SitesBLAST
Comparing PfGW456L13_3755 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3755 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)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 95% coverage: 13:368/374 of query aligns to 198:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A70), T258 (≠ V73), S281 (= S96), G302 (≠ T117), G303 (= G118), S305 (= S120), S472 (≠ R257), I532 (≠ S312), M539 (≠ T319)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 95% coverage: 13:368/374 of query aligns to 198:588/607 of Q7XJJ7
- K205 (= K20) mutation to A: Loss of activity.
- SS 281:282 (= SS 96:97) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 117:120) binding
- S305 (= S120) mutation to A: Loss of activity.
- R307 (= R122) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
52% identity, 40% coverage: 13:160/374 of query aligns to 29:177/425 of Q9FR37
- K36 (= K20) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S96) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S97) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D116) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S120) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C128) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 95% coverage: 13:368/374 of query aligns to 88:497/508 of 3a1iA
- active site: K95 (= K20), S170 (= S96), S171 (= S97), G189 (≠ T115), Q191 (≠ T117), G192 (= G118), G193 (= G119), A194 (≠ S120), I197 (≠ V123)
- binding benzamide: F145 (= F71), S146 (≠ G72), G147 (≠ V73), Q191 (≠ T117), G192 (= G118), G193 (= G119), A194 (≠ S120), W327 (= W238)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 90% coverage: 17:353/374 of query aligns to 69:451/478 of 3h0mA
- active site: K72 (= K20), S147 (= S96), S148 (= S97), S166 (≠ T115), T168 (= T117), G169 (= G118), G170 (= G119), S171 (= S120), Q174 (≠ V123)
- binding glutamine: M122 (≠ F71), G123 (= G72), D167 (= D116), T168 (= T117), G169 (= G118), G170 (= G119), S171 (= S120), F199 (≠ L148), Y302 (≠ G229), R351 (= R257), D418 (≠ T319)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 90% coverage: 17:353/374 of query aligns to 69:451/478 of 3h0lA
- active site: K72 (= K20), S147 (= S96), S148 (= S97), S166 (≠ T115), T168 (= T117), G169 (= G118), G170 (= G119), S171 (= S120), Q174 (≠ V123)
- binding asparagine: G123 (= G72), S147 (= S96), G169 (= G118), G170 (= G119), S171 (= S120), Y302 (≠ G229), R351 (= R257), D418 (≠ T319)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
32% identity, 77% coverage: 18:305/374 of query aligns to 67:388/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 96% coverage: 17:374/374 of query aligns to 62:460/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 91% coverage: 13:352/374 of query aligns to 74:460/487 of 1m21A
- active site: K81 (= K20), S160 (= S96), S161 (= S97), T179 (= T115), T181 (= T117), D182 (≠ G118), G183 (= G119), S184 (= S120), C187 (≠ V123)
- binding : A129 (= A70), N130 (vs. gap), F131 (vs. gap), C158 (≠ G94), G159 (= G95), S160 (= S96), S184 (= S120), C187 (≠ V123), I212 (≠ L148), R318 (≠ L217), L321 (≠ S220), L365 (≠ R257), F426 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 92% coverage: 14:357/374 of query aligns to 94:476/507 of Q84DC4
- K100 (= K20) mutation to A: Abolishes activity on mandelamide.
- S180 (= S96) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S97) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G118) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S120) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V123) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A225) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ L269) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ T319) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 95% coverage: 14:368/374 of query aligns to 68:448/457 of 6c6gA
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 93% coverage: 19:364/374 of query aligns to 90:457/605 of Q936X2
- K91 (= K20) mutation to A: Loss of activity.
- S165 (= S96) mutation to A: Loss of activity.
