SitesBLAST
Comparing WP_083784660.1 NCBI__GCF_000019365.1:WP_083784660.1 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)
53% identity, 89% coverage: 51:493/499 of query aligns to 10:454/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 88% coverage: 51:488/499 of query aligns to 14:467/478 of 3h0mA
- active site: K72 (= K115), S147 (= S191), S148 (= S192), S166 (= S210), T168 (= T212), G169 (≠ N213), G170 (= G214), S171 (= S215), Q174 (≠ V218)
- binding glutamine: M122 (≠ Y166), G123 (≠ D167), D167 (= D211), T168 (= T212), G169 (≠ N213), G170 (= G214), S171 (= S215), F199 (= F243), Y302 (≠ A342), R351 (= R372), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 88% coverage: 51:488/499 of query aligns to 14:467/478 of 3h0lA
- active site: K72 (= K115), S147 (= S191), S148 (= S192), S166 (= S210), T168 (= T212), G169 (≠ N213), G170 (= G214), S171 (= S215), Q174 (≠ V218)
- binding asparagine: G123 (≠ D167), S147 (= S191), G169 (≠ N213), G170 (= G214), S171 (= S215), Y302 (≠ A342), R351 (= R372), D418 (vs. gap)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 88% coverage: 51:487/499 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K115), S154 (= S191), S155 (= S192), S173 (= S210), T175 (= T212), G176 (≠ N213), G177 (= G214), S178 (= S215), Q181 (≠ V218)
- binding glutamine: G130 (≠ D167), S154 (= S191), D174 (= D211), T175 (= T212), G176 (≠ N213), S178 (= S215), F206 (= F243), Y309 (≠ A342), Y310 (= Y343), R358 (= R372), D425 (≠ G439)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 88% coverage: 51:487/499 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K115), S154 (= S191), S155 (= S192), S173 (= S210), T175 (= T212), G176 (≠ N213), G177 (= G214), S178 (= S215), Q181 (≠ V218)
- binding asparagine: M129 (≠ Y166), G130 (≠ D167), T175 (= T212), G176 (≠ N213), S178 (= S215), Y309 (≠ A342), Y310 (= Y343), R358 (= R372), D425 (≠ G439)
3kfuE Crystal structure of the transamidosome (see paper)
39% identity, 92% coverage: 43:499/499 of query aligns to 1:466/468 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)
32% identity, 83% coverage: 84:495/499 of query aligns to 174:597/607 of Q7XJJ7
- K205 (= K115) mutation to A: Loss of activity.
- SS 281:282 (= SS 191:192) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TNGS 212:215) binding
- S305 (= S215) mutation to A: Loss of activity.
- R307 (= R217) mutation to A: Loss of activity.
- S360 (≠ P270) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
32% identity, 83% coverage: 84:495/499 of query aligns to 174:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A165), T258 (≠ F168), S281 (= S191), G302 (≠ T212), G303 (≠ N213), S305 (= S215), S472 (≠ R372), I532 (≠ M432), M539 (≠ G439)
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 90% coverage: 45:495/499 of query aligns to 9:484/487 of 1m21A
- active site: K81 (= K115), S160 (= S191), S161 (= S192), T179 (≠ S210), T181 (= T212), D182 (≠ N213), G183 (= G214), S184 (= S215), C187 (≠ V218)
- binding : A129 (= A165), N130 (≠ Y166), F131 (vs. gap), C158 (≠ G189), G159 (= G190), S160 (= S191), S184 (= S215), C187 (≠ V218), I212 (≠ F243), R318 (≠ A342), L321 (≠ I345), L365 (≠ V369), F426 (= F441)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 86% coverage: 44:470/499 of query aligns to 8:456/490 of 4yjiA
- active site: K79 (= K115), S158 (= S191), S159 (= S192), G179 (≠ T212), G180 (≠ N213), G181 (= G214), A182 (≠ S215)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L117), G132 (≠ A165), S158 (= S191), G179 (≠ T212), G180 (≠ N213), A182 (≠ S215)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 90% coverage: 48:495/499 of query aligns to 16:478/482 of 3a2qA
- active site: K69 (= K115), S147 (= S191), S148 (= S192), N166 (≠ S210), A168 (≠ T212), A169 (≠ N213), G170 (= G214), A171 (≠ S215), I174 (≠ V218)
- binding 6-aminohexanoic acid: G121 (≠ A165), G121 (≠ A165), N122 (≠ Y166), S147 (= S191), A168 (≠ T212), A168 (≠ T212), A169 (≠ N213), A171 (≠ S215), C313 (≠ A351)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 86% coverage: 61:488/499 of query aligns to 21:439/461 of 4gysB
- active site: K72 (= K115), S146 (= S191), S147 (= S192), T165 (≠ S210), T167 (= T212), A168 (≠ N213), G169 (= G214), S170 (= S215), V173 (= V218)
- binding malonate ion: A120 (= A165), G122 (≠ D167), S146 (= S191), T167 (= T212), A168 (≠ N213), S170 (= S215), S193 (≠ A238), G194 (= G239), V195 (≠ S240), R200 (≠ G245), Y297 (≠ S346), R305 (≠ H354)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 88% coverage: 51:487/499 of query aligns to 37:487/507 of Q84DC4
- K100 (= K115) mutation to A: Abolishes activity on mandelamide.
