SitesBLAST
Comparing GFF2509 FitnessBrowser__Phaeo:GFF2509 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
32% identity, 97% coverage: 6:457/468 of query aligns to 5:478/485 of 2f2aA
- active site: K79 (= K80), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ D184)
- binding glutamine: G130 (≠ H131), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (≠ Y210), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ K343), D425 (≠ E405)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
32% identity, 97% coverage: 6:457/468 of query aligns to 5:478/485 of 2dqnA
- active site: K79 (= K80), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ D184)
- binding asparagine: M129 (≠ A130), G130 (≠ H131), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ K343), D425 (≠ E405)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 98% coverage: 8:467/468 of query aligns to 6:454/457 of 5h6sC
- active site: K77 (= K80), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ T129), R128 (≠ H131), W129 (≠ R132), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (≠ L317), F338 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 94% coverage: 11:452/468 of query aligns to 4:454/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
39% identity, 51% coverage: 8:245/468 of query aligns to 6:230/478 of 3h0mA
- active site: K72 (= K80), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ D184)
- binding glutamine: M122 (≠ A130), G123 (≠ A133), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ Y210)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
39% identity, 51% coverage: 8:245/468 of query aligns to 6:230/478 of 3h0lA
- active site: K72 (= K80), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ D184)
- binding asparagine: G123 (≠ A133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 82% coverage: 70:452/468 of query aligns to 85:497/508 of 3a1iA
- active site: K95 (= K80), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ D184)
- binding benzamide: F145 (≠ A130), S146 (≠ H131), G147 (≠ R132), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ F314)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
39% identity, 52% coverage: 21:265/468 of query aligns to 20:267/487 of 1m21A
- active site: K81 (= K80), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ D184)
- binding : A129 (≠ T129), N130 (≠ A130), F131 (≠ H131), C158 (≠ S155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ D184), I212 (≠ V208)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
28% identity, 96% coverage: 10:457/468 of query aligns to 4:457/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 97% coverage: 3:455/468 of query aligns to 23:490/507 of Q84DC4
- T31 (≠ Q11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ D184) 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 (≠ A295) 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 (= Q347) 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 (vs. gap) 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.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 84% coverage: 64:455/468 of query aligns to 46:410/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S157), S132 (= S158), T150 (≠ S176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ D184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ D184), P359 (≠ S401)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 52% coverage: 1:245/468 of query aligns to 131:364/616 of 6diiH
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)
31% identity, 52% coverage: 1:245/468 of query aligns to 131:364/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ P241) mutation to A: No effect.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
36% identity, 50% coverage: 5:240/468 of query aligns to 3:228/482 of 3a2qA
- active site: K69 (= K80), S147 (= S157), S148 (= S158), N166 (≠ S176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ D184)
- binding 6-aminohexanoic acid: G121 (≠ T129), G121 (≠ T129), N122 (≠ A130), S147 (= S157), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181)
Sites not aligning to the query:
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)
32% identity, 63% coverage: 11:305/468 of query aligns to 81:366/579 of Q9TUI8
- S217 (= S157) mutation to A: Loss of activity.
- S218 (= S158) mutation to A: Lowers activity by at least 98%.
- D237 (= D177) mutation D->E,N: Loss of activity.
- S241 (= S181) mutation to A: Loss of activity.
- C249 (= C189) mutation to A: Loss of activity.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 84% coverage: 64:455/468 of query aligns to 46:410/412 of 1ocmA
- active site: K62 (= K80), S131 (= S157), S132 (= S158), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ H131), S131 (= S157), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ D184), P359 (≠ S401)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 87% coverage: 50:456/468 of query aligns to 45:442/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (≠ G156), T165 (≠ S176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ D184)
- binding malonate ion: A120 (≠ T129), G122 (≠ H131), S146 (= S155), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ T204), G194 (= G205), V195 (= V208), R200 (≠ G213), Y297 (≠ E315), R305 (= R332)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
34% identity, 50% coverage: 8:242/468 of query aligns to 6:240/564 of 6te4A
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 58% coverage: 6:275/468 of query aligns to 5:298/490 of 4yjiA
- active site: K79 (= K80), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ S82), G132 (≠ A130), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
3pr0A Crystal structure of a covalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
31% identity, 60% coverage: 16:295/468 of query aligns to 54:324/545 of 3pr0A
- active site: K110 (= K80), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (≠ T178), G207 (= G179), G208 (= G180), S209 (= S181), F212 (≠ D184)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptane-1,1-diol: M159 (≠ A130), F160 (≠ H131), S161 (≠ R132), S185 (= S157), D205 (= D177), I206 (≠ T178), G207 (= G179), S209 (= S181)
Sites not aligning to the query:
Query Sequence
>GFF2509 FitnessBrowser__Phaeo:GFF2509
MQEWLFASAVQMAAALQRKTISSRELVTLHLEHISVVNPAINAIVTLAAERALEEAQVTD
AQIAQGRFSGPLMGVPVTIKDSFDTEGIVSTYGMAARAGFVPNRDATVVARLRKAGAIVL
GKTNTSELTAHRAEHTNPPLHGRTNNPHDFARSPSGSSGGAAAAVAAGCAALDIGSDTGG
SIRDPAHVCGVVGIKPSAGLVPRTGHCVSYGLGTLDLLTQVGPMARYVEDVSLALSVISG
PDGNDLDANSVYSCNIEDVDLAGLRVAYYTDSGAHQVSDDATKAVISAAAALQDAKAVLR
QDFPACLFDASKLFEALVSVDGGLWKHELAKRAIRGGTAGSRKLMPQLSALAPDSTVTAF
GKRIGPFKAGLADYMEKYDALLGPVSPQAARLHADTPQGYSFWNELSAHNLSGFPAVTVP
AARTSNGLPVGVQIVSTAGRDHVALAVAKAIQTRLNCTFKPQIRTATG
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