 (= E194), E202 (= E194), E279 (= E268), S287 (= S276), Y291 (= Y280)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
26% identity, 85% coverage: 10:355/408 of query aligns to 11:367/432 of 1k97A
- active site: D22 (= D21), R106 (= R101), D135 (= D130), S191 (= S183)
- binding aspartic acid: S129 (≠ A124), T130 (= T125), G133 (= G128), N134 (= N129), D135 (= D130)
- binding citrulline: Y98 (= Y93), T102 (= T97), P103 (≠ S98), R138 (= R133), S191 (= S183), T192 (≠ M184), D193 (= D185), T200 (≠ S192), E202 (= E194), E279 (= E268), Y291 (= Y280), Y331 (= Y320)
Query Sequence
>GFF2423 FitnessBrowser__Marino:GFF2423
MWSKGMSDIKKVVLAYSGGLDTSVIVRWLQDTYNCEVVTFTADIGQGEEVEPARAKAEAL
GVKEIYIEDLREEFVRDYVFPMFRANTIYEGEYLLGTSIARPLIAKRLIDIANETGADAI
SHGATGKGNDQVRFELGAYALKPGVKVIAPWREWDLNSREKLLKYCEERNIPVEMKKGKS
PYSMDANLLHISYEGINLEDPWAEAEEDMWRWSVSPEAAPDEPTYVELTYKKGDIVAIDG
QDMKPHLVLETLNKLAGANGIGRLDIVENRYVGMKSRGCYETPGGTIMLRAHRAIESITL
DREVAHLKDSIMPRYAEVIYNGYWWSPEREALQALIDQTQNYVNGTVRLKLYKGNVDVVG
RKSEDSLFDEKIATFEEDQGAYDQKDAEGFIKLNALRLRIAAGKGRKL
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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