- S189 (= S120) mutation to A: Loss of activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
43% identity, 40% coverage: 18:165/374 of query aligns to 36:185/450 of 4n0iA
- active site: K38 (= K20), S116 (= S96), S117 (= S97), T135 (= T115), T137 (= T117), G138 (= G118), G139 (= G119), S140 (= S120), L143 (≠ V123)
- binding glutamine: G89 (= G72), T137 (= T117), G138 (= G118), S140 (= S120), Y168 (≠ L148)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
32% identity, 92% coverage: 13:357/374 of query aligns to 55:396/412 of 1o9oA
- active site: K62 (= K20), A131 (≠ S96), S132 (= S97), T150 (= T115), T152 (= T117), G153 (= G118), G154 (= G119), S155 (= S120), R158 (≠ V123)
- binding 3-amino-3-oxopropanoic acid: G130 (= G95), T152 (= T117), G153 (= G118), G154 (= G119), S155 (= S120), R158 (≠ V123), P359 (≠ K313)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
39% identity, 42% coverage: 17:173/374 of query aligns to 76:231/485 of 2f2aA
- active site: K79 (= K20), S154 (= S96), S155 (= S97), S173 (≠ T115), T175 (= T117), G176 (= G118), G177 (= G119), S178 (= S120), Q181 (≠ V123)
- binding glutamine: G130 (= G72), S154 (= S96), D174 (= D116), T175 (= T117), G176 (= G118), S178 (= S120), F206 (≠ L148)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
39% identity, 42% coverage: 17:173/374 of query aligns to 76:231/485 of 2dqnA
- active site: K79 (= K20), S154 (= S96), S155 (= S97), S173 (≠ T115), T175 (= T117), G176 (= G118), G177 (= G119), S178 (= S120), Q181 (≠ V123)
- binding asparagine: M129 (≠ F71), G130 (= G72), T175 (= T117), G176 (= G118), S178 (= S120)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
33% identity, 92% coverage: 13:357/374 of query aligns to 55:396/412 of 1ocmA
- active site: K62 (= K20), S131 (= S96), S132 (= S97), T152 (= T117), G153 (= G118), G154 (= G119), S155 (= S120)
- binding pyrophosphate 2-: R113 (≠ N77), S131 (= S96), Q151 (≠ D116), T152 (= T117), G153 (= G118), G154 (= G119), S155 (= S120), R158 (≠ V123), P359 (≠ T319)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 87% coverage: 43:368/374 of query aligns to 94:468/482 of 3a2qA
- active site: S147 (= S96), S148 (= S97), N166 (≠ T115), A168 (≠ T117), A169 (≠ G118), G170 (= G119), A171 (≠ S120), I174 (≠ V123)
- binding 6-aminohexanoic acid: G121 (≠ A70), G121 (≠ A70), N122 (≠ F71), S147 (= S96), A168 (≠ T117), A168 (≠ T117), A169 (≠ G118), A171 (≠ S120), C313 (vs. gap)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 95% coverage: 14:368/374 of query aligns to 66:438/461 of 4gysB
- active site: K72 (= K20), S146 (= S96), S147 (= S97), T165 (= T115), T167 (= T117), A168 (≠ G118), G169 (= G119), S170 (= S120), V173 (= V123)
- binding malonate ion: A120 (= A70), G122 (= G72), S146 (= S96), T167 (= T117), A168 (≠ G118), S170 (= S120), S193 (≠ V143), G194 (= G144), V195 (≠ A145), R200 (≠ S150), Y297 (vs. gap), R305 (≠ N237)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 94% coverage: 10:359/374 of query aligns to 65:434/457 of 5h6sC
- active site: K77 (= K20), S152 (= S96), S153 (= S97), L173 (≠ T117), G174 (= G118), G175 (= G119), S176 (= S120)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A70), R128 (≠ G72), W129 (≠ V73), S152 (= S96), L173 (≠ T117), G174 (= G118), S176 (= S120), W306 (= W238), F338 (vs. gap)
Query Sequence
>PfGW456L13_3755 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3755
MSTFISEFLLGGNGKRVAIKDSIDIAGHPTRSGSRAFADAPAATQNAEVVDAILDAGWQI
VGKTNLHELAFGVTGINDWTGTPINPQAPDRVPGGSSSGSASAVAAGLADIAIGTDTGGS
VRVPAACCGIAGLKPTYGRVSRVGAHPLESSLDCVGPFAKSMDDLIAAMQVICPGFTAQG
LPGDGARVGFLEVACDSHLQASLGAAADRAGWRRSNLHLSEFEAAFAAGLTVINFENWAA
FGHLTGKGLIGADVETRLLAASRTTREELADACAVRTRFTQQVDAALEDFAVLLLPTLPT
LPPTLSEARAGSKAVAGMTPLVRPFNLSGHPALTVPVELDCGGLKVGLQIVGRKGQDELV
CAFGAQLQASTTQS
Or try a new SitesBLAST search
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