SitesBLAST
Comparing Echvi_3131 FitnessBrowser__Cola:Echvi_3131 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)
Q57757 Agmatinase; EC 3.5.3.11 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
29% identity, 87% coverage: 31:338/356 of query aligns to 19:275/284 of Q57757
- C71 (≠ I105) mutation to S: 24% of wild-type activity in the presence of DTT.
- C136 (≠ A185) mutation to A: 89% of wild-type activity in the presence of DTT.
- C151 (≠ S200) mutation to S: 5% of wild-type activity in the presence of DTT.
- C229 (≠ G292) mutation to A: 96% of wild-type activity in the presence of DTT.
3lhlA Crystal structure of a putative agmatinase from clostridium difficile
28% identity, 58% coverage: 138:342/356 of query aligns to 74:267/276 of 3lhlA
- active site: H95 (= H159), D118 (= D182), H120 (= H184), D122 (= D186), H134 (= H198), D199 (= D274), D201 (= D276), E245 (= E320)
- binding manganese (ii) ion: H95 (= H159), D118 (= D182), D118 (= D182), H120 (= H184), D122 (= D186), D122 (= D186), H134 (= H198), D199 (= D274), D199 (= D274), D201 (= D276)
3pzlB The crystal structure of agmatine ureohydrolase of thermoplasma volcanium
25% identity, 87% coverage: 31:339/356 of query aligns to 21:278/293 of 3pzlB
- active site: H112 (= H159), D132 (= D182), H134 (= H184), D136 (= D186), H148 (= H198), D217 (= D274), D219 (= D276), E260 (= E320)
- binding manganese (ii) ion: H112 (= H159), D132 (= D182), D132 (= D182), H134 (= H184), D136 (= D186), D217 (= D274), D217 (= D274), D219 (= D276)
P0DJQ3 Proclavaminate amidinohydrolase; Proclavaminic acid amidino hydrolase; EC 3.5.3.22 from Streptomyces clavuligerus (see paper)
26% identity, 90% coverage: 26:344/356 of query aligns to 21:307/313 of P0DJQ3
- H121 (= H159) binding
- D144 (= D182) binding ; binding
- H146 (= H184) binding
- D148 (= D186) binding
- D235 (= D274) binding ; binding
- D237 (= D276) binding
1gq6B Proclavaminate amidino hydrolase from streptomyces clavuligerus (see paper)
26% identity, 90% coverage: 26:344/356 of query aligns to 13:299/301 of 1gq6B
- active site: H113 (= H159), D136 (= D182), H138 (= H184), D140 (= D186), H152 (= H198), D227 (= D274), D229 (= D276), E271 (= E320)
- binding manganese (ii) ion: H113 (= H159), D136 (= D182), D136 (= D182), H138 (= H184), D140 (= D186), D227 (= D274), D227 (= D274), D229 (= D276)
5hjaA Crystal structure of leishmania mexicana arginase in complex with inhibitor abhdp (see paper)
28% identity, 57% coverage: 138:339/356 of query aligns to 81:295/303 of 5hjaA
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
- binding (R)-2-amino-6-borono-2-(1-(3,4-dichlorobenzyl)piperidin-4-yl)hexanoic acid: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), S138 (vs. gap), H142 (≠ E192), G143 (= G193), A180 (≠ D221), V181 (≠ Y222), D182 (≠ E224), D231 (= D274), D233 (= D276)
Q9I3S3 Guanidinobutyrase; EC 3.5.3.7 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
29% identity, 55% coverage: 146:342/356 of query aligns to 116:309/319 of Q9I3S3
- H129 (= H159) binding
- D152 (= D182) binding ; binding
- H154 (= H184) binding
- D156 (= D186) binding
- M161 (≠ Y191) mutation to Y: Loss of activity.
- D243 (= D274) binding
- D245 (= D276) binding
3nioA Crystal structure of pseudomonas aeruginosa guanidinobutyrase (see paper)
29% identity, 55% coverage: 146:342/356 of query aligns to 113:306/316 of 3nioA
- active site: H126 (= H159), D149 (= D182), H151 (= H184), D153 (= D186), H165 (= H198), D240 (= D274), D242 (= D276), E284 (= E320)
- binding manganese (ii) ion: H126 (= H159), D149 (= D182), D149 (= D182), H151 (= H184), D153 (= D186), D240 (= D274), D240 (= D274), D242 (= D276)
5hj9A Crystal structure of leishmania mexicana arginase in complex with inhibitor abhpe (see paper)
28% identity, 52% coverage: 138:323/356 of query aligns to 81:279/311 of 5hj9A
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
- binding [(5R)-5-amino-5-carboxy-7-(piperidin-1-yl)heptyl](trihydroxy)borate(1-): H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), S138 (vs. gap), H142 (≠ E192), G143 (= G193), D182 (≠ E224), D231 (= D274), E276 (= E320)
4iu5A Crystal structure of leishmania mexicana arginase in complex with catalytic product l-ornithine (see paper)
28% identity, 52% coverage: 138:323/356 of query aligns to 81:279/310 of 4iu5A
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