- S180 (= S191) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S192) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ N213) 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 (= S215) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V218) 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 (≠ V317) 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 (= Q388) 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 (≠ L434) 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.
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)
42% identity, 31% coverage: 107:260/499 of query aligns to 28:182/425 of Q9FR37
- K36 (= K115) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S191) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S192) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D211) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S215) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C223) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
34% identity, 47% coverage: 44:278/499 of query aligns to 7:245/457 of 5h6sC
- active site: K77 (= K115), S152 (= S191), S153 (= S192), L173 (≠ T212), G174 (≠ N213), G175 (= G214), S176 (= S215)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A165), R128 (≠ D167), W129 (≠ F168), S152 (= S191), L173 (≠ T212), G174 (≠ N213), S176 (= S215)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
32% identity, 82% coverage: 87:493/499 of query aligns to 64:467/605 of Q936X2
- K91 (= K115) mutation to A: Loss of activity.
- S165 (= S191) mutation to A: Loss of activity.
- S189 (= S215) mutation to A: Loss of activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
37% identity, 51% coverage: 105:356/499 of query aligns to 85:341/508 of 3a1iA
- active site: K95 (= K115), S170 (= S191), S171 (= S192), G189 (≠ S210), Q191 (≠ T212), G192 (≠ N213), G193 (= G214), A194 (≠ S215), I197 (≠ V218)
- binding benzamide: F145 (≠ Y166), S146 (≠ D167), G147 (≠ F168), Q191 (≠ T212), G192 (≠ N213), G193 (= G214), A194 (≠ S215), W327 (≠ A342)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 88% coverage: 50:489/499 of query aligns to 10:409/412 of 1ocmA
- active site: K62 (= K115), S131 (= S191), S132 (= S192), T152 (= T212), G153 (≠ N213), G154 (= G214), S155 (= S215)
- binding pyrophosphate 2-: R113 (vs. gap), S131 (= S191), Q151 (≠ D211), T152 (= T212), G153 (≠ N213), G154 (= G214), S155 (= S215), R158 (≠ V218), P359 (= P436)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 88% coverage: 50:489/499 of query aligns to 10:409/412 of 1o9oA
- active site: K62 (= K115), A131 (≠ S191), S132 (= S192), T150 (≠ S210), T152 (= T212), G153 (≠ N213), G154 (= G214), S155 (= S215), R158 (≠ V218)
- binding 3-amino-3-oxopropanoic acid: G130 (= G190), T152 (= T212), G153 (≠ N213), G154 (= G214), S155 (= S215), R158 (≠ V218), P359 (= P436)
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: 61:273/499 of query aligns to 24:242/564 of 6te4A
Sites not aligning to the query:
Query Sequence
>WP_083784660.1 NCBI__GCF_000019365.1:WP_083784660.1
MARGRPRPPRDAAGRRRASGGASPAGRARSRPGLRGRAVTPDFAAAIAGRVARRELGARA
VVAAALDRIAALDPRVGAFTDVTAARALAAAEALDARLDRGEAAGPLAGVPFAVKNLIDV
AGLPTRAGSRINRERVPAARDGALVRRLEAAGAILVGALNMGEYAYDFTGENVHDGPSRN
PHALAHMSGGSSGGSGAALAAGLVPLTLGSDTNGSIRVPSAFCGVFGLKPTYGRLTRAGS
FPFVGSLDHLGPMARSVADLALAYDAMQGPDPEDPVATRRPPEPVTPLLGRGAEGLRVAV
AGGYFARGGDPEAFEAVARVARALGADATVEIPEAARARAAAYLISAAEGAALHLDRLRA
RPGDFDPAVRDRLLAGAMIPAPHVERAQRFRRWYAGAVAEVFAGVDAILAPATPCRAPRG
GETVLVLDGVAMPLRPNLGVFTQPISFVGLPVAAVPVWLDDGLPLGVQVIAAPWREDVAL
RIAHALEQAGVARAPVAPL
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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