SitesBLAST
Comparing SMa1377 FitnessBrowser__Smeli:SMa1377 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)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 91% coverage: 12:440/471 of query aligns to 1:456/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 93% coverage: 4:439/471 of query aligns to 2:467/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding glutamine: M122 (≠ F130), G123 (= G131), D167 (= D175), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), F199 (≠ L207), Y302 (≠ M304), R351 (≠ G335), D418 (≠ P389)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 93% coverage: 4:439/471 of query aligns to 2:467/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding asparagine: G123 (= G131), S147 (= S155), G169 (≠ A177), G170 (= G178), S171 (= S179), Y302 (≠ M304), R351 (≠ G335), D418 (≠ P389)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 81% coverage: 63:442/471 of query aligns to 188:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S155), G302 (≠ T176), G303 (≠ A177), S305 (= S179), S472 (≠ A318), I532 (≠ Y384), M539 (≠ P391)
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)
28% identity, 81% coverage: 63:442/471 of query aligns to 188:592/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ R234) mutation to A: No effect.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 92% coverage: 8:438/471 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (= T176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding glutamine: G130 (= G131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (≠ A177), S178 (= S179), F206 (≠ L207), Y309 (≠ T300), Y310 (≠ V301), R358 (= R329), D425 (≠ P389)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 92% coverage: 8:438/471 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (= T176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding asparagine: M129 (≠ F130), G130 (= G131), T175 (= T176), G176 (≠ A177), S178 (= S179), Y309 (≠ T300), Y310 (≠ V301), R358 (= R329), D425 (≠ P389)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 92% coverage: 4:438/471 of query aligns to 25:487/507 of Q84DC4
- T31 (≠ R10) 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 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L182) 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 (≠ F295) 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 (vs. gap) 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.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 79% coverage: 70:439/471 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ T176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), I197 (≠ L182)
- binding benzamide: F145 (= F130), S146 (≠ G131), G147 (= G132), Q191 (≠ T176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), W327 (≠ P298)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 94% coverage: 8:450/471 of query aligns to 2:455/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ T176), G174 (≠ A177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ G131), W129 (≠ G132), S152 (= S155), L173 (≠ T176), G174 (≠ A177), S176 (= S179), W306 (vs. gap), F338 (= F322)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 90% coverage: 22:445/471 of query aligns to 16:455/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 94% coverage: 9:451/471 of query aligns to 8:485/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (= T176), D182 (≠ A177), G183 (= G178), S184 (= S179), C187 (≠ L182)
- binding : A129 (= A129), N130 (vs. gap), F131 (= F130), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ L182), I212 (≠ L207), R318 (≠ T300), L321 (≠ M303), L365 (≠ I336), F426 (vs. gap)
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)
26% identity, 78% coverage: 72:437/471 of query aligns to 28:421/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ R260) mutation to T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 88% coverage: 25:439/471 of query aligns to 20:439/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (= T176), A168 (= A177), G169 (= G178), S170 (= S179), V173 (≠ L182)
- binding malonate ion: A120 (= A129), G122 (= G131), S146 (= S155), T167 (= T176), A168 (= A177), S170 (= S179), S193 (≠ D202), G194 (= G203), V195 (≠ I204), R200 (≠ A209), Y297 (≠ F295), R305 (≠ M304)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 75% coverage: 69:421/471 of query aligns to 51:390/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (= T174), T152 (= T176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ L182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (= T176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ L182), P359 (= P382)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
31% identity, 75% coverage: 69:421/471 of query aligns to 51:390/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (= T176), G153 (≠ A177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ G131), S131 (= S155), Q151 (≠ D175), T152 (= T176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ L182), P359 (= P389)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 94% coverage: 8:452/471 of query aligns to 7:487/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ T176), G180 (≠ A177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ T82), G132 (≠ A129), S158 (= S155), G179 (≠ T176), G180 (≠ A177), A182 (≠ S179)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 81% coverage: 67:449/471 of query aligns to 78:472/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) 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)
33% identity, 53% coverage: 4:252/471 of query aligns to 2:255/564 of 6te4A
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 48% coverage: 13:240/471 of query aligns to 11:235/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ T176), A169 (= A177), G170 (= G178), A171 (≠ S179), I174 (≠ L182)
- binding 6-aminohexanoic acid: G121 (≠ A129), G121 (≠ A129), N122 (≠ F130), S147 (= S155), A168 (≠ T176), A168 (≠ T176), A169 (= A177), A171 (≠ S179)
Sites not aligning to the query:
Query Sequence
>SMa1377 FitnessBrowser__Smeli:SMa1377
MTALENLSIRKLAAMVRAREISAVDVTTHFLGRIVAYDDALCGFNVPAPEAALDAAHDLD
TYLNAGGEAGALAGIPLSIKDTADVAGLPSAGASASRSGRTATADATVVARMKAAGGIVL
GKANCHELAFGGPSFDLPFPPARNPWNLDRFPGGSSSGSGVTVAAGLCLGSLATDTAGSI
RLPATMCGVFGLKPGHDTLPLDGIAVLAATMDHVGPVARTADDTRILFDVMAGRSPGSPF
VGSLKGLRIGVPENEWDVGRLIHPDVRAAIDGAIEVARSEGADIVPLRLPSLEDFHAPGT
VLMMCEVAAEHAASVRAAWDKFGAIFRARALVGEGIAVHDFRLAERLRPVLRKRLLDAMS
NVDCLLVPGALAPPGPLASVDPFYFMKDPIPNIVANYTGFPALAFPAGFGGDGMPVGVQI
MGVPRSEHRLLDIAESFERADPSRFAARTPPGLEGRPEPCLFKLELPARAM
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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