SitesBLAST
Comparing N515DRAFT_0701 FitnessBrowser__Dyella79:N515DRAFT_0701 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)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
55% identity, 90% coverage: 34:520/541 of query aligns to 8:487/487 of 1m21A
- active site: K81 (= K103), S160 (= S185), S161 (= S186), T179 (≠ S204), T181 (= T206), D182 (= D207), G183 (= G208), S184 (= S209), C187 (= C212)
- binding : A129 (= A154), N130 (= N155), F131 (≠ M156), C158 (= C183), G159 (= G184), S160 (= S185), S184 (= S209), C187 (= C212), I212 (= I237), R318 (≠ L343), L321 (= L346), L365 (= L391), F426 (≠ T459)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 89% coverage: 33:515/541 of query aligns to 6:472/478 of 3h0mA
- active site: K72 (= K103), S147 (= S185), S148 (= S186), S166 (= S204), T168 (= T206), G169 (≠ D207), G170 (= G208), S171 (= S209), Q174 (≠ C212)
- binding glutamine: M122 (≠ N155), G123 (≠ M156), D167 (≠ E205), T168 (= T206), G169 (≠ D207), G170 (= G208), S171 (= S209), F199 (≠ I237), Y302 (≠ E342), R351 (≠ Q394), D418 (≠ G456)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 89% coverage: 33:515/541 of query aligns to 6:472/478 of 3h0lA
- active site: K72 (= K103), S147 (= S185), S148 (= S186), S166 (= S204), T168 (= T206), G169 (≠ D207), G170 (= G208), S171 (= S209), Q174 (≠ C212)
- binding asparagine: G123 (≠ M156), S147 (= S185), G169 (≠ D207), G170 (= G208), S171 (= S209), Y302 (≠ E342), R351 (≠ Q394), D418 (≠ G456)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 89% coverage: 28:511/541 of query aligns to 2:475/485 of 2f2aA
- active site: K79 (= K103), S154 (= S185), S155 (= S186), S173 (= S204), T175 (= T206), G176 (≠ D207), G177 (= G208), S178 (= S209), Q181 (≠ C212)
- binding glutamine: G130 (≠ A161), S154 (= S185), D174 (≠ E205), T175 (= T206), G176 (≠ D207), S178 (= S209), F206 (≠ I237), Y309 (≠ L343), Y310 (≠ T344), R358 (≠ Q394), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 89% coverage: 28:511/541 of query aligns to 2:475/485 of 2dqnA
- active site: K79 (= K103), S154 (= S185), S155 (= S186), S173 (= S204), T175 (= T206), G176 (≠ D207), G177 (= G208), S178 (= S209), Q181 (≠ C212)
- binding asparagine: M129 (≠ H160), G130 (≠ A161), T175 (= T206), G176 (≠ D207), S178 (= S209), Y309 (≠ L343), Y310 (≠ T344), R358 (≠ Q394), D425 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 88% coverage: 36:510/541 of query aligns to 4:455/468 of 3kfuE
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, 80% coverage: 85:518/541 of query aligns to 187:597/607 of Q7XJJ7
- K205 (= K103) mutation to A: Loss of activity.
- SS 281:282 (= SS 185:186) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TDGS 206:209) binding
- S305 (= S209) mutation to A: Loss of activity.
- R307 (≠ I211) mutation to A: Loss of activity.
- S360 (= S264) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 80% coverage: 85:518/541 of query aligns to 187:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A154), T258 (≠ S162), S281 (= S185), G302 (≠ T206), G303 (≠ D207), S305 (= S209), S472 (≠ L391), I532 (≠ V460), M539 (vs. gap)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 79% coverage: 93:518/541 of query aligns to 85:506/508 of 3a1iA
- active site: K95 (= K103), S170 (= S185), S171 (= S186), G189 (≠ S204), Q191 (≠ T206), G192 (≠ D207), G193 (= G208), A194 (≠ S209), I197 (≠ C212)
- binding benzamide: F145 (≠ H160), S146 (≠ A161), G147 (≠ S162), Q191 (≠ T206), G192 (≠ D207), G193 (= G208), A194 (≠ S209), W327 (≠ P341)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 90% coverage: 25:509/541 of query aligns to 20:487/507 of Q84DC4
- T31 (≠ K35) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K103) mutation to A: Abolishes activity on mandelamide.
