SitesBLAST
Comparing H281DRAFT_02970 FitnessBrowser__Burk376:H281DRAFT_02970 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)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
57% identity, 94% coverage: 10:455/473 of query aligns to 2:453/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
33% identity, 89% coverage: 20:439/473 of query aligns to 16:455/478 of 3h0mA
- active site: K72 (= K82), S147 (= S158), S148 (= S159), S166 (≠ T177), T168 (= T179), G169 (≠ N180), G170 (= G181), S171 (= S182), Q174 (≠ V185)
- binding glutamine: M122 (≠ Y133), G123 (= G134), D167 (= D178), T168 (= T179), G169 (≠ N180), G170 (= G181), S171 (= S182), F199 (= F210), Y302 (≠ A305), R351 (= R335), D418 (≠ G402)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
33% identity, 89% coverage: 20:439/473 of query aligns to 16:455/478 of 3h0lA
- active site: K72 (= K82), S147 (= S158), S148 (= S159), S166 (≠ T177), T168 (= T179), G169 (≠ N180), G170 (= G181), S171 (= S182), Q174 (≠ V185)
- binding asparagine: G123 (= G134), S147 (= S158), G169 (≠ N180), G170 (= G181), S171 (= S182), Y302 (≠ A305), R351 (= R335), D418 (≠ G402)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
33% identity, 88% coverage: 36:450/473 of query aligns to 33:473/485 of 2f2aA
- active site: K79 (= K82), S154 (= S158), S155 (= S159), S173 (≠ T177), T175 (= T179), G176 (≠ N180), G177 (= G181), S178 (= S182), Q181 (≠ V185)
- binding glutamine: G130 (= G134), S154 (= S158), D174 (= D178), T175 (= T179), G176 (≠ N180), S178 (= S182), F206 (= F210), Y309 (≠ A305), Y310 (≠ F306), R358 (= R335), D425 (≠ G402)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
33% identity, 88% coverage: 36:450/473 of query aligns to 33:473/485 of 2dqnA
- active site: K79 (= K82), S154 (= S158), S155 (= S159), S173 (≠ T177), T175 (= T179), G176 (≠ N180), G177 (= G181), S178 (= S182), Q181 (≠ V185)
- binding asparagine: M129 (≠ Y133), G130 (= G134), T175 (= T179), G176 (≠ N180), S178 (= S182), Y309 (≠ A305), Y310 (≠ F306), R358 (= R335), D425 (≠ G402)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 90% coverage: 19:446/473 of query aligns to 10:456/468 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)
30% identity, 88% coverage: 52:465/473 of query aligns to 175:603/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 158:159) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TNGS 179:182) binding
- S305 (= S182) mutation to A: Loss of activity.
- R307 (= R184) mutation to A: Loss of activity.
- S360 (≠ T237) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 88% coverage: 52:465/473 of query aligns to 175:603/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A132), T258 (≠ F135), S281 (= S158), G302 (≠ T179), G303 (≠ N180), S305 (= S182), S472 (≠ A338), I532 (≠ L395), M539 (≠ G402)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 94% coverage: 9:452/473 of query aligns to 5:470/482 of 3a2qA
- active site: K69 (= K82), S147 (= S158), S148 (= S159), N166 (≠ T177), A168 (≠ T179), A169 (≠ N180), G170 (= G181), A171 (≠ S182), I174 (≠ V185)
- binding 6-aminohexanoic acid: G121 (≠ A132), G121 (≠ A132), N122 (≠ Y133), S147 (= S158), A168 (≠ T179), A168 (≠ T179), A169 (≠ N180), A171 (≠ S182), C313 (vs. gap)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 93% coverage: 10:450/473 of query aligns to 6:444/457 of 5h6sC
- active site: K77 (= K82), S152 (= S158), S153 (= S159), L173 (≠ T179), G174 (≠ N180), G175 (= G181), S176 (= S182)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A132), R128 (≠ G134), W129 (≠ F135), S152 (= S158), L173 (≠ T179), G174 (≠ N180), S176 (= S182), W306 (≠ A305), F338 (≠ Y325)
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, 36% coverage: 74:242/473 of query aligns to 28:197/425 of Q9FR37
