SitesBLAST
Comparing CCNA_02519 FitnessBrowser__Caulo:CCNA_02519 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 92% coverage: 39:488/489 of query aligns to 40:485/485 of 2f2aA
- active site: K79 (= K77), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding glutamine: G130 (= G128), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (= F209), Y309 (= Y312), Y310 (= Y313), R358 (= R360), D425 (= D427)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 92% coverage: 39:488/489 of query aligns to 40:485/485 of 2dqnA
- active site: K79 (= K77), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding asparagine: M129 (= M127), G130 (= G128), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (= Y312), Y310 (= Y313), R358 (= R360), D425 (= D427)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 89% coverage: 39:472/489 of query aligns to 39:462/478 of 3h0mA
- active site: K72 (= K77), S147 (≠ L152), S148 (≠ T153), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding glutamine: M122 (= M127), G123 (= G128), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (= F209), Y302 (= Y312), R351 (= R360), D418 (= D427)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 89% coverage: 39:472/489 of query aligns to 39:462/478 of 3h0lA
- active site: K72 (= K77), S147 (≠ L152), S148 (≠ T153), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding asparagine: G123 (= G128), S147 (≠ L152), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (= Y312), R351 (= R360), D418 (= D427)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 96% coverage: 19:486/489 of query aligns to 13:461/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
38% identity, 83% coverage: 69:475/489 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K77), S116 (= S157), S117 (= S158), T135 (= T176), T137 (= T178), G138 (= G179), G139 (= G180), S140 (= S181), L143 (≠ Q184)
- binding glutamine: G89 (= G128), T137 (= T178), G138 (= G179), S140 (= S181), Y168 (≠ F209), Y271 (= Y312), Y272 (= Y313), R320 (= R360), D404 (= D427)
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, 79% coverage: 102:489/489 of query aligns to 231:601/607 of Q7XJJ7
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ H236) mutation to A: No effect.
Sites not aligning to the query:
- 205 K→A: Loss of activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
32% identity, 79% coverage: 102:489/489 of query aligns to 231:601/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A126), T258 (≠ S129), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (= S351), I532 (≠ N418), M539 (≠ L425)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 97% coverage: 12:486/489 of query aligns to 43:508/508 of 3a1iA
- active site: K95 (= K77), S170 (≠ P154), S171 (≠ G155), G189 (≠ A173), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ Q184)
- binding benzamide: F145 (≠ M127), S146 (≠ G128), G147 (≠ S129), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ Y312)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 95% coverage: 15:477/489 of query aligns to 15:477/487 of 1m21A
- active site: K81 (= K77), S160 (= S157), S161 (= S158), T179 (= T176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ Q184)
- binding : A129 (= A126), N130 (≠ M127), F131 (≠ G128), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ Q184), I212 (≠ F209), R318 (≠ Y313), L321 (≠ A316), L365 (= L362), F426 (≠ D419)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 3:480/489 of query aligns to 25:491/507 of Q84DC4
- T31 (≠ K9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K77) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q184) 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 (≠ L309) 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 (≠ D374) 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 (≠ T432) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 96% coverage: 12:481/489 of query aligns to 7:452/457 of 6c6gA
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 87% coverage: 48:474/489 of query aligns to 62:459/605 of Q936X2
- K91 (= K77) mutation to A: Loss of activity.
- S165 (≠ T149) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 96% coverage: 12:479/489 of query aligns to 12:476/490 of 4yjiA
- active site: K79 (= K77), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L79), G132 (≠ A126), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
25% identity, 98% coverage: 3:479/489 of query aligns to 5:447/457 of 5h6sC
- active site: K77 (= K77), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A126), R128 (≠ G128), W129 (≠ S129), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (≠ Y312), F338 (≠ I363)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 86% coverage: 58:477/489 of query aligns to 55:439/461 of 4gysB
- active site: K72 (= K77), S146 (≠ P154), S147 (≠ G155), T165 (= T176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ Q184)
- binding malonate ion: A120 (= A126), G122 (= G128), S146 (≠ P154), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ W204), G194 (= G205), V195 (= V206), R200 (≠ S211), Y297 (= Y327), R305 (= R335)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 89% coverage: 44:478/489 of query aligns to 29:409/412 of 1o9oA
- active site: K62 (= K77), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (= P420)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
26% identity, 62% coverage: 3:303/489 of query aligns to 2:341/564 of 6te4A
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 89% coverage: 44:478/489 of query aligns to 29:409/412 of 1ocmA
- active site: K62 (= K77), S131 (≠ P154), S132 (≠ G155), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ S130), S131 (≠ P154), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (= P420)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 50% coverage: 23:266/489 of query aligns to 25:259/482 of 3a2qA
- active site: K69 (= K77), S147 (≠ L152), S148 (≠ T153), N166 (≠ T176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ Q184)
- binding 6-aminohexanoic acid: G121 (≠ A126), G121 (≠ A126), N122 (≠ M127), S147 (≠ L152), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181)
Sites not aligning to the query:
Query Sequence
>CCNA_02519 FitnessBrowser__Caulo:CCNA_02519
MSLTNLTLKAAIDGLAAREFTSVELTRAHIEAIEAARGLNAYILETPDKAIDMAAKSDAR
RALGEAGPLEGAPLGVKDLFCTNGVRTTACSKILENFVPTYESTVTSQLWRDGAVMLGKL
NLDQFAMGSSNETSYFGPVTNPWRAQGSTKALTPGGSSGGSAAAVAADLCLGATATDTGG
SIRQPAAFTGTVGIKPTYGRCSRWGVVAFASSLDQAGPIAKTVEDAALLLTSMSGHDPKD
STSLDIPVPDFTQFVGKSVKGLKIGIPKEYRVDNMPAEIEKLWQDGIAWLKEAGCEIVDI
SLPHTKYALPAYYIVAPAEASSNLARYDGMRYGLREEGANLTEIYENTRASGFGDEVKRR
ILIGTYVLSAGYYDAYYLKALKVRRRIAEDFDNAWTQCDAILTPTAPSAAFGLGENSNDP
IAMYLNDVFTVTTNLAGLPGLSLPAGLDANGLPLGLQIIGKPLDEATVFSVAGAVEKAAG
FTAKAEKWW
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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