SitesBLAST
Comparing PfGW456L13_3117 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3117 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)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 92% coverage: 8:417/446 of query aligns to 135:564/607 of Q7XJJ7
- K205 (= K72) mutation to A: Loss of activity.
- SS 281:282 (= SS 150:151) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 171:174) binding
- S305 (= S174) mutation to A: Loss of activity.
- R307 (= R176) mutation to A: Loss of activity.
- S360 (≠ N231) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 92% coverage: 8:417/446 of query aligns to 135:564/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A122), T258 (≠ G125), S281 (= S150), G302 (≠ T171), G303 (≠ A172), S305 (= S174), S472 (≠ R327), I532 (≠ A385), M539 (≠ L392)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 99% coverage: 2:444/446 of query aligns to 28:490/507 of Q84DC4
- T31 (≠ M5) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K72) mutation to A: Abolishes activity on mandelamide.
- S180 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A172) 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 (= S174) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I177) 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 (vs. gap) 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 (≠ P336) 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 (≠ N388) 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.
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)
28% identity, 83% coverage: 66:435/446 of query aligns to 30:416/425 of Q9FR37
- K36 (= K72) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S150) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S151) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D170) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S174) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N182) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (vs. gap) mutation to T: Slightly reduces catalytic activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
47% identity, 37% coverage: 63:229/446 of query aligns to 82:244/605 of Q936X2
- K91 (= K72) mutation to A: Loss of activity.
- S165 (= S150) mutation to A: Loss of activity.
- S189 (= S174) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 51% coverage: 2:228/446 of query aligns to 1:228/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
39% identity, 37% coverage: 63:228/446 of query aligns to 72:238/487 of 1m21A
- active site: K81 (= K72), S160 (= S150), S161 (= S151), T179 (= T169), T181 (= T171), D182 (≠ A172), G183 (= G173), S184 (= S174), C187 (≠ I177)
- binding : A129 (= A122), N130 (≠ Y123), F131 (vs. gap), C158 (≠ G148), G159 (= G149), S160 (= S150), S184 (= S174), C187 (≠ I177), I212 (≠ L202)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
45% identity, 35% coverage: 62:218/446 of query aligns to 62:214/461 of 4gysB
- active site: K72 (= K72), S146 (= S150), S147 (= S151), T165 (= T169), T167 (= T171), A168 (= A172), G169 (= G173), S170 (= S174), V173 (≠ I177)
- binding malonate ion: A120 (= A122), G122 (≠ S124), S146 (= S150), T167 (= T171), A168 (= A172), S170 (= S174), S193 (≠ K197), G194 (= G198), V195 (≠ L199), R200 (≠ I204)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 50% coverage: 2:222/446 of query aligns to 5:232/564 of 6te4A
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 90% coverage: 40:441/446 of query aligns to 40:454/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
34% identity, 51% coverage: 3:229/446 of query aligns to 6:226/478 of 3h0mA
- active site: K72 (= K72), S147 (= S150), S148 (= S151), S166 (≠ T169), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), Q174 (≠ I177)
- binding glutamine: M122 (≠ L126), G123 (= G127), D167 (= D170), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), F199 (≠ L202)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
34% identity, 51% coverage: 3:229/446 of query aligns to 6:226/478 of 3h0lA
- active site: K72 (= K72), S147 (= S150), S148 (= S151), S166 (≠ T169), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), Q174 (≠ I177)
- binding asparagine: G123 (= G127), S147 (= S150), G169 (≠ A172), G170 (= G173), S171 (= S174)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
27% identity, 77% coverage: 69:411/446 of query aligns to 66:422/593 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.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 56% coverage: 66:313/446 of query aligns to 73:295/485 of 2f2aA
- active site: K79 (= K72), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (≠ A172), G177 (= G173), S178 (= S174), Q181 (≠ I177)
- binding glutamine: G130 (≠ S124), S154 (= S150), D174 (= D170), T175 (= T171), G176 (≠ A172), S178 (= S174), F206 (≠ L202)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 56% coverage: 66:313/446 of query aligns to 73:295/485 of 2dqnA
- active site: K79 (= K72), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (≠ A172), G177 (= G173), S178 (= S174), Q181 (≠ I177)
- binding asparagine: M129 (≠ Y123), G130 (≠ S124), T175 (= T171), G176 (≠ A172), S178 (= S174)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
24% identity, 96% coverage: 2:429/446 of query aligns to 5:441/457 of 5h6sC
- active site: K77 (= K72), S152 (= S150), S153 (= S151), L173 (≠ T171), G174 (≠ A172), G175 (= G173), S176 (= S174)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A122), R128 (≠ S124), W129 (≠ G125), S152 (= S150), L173 (≠ T171), G174 (≠ A172), S176 (= S174), W306 (= W298), F338 (≠ R323)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 77% coverage: 70:411/446 of query aligns to 93:468/508 of 3a1iA
- active site: K95 (= K72), S170 (= S150), S171 (= S151), G189 (≠ T169), Q191 (≠ T171), G192 (≠ A172), G193 (= G173), A194 (≠ S174), I197 (= I177)
- binding benzamide: F145 (≠ Y123), S146 (= S124), G147 (= G125), Q191 (≠ T171), G192 (≠ A172), G193 (= G173), A194 (≠ S174), W327 (≠ R290)
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
33% identity, 34% coverage: 66:216/446 of query aligns to 136:287/579 of Q9TUI8
- S217 (≠ G148) mutation to A: Loss of activity.
- S218 (≠ G149) mutation to A: Lowers activity by at least 98%.
- D237 (= D170) mutation D->E,N: Loss of activity.
- S241 (= S174) mutation to A: Loss of activity.
- C249 (≠ N182) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 50% coverage: 6:229/446 of query aligns to 10:239/490 of 4yjiA
- active site: K79 (= K72), S158 (≠ G149), S159 (= S150), G179 (≠ T171), G180 (≠ A172), G181 (= G173), A182 (≠ S174)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L74), G132 (≠ A122), S158 (≠ G149), G179 (≠ T171), G180 (≠ A172), A182 (≠ S174)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 34% coverage: 59:210/446 of query aligns to 25:176/450 of 4n0iA
- active site: K38 (= K72), S116 (= S150), S117 (= S151), T135 (= T169), T137 (= T171), G138 (≠ A172), G139 (= G173), S140 (= S174), L143 (≠ I177)
- binding glutamine: G89 (≠ S124), T137 (= T171), G138 (≠ A172), S140 (= S174), Y168 (≠ L202)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_3117 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3117
MITMMQTAERLRQGLTTPDKLIESALAAIKNSAYVFIDVLEQRAFNDAEASTRRWRQGAP
LSPFDGIPYAVKDLLDVVGSRTTAGSITRIDAPMAVEDAEVIAALAALGMIPLGKTNLTE
FAYSGLGLNPHFGTPTCDVAVSESRVPGGSSSGSAIAVQRGIVTCAIGTDTAGSIRIPAA
FNGLVGYKASTSRYSMKGLHPLAITLDSLGPFAHTVADCVALDAAMRGFKNVAIEAVNLS
SLRFVVDDGVMSDPALQPVVQHNLVSMMERLRAAGAQVERRPVLAVARTRELIVREGWLG
AIEAWRLLGAIVEGPQGHQMDRRVRHRLRAAKEVDPASEARIRHLRTELMAAMERELDGA
ILVMPTVKHVAPPMAPLSNDDELFASVNLETLSLTMIGSLLDMPGVAIPSGKDSIGLATS
TLFSTTQGRDDQLLSACLAIETRLCD
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