- binding L-ornithine: H127 (= H184), D129 (= D186), S138 (vs. gap), H142 (≠ E192)
4iu4A Crystal structure of leishmania mexicana arginase in complex with inhibitor bec (see paper)
28% identity, 52% coverage: 138:323/356 of query aligns to 81:279/310 of 4iu4A
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
- binding s-2-(boronoethyl)-l-cysteine: D125 (= D182), H127 (= H184), D129 (= D186), S138 (vs. gap), H142 (≠ E192), D182 (≠ E224), D231 (= D274), D233 (= D276), E276 (= E320)
4iu1A Crystal structure of leishmania mexicana arginase in complex with inhibitor nor-noha (see paper)
28% identity, 52% coverage: 138:323/356 of query aligns to 81:279/310 of 4iu1A
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
- binding nor-n-omega-hydroxy-l-arginine: H127 (= H184), D129 (= D186), N131 (≠ R188), S138 (vs. gap), H142 (≠ E192), D182 (≠ E224), T245 (= T288)
4iu0A Crystal structure of leishmania mexicana arginase in complex with inhibitor abh (see paper)
28% identity, 52% coverage: 138:323/356 of query aligns to 81:279/310 of 4iu0A
- active site: H102 (= H159), D125 (= D182), H127 (= H184), D129 (= D186), H142 (≠ E192), D231 (= D274), D233 (= D276), E276 (= E320)
- binding 2(s)-amino-6-boronohexanoic acid: D125 (= D182), H127 (= H184), D129 (= D186), S138 (vs. gap), H142 (≠ E192), D231 (= D274), E276 (= E320)
- binding manganese (ii) ion: H102 (= H159), D125 (= D182), D125 (= D182), H127 (= H184), D129 (= D186), D231 (= D274), D231 (= D274), D233 (= D276)
P60651 Agmatinase; Agmatine ureohydrolase; AUH; EC 3.5.3.11 from Escherichia coli (strain K12) (see paper)
26% identity, 90% coverage: 11:329/356 of query aligns to 7:283/306 of P60651
- H163 (= H198) mutation to F: Loss of activity.
7lbaB E. Coli agmatinase (see paper)
26% identity, 90% coverage: 11:329/356 of query aligns to 14:290/310 of 7lbaB
7lolA The structure of agmatinase from e. Coli at 1.8 a displaying urea and agmatine (see paper)
26% identity, 85% coverage: 27:329/356 of query aligns to 18:273/294 of 7lolA
- binding agmatine: Y145 (≠ Q190), H153 (= H198)
- binding manganese (ii) ion: H116 (= H159), D139 (= D182), D139 (= D182), H141 (= H184), D143 (= D186), D220 (= D274), D220 (= D274), D222 (= D276)
- binding urea: D143 (= D186), H153 (= H198), D220 (= D274), E264 (= E320)
7loxA The structure of agmatinase from e. Coli at 3.2 a displaying guanidine in the active site (see paper)
29% identity, 56% coverage: 131:329/356 of query aligns to 78:263/284 of 7loxA
- binding guanidine: H106 (= H159), H131 (= H184), H131 (= H184), D133 (= D186), D133 (= D186), H143 (= H198), D210 (= D274)
- binding manganese (ii) ion: H106 (= H159), D129 (= D182), D129 (= D182), H131 (= H184), D133 (= D186), D210 (= D274), D210 (= D274), D212 (= D276)
6vstD Arginase from medicago truncatula in complex with ornithine (see paper)
29% identity, 60% coverage: 132:346/356 of query aligns to 111:318/320 of 6vstD
6vstA Arginase from medicago truncatula in complex with ornithine (see paper)
29% identity, 60% coverage: 132:346/356 of query aligns to 108:315/317 of 6vstA
- binding manganese (ii) ion: H136 (= H159), D160 (= D182), D160 (= D182), H162 (= H184), D164 (= D186), D245 (= D274), D245 (= D274), D247 (= D276)
- binding L-ornithine: H162 (= H184), Y166 (≠ R188), H176 (= H198), H259 (≠ T288)
G7JFU5 Arginase, mitochondrial; Agmatinase ARGAH; Arginine amidohydrolase; MtARGAH; EC 3.5.3.1; EC 3.5.3.11 from Medicago truncatula (Barrel medic) (Medicago tribuloides) (see paper)
29% identity, 60% coverage: 132:346/356 of query aligns to 129:336/338 of G7JFU5
- H157 (= H159) binding
- D181 (= D182) binding ; binding
- H183 (= H184) binding
- D185 (= D186) binding
- DLY 185:187 (≠ DLR 186:188) binding
- S220 (≠ D221) binding
- D266 (= D274) binding ; binding
- D268 (= D276) binding
Sites not aligning to the query:
Query Sequence
>Echvi_3131 FitnessBrowser__Cola:Echvi_3131
MTTKKQKAIDKFDPNGVSSEGSIFGLPFDEETASVVIVPVPWEVTVSYAPGTANGPQAIL
DASSQVDLFQDDITDAWTMGIHMLPIPENVYSNNTKYRILAGNYIDWLERGSPKEERERF
GAVPALIDKACQSMNDWVYETAKDQLNQGKLVALVGGDHSTPLGHIKALSERYSSFGILQ
IDAHADLRDQYEGFNYSHASISHNFLNIPQVEKLVQVGVRDYCEEESDRIDGDDRITTFF
DHHIKEQLYEGVTWRTICDQVIASLPREIYITIDIDGLDPKLCPHTGTPVPGGFDLNQLL
YLMKLIVKSGRKIIGFDLVEVAPGEDDSEWDGNVGARLLYRMSNLMGVSHGKLWWK
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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