SitesBLAST
Comparing N515DRAFT_4323 FitnessBrowser__Dyella79:N515DRAFT_4323 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 93% coverage: 12:448/469 of query aligns to 2:462/478 of 3h0mA
- active site: K72 (= K87), S147 (= S161), S148 (= S162), S166 (= S180), T168 (≠ S182), G169 (≠ L183), G170 (= G184), S171 (= S185), Q174 (≠ I188)
- binding glutamine: M122 (≠ L136), G123 (= G137), D167 (= D181), T168 (≠ S182), G169 (≠ L183), G170 (= G184), S171 (= S185), F199 (≠ A213), Y302 (vs. gap), R351 (≠ F343), D418 (≠ A403)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 93% coverage: 12:448/469 of query aligns to 2:462/478 of 3h0lA
- active site: K72 (= K87), S147 (= S161), S148 (= S162), S166 (= S180), T168 (≠ S182), G169 (≠ L183), G170 (= G184), S171 (= S185), Q174 (≠ I188)
- binding asparagine: G123 (= G137), S147 (= S161), G169 (≠ L183), G170 (= G184), S171 (= S185), Y302 (vs. gap), R351 (≠ F343), D418 (≠ A403)
3kfuE Crystal structure of the transamidosome (see paper)
37% identity, 91% coverage: 24:448/469 of query aligns to 9:450/468 of 3kfuE
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 93% coverage: 19:454/469 of query aligns to 5:450/457 of 6c6gA
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 93% coverage: 31:467/469 of query aligns to 145:597/607 of Q7XJJ7
- K205 (= K87) mutation to A: Loss of activity.
- SS 281:282 (= SS 161:162) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ SLGS 182:185) binding
- S305 (= S185) mutation to A: Loss of activity.
- R307 (= R187) mutation to A: Loss of activity.
- S360 (≠ Y240) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 93% coverage: 31:467/469 of query aligns to 145:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A135), T258 (≠ A138), S281 (= S161), G302 (≠ S182), G303 (≠ L183), S305 (= S185), S472 (≠ M346), I532 (≠ P399), M539 (≠ T406)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 96% coverage: 12:461/469 of query aligns to 3:482/485 of 2f2aA
- active site: K79 (= K87), S154 (= S161), S155 (= S162), S173 (= S180), T175 (≠ S182), G176 (≠ L183), G177 (= G184), S178 (= S185), Q181 (≠ I188)
- binding glutamine: G130 (= G137), S154 (= S161), D174 (= D181), T175 (≠ S182), G176 (≠ L183), S178 (= S185), F206 (≠ A213), Y309 (vs. gap), Y310 (vs. gap), R358 (= R345), D425 (≠ A403)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 96% coverage: 12:461/469 of query aligns to 3:482/485 of 2dqnA
- active site: K79 (= K87), S154 (= S161), S155 (= S162), S173 (= S180), T175 (≠ S182), G176 (≠ L183), G177 (= G184), S178 (= S185), Q181 (≠ I188)
- binding asparagine: M129 (≠ L136), G130 (= G137), T175 (≠ S182), G176 (≠ L183), S178 (= S185), Y309 (vs. gap), Y310 (vs. gap), R358 (= R345), D425 (≠ A403)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 87% coverage: 34:441/469 of query aligns to 18:427/461 of 4gysB
- active site: K72 (= K87), S146 (= S161), S147 (= S162), T165 (≠ S180), T167 (≠ S182), A168 (≠ L183), G169 (= G184), S170 (= S185), V173 (≠ I188)
- binding malonate ion: A120 (= A135), G122 (= G137), S146 (= S161), T167 (≠ S182), A168 (≠ L183), S170 (= S185), S193 (≠ R208), G194 (= G209), V195 (≠ L210), R200 (= R215), Y297 (≠ R314), R305 (≠ M324)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
34% identity, 79% coverage: 67:436/469 of query aligns to 71:445/605 of Q936X2
- K91 (= K87) mutation to A: Loss of activity.
- S165 (= S161) mutation to A: Loss of activity.