- K36 (= K82) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S158) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S159) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D178) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S182) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C190) 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)
33% identity, 91% coverage: 19:450/473 of query aligns to 13:442/461 of 4gysB
- active site: K72 (= K82), S146 (= S158), S147 (= S159), T165 (= T177), T167 (= T179), A168 (≠ N180), G169 (= G181), S170 (= S182), V173 (= V185)
- binding malonate ion: A120 (= A132), G122 (= G134), S146 (= S158), T167 (= T179), A168 (≠ N180), S170 (= S182), S193 (≠ H205), G194 (= G206), V195 (≠ T207), R200 (≠ A212), Y297 (≠ T309), R305 (≠ H317)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 91% coverage: 28:459/473 of query aligns to 32:506/508 of 3a1iA
- active site: K95 (= K82), S170 (= S158), S171 (= S159), G189 (≠ T177), Q191 (≠ T179), G192 (≠ N180), G193 (= G181), A194 (≠ S182), I197 (≠ V185)
- binding benzamide: F145 (≠ Y133), S146 (≠ G134), G147 (≠ F135), Q191 (≠ T179), G192 (≠ N180), G193 (= G181), A194 (≠ S182), W327 (≠ P296)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 91% coverage: 23:451/473 of query aligns to 42:488/507 of Q84DC4
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ N180) 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 (= S182) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V185) 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 (= S280) 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 (≠ A344) 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 (≠ V397) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 48% coverage: 21:245/473 of query aligns to 18:247/487 of 1m21A
- active site: K81 (= K82), S160 (= S158), S161 (= S159), T179 (= T177), T181 (= T179), D182 (≠ N180), G183 (= G181), S184 (= S182), C187 (≠ V185)
- binding : A129 (= A132), N130 (≠ Y133), F131 (vs. gap), C158 (≠ G156), G159 (= G157), S160 (= S158), S184 (= S182), C187 (≠ V185), I212 (≠ F210)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 86% coverage: 27:433/473 of query aligns to 37:444/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S158) mutation to A: Loss of activity.
- S189 (= S182) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
40% identity, 46% coverage: 17:234/473 of query aligns to 13:236/564 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)
29% identity, 90% coverage: 9:433/473 of query aligns to 6:456/490 of 4yjiA
- active site: K79 (= K82), S158 (= S158), S159 (= S159), G179 (≠ T179), G180 (≠ N180), G181 (= G181), A182 (≠ S182)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L84), G132 (≠ A132), S158 (= S158), G179 (≠ T179), G180 (≠ N180), A182 (≠ S182)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
43% identity, 33% coverage: 75:230/473 of query aligns to 62:218/593 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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
32% identity, 45% coverage: 29:243/473 of query aligns to 2:201/450 of 4n0iA
- active site: K38 (= K82), S116 (= S158), S117 (= S159), T135 (= T177), T137 (= T179), G138 (≠ N180), G139 (= G181), S140 (= S182), L143 (≠ V185)
- binding glutamine: G89 (= G134), T137 (= T179), G138 (≠ N180), S140 (= S182), Y168 (≠ F210)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_02970 FitnessBrowser__Burk376:H281DRAFT_02970
MTPSSSGAESALSIARAYAQGAFSARELIEATLARIDAYDTQVNAFTTVTRERALAEADA
LDARRASGHNLPPLAGVPFAAKNLFDISGVTTLAGSRVLADAPPAAADATLVERLCAQGA
ILIGALNMDEFAYGFTTENHHAGPCRNPHDLTRTAGGSSGGSAAAVAAGFVPLTLGTDTN
GSVRVPASLCGVFGVKPTYGRLSRHGTWPFVASLDHMGAFARTVDDLAAVYDALQGTEAL
DPACAQRGFESVDTRPGPLRVARLGGYFDTYANDDAREASHAAAHALSATHTVEYPDADA
ARGAAFLITAAEGGQLHMENLRTHYGAREPLSRDRLIAGALLPAAWVVQAQRVRAALRRR
VLELFERYDVLIAPATPVVAPRIGDEFMEVNGERLAVRPNLGMLTQPVSCLGLPVVAAPM
RTRGGLPVGVQLIAAPWREDLAFEAARRLEAAQLAVSPPPPFGDLAAHAGAQR
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