- S180 (= S185) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S186) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ D207) 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 (= S209) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ C212) 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 (≠ G339) 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 (≠ E408) 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.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 92% coverage: 31:529/541 of query aligns to 5:490/490 of 4yjiA
- active site: K79 (= K103), S158 (= S185), S159 (= S186), G179 (≠ T206), G180 (≠ D207), G181 (= G208), A182 (≠ S209)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N105), G132 (≠ N155), S158 (= S185), G179 (≠ T206), G180 (≠ D207), A182 (≠ S209)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
38% identity, 40% coverage: 86:300/541 of query aligns to 53:262/457 of 6c6gA
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 43% coverage: 33:266/541 of query aligns to 6:241/564 of 6te4A
Sites not aligning to the query:
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)
38% identity, 29% coverage: 95:252/541 of query aligns to 28:180/425 of Q9FR37
- K36 (= K103) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S185) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S186) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (≠ E205) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S209) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N217) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
36% identity, 46% coverage: 51:299/541 of query aligns to 18:251/461 of 4gysB
- active site: K72 (= K103), S146 (= S185), S147 (= S186), T165 (≠ S204), T167 (= T206), A168 (≠ D207), G169 (= G208), S170 (= S209), V173 (≠ C212)
- binding malonate ion: A120 (= A154), G122 (≠ A161), S146 (= S185), T167 (= T206), A168 (≠ D207), S170 (= S209), S193 (= S232), G194 (= G233), V195 (≠ I234), R200 (≠ H239)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
35% identity, 36% coverage: 79:274/541 of query aligns to 64:254/605 of Q936X2
- K91 (= K103) mutation to A: Loss of activity.
- S165 (≠ A192) mutation to A: Loss of activity.
- S189 (= S209) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 56% coverage: 36:336/541 of query aligns to 9:300/457 of 5h6sC
- active site: K77 (= K103), S152 (= S185), S153 (= S186), L173 (≠ T206), G174 (≠ D207), G175 (= G208), S176 (= S209)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A154), R128 (= R157), W129 (≠ S158), S152 (= S185), L173 (≠ T206), G174 (≠ D207), S176 (= S209)
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, 40% coverage: 34:251/541 of query aligns to 79:287/579 of Q9TUI8
- S217 (= S185) mutation to A: Loss of activity.
- S218 (= S186) mutation to A: Lowers activity by at least 98%.
- D237 (≠ E205) mutation D->E,N: Loss of activity.
- S241 (= S209) mutation to A: Loss of activity.
- C249 (≠ N217) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 56% coverage: 33:333/541 of query aligns to 3:263/412 of 1o9oA
- active site: K62 (= K103), A131 (≠ S185), S132 (= S186), T150 (≠ S204), T152 (= T206), G153 (≠ D207), G154 (= G208), S155 (= S209), R158 (≠ C212)
- binding 3-amino-3-oxopropanoic acid: G130 (= G184), T152 (= T206), G153 (≠ D207), G154 (= G208), S155 (= S209), R158 (≠ C212)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 45% coverage: 31:272/541 of query aligns to 4:237/482 of 3a2qA
- active site: K69 (= K103), S147 (= S185), S148 (= S186), N166 (≠ S204), A168 (≠ T206), A169 (≠ D207), G170 (= G208), A171 (≠ S209), I174 (≠ C212)
- binding 6-aminohexanoic acid: G121 (≠ A154), G121 (≠ A154), N122 (= N155), S147 (= S185), A168 (≠ T206), A168 (≠ T206), A169 (≠ D207), A171 (≠ S209)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_0701 FitnessBrowser__Dyella79:N515DRAFT_0701
MTRLPLSLSLAALLLASTALPAQSADPALAWASIKELQQRMDAGQLRSEALARLFLERIQ
RIDRDGPALRAVLETNPDALKLAAQIDRQKPKGALRGIPVLLKDNIDTGDRMLTTAGSLA
LADAPPAPRDAGLVARLRKNGALILGKTNLSEWANMRSNHASSGWSARGGQTRNPYALDR
NPCGSSAGSGAAVAAGLATVAIGSETDGSIICPAAANGIVGIKPTVGLVSRSGIVPISHN
QDTAGPMARTVADAAAVLGAIAGSDPRDPATAEADKHATDYTRFLDPNGLKGKRIGVVRG
LAGAEPNADRILEQSIALMKAQGAVIVDPVELPHLKELGDPELTVLLYDLKQDMQAYLAT
RTGTSMKTLADLIAFNKREAEREMPWFGQELFEQAQAKGPLTDKDYVEAQAKAKRFAGPE
GIDVALAKDHLDALLAPSWGPTFVTDPVLGDHVVSGDPTVGGASQPAAVAGYPSITVPAG
FAHDLPVGIVFFGAKWSEPTLITIAYGYEQHAQAWRAPRFLDTVGGKPVMADADHVLEMT
R
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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