- S189 (= S185) mutation to A: Loss of activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 91% coverage: 24:448/469 of query aligns to 15:472/487 of 1m21A
- active site: K81 (= K87), S160 (= S161), S161 (= S162), T179 (≠ S180), T181 (≠ S182), D182 (≠ L183), G183 (= G184), S184 (= S185), C187 (≠ I188)
- binding : A129 (= A135), N130 (≠ L136), F131 (≠ G137), C158 (≠ G159), G159 (= G160), S160 (= S161), S184 (= S185), C187 (≠ I188), I212 (≠ A213), R318 (vs. gap), L321 (vs. gap), L365 (≠ A322), F426 (≠ S401)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
36% identity, 50% coverage: 14:247/469 of query aligns to 4:244/457 of 5h6sC
- active site: K77 (= K87), S152 (= S161), S153 (= S162), L173 (≠ S182), G174 (≠ L183), G175 (= G184), S176 (= S185)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A135), R128 (≠ G137), W129 (≠ A138), S152 (= S161), L173 (≠ S182), G174 (≠ L183), S176 (= S185)
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)
44% identity, 33% coverage: 79:235/469 of query aligns to 28:191/425 of Q9FR37
- K36 (= K87) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S161) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S162) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D181) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S185) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C193) 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, 79% coverage: 77:447/469 of query aligns to 85:492/508 of 3a1iA
- active site: K95 (= K87), S170 (= S161), S171 (= S162), G189 (≠ S180), Q191 (≠ S182), G192 (≠ L183), G193 (= G184), A194 (≠ S185), I197 (= I188)
- binding benzamide: F145 (≠ L136), S146 (≠ G137), G147 (≠ A138), Q191 (≠ S182), G192 (≠ L183), G193 (= G184), A194 (≠ S185), W327 (= W307)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 91% coverage: 28:455/469 of query aligns to 41:490/507 of Q84DC4
- K100 (= K87) mutation to A: Abolishes activity on mandelamide.
- S180 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ L183) 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 (= S185) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I188) 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 (≠ T312) 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 (≠ R374) 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 (≠ F408) 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.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 90% coverage: 26:448/469 of query aligns to 16:464/482 of 3a2qA
- active site: K69 (= K87), S147 (= S161), S148 (= S162), N166 (≠ S180), A168 (≠ S182), A169 (≠ L183), G170 (= G184), A171 (≠ S185), I174 (= I188)
- binding 6-aminohexanoic acid: G121 (≠ A135), G121 (≠ A135), N122 (≠ L136), S147 (= S161), A168 (≠ S182), A168 (≠ S182), A169 (≠ L183), A171 (≠ S185), C313 (≠ W307)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 91% coverage: 21:445/469 of query aligns to 3:466/490 of 4yjiA
- active site: K79 (= K87), S158 (= S161), S159 (= S162), G179 (≠ S182), G180 (≠ L183), G181 (= G184), A182 (≠ S185)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N89), G132 (≠ A135), S158 (= S161), G179 (≠ S182), G180 (≠ L183), A182 (≠ S185)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
35% identity, 50% coverage: 11:243/469 of query aligns to 1:242/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 36% coverage: 79:247/469 of query aligns to 30:202/450 of 4n0iA
- active site: K38 (= K87), S116 (= S161), S117 (= S162), T135 (≠ S180), T137 (≠ S182), G138 (≠ L183), G139 (= G184), S140 (= S185), L143 (≠ I188)
- binding glutamine: G89 (= G137), T137 (≠ S182), G138 (≠ L183), S140 (= S185), Y168 (≠ A213)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
41% identity, 31% coverage: 82:225/469 of query aligns to 64:210/593 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.
Query Sequence
>N515DRAFT_4323 FitnessBrowser__Dyella79:N515DRAFT_4323
MNQLPPISDRDLRRATLCQLLHWLAAGRVHPEGLAEVYLEAIERLNPQLNAYVGLSAGLL
REQARAAQHRRRDGVLGRLDGLPVAIKDNFDVAGWPTRAGLPGRAQPAQGDAHAVARLRA
SGAVLLGKTNMDEGALGASTDNPHTGPTHNPHRHGYTAGGSSGGAAAAVAAGMAVAAIGS
DSLGSIRIPASYCGVYALKPTHGEISARGLVPAARRLDAVGLLARSANDLTVLLQVLAGY
DADDARSRRRRVAFAPPDWEPGNLRCGLLPDLAAVGVEAAVIDVFEDALSRLPRELGERR
QVDFSDWDFARTRRAGLFLMEAEMLSTFAADLDDAEHPASERFRRMLSYAATKSAADYAV
ADRVLDAATLKMRRLFAQIDVLVLPTTPQGAFPLGGAVPDSQADLTSFASLAGCPAVSIP
MGTLPDGMPVGMQLVGARGSDLRLLELAEVCAATLDAEPVYPVEPRPLA
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