SitesBLAST
Comparing CCNA_02558 FitnessBrowser__Caulo:CCNA_02558 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
52% identity, 90% coverage: 46:522/528 of query aligns to 15:487/487 of 1m21A
- active site: K81 (= K112), S160 (= S193), S161 (= S194), T179 (= T212), T181 (= T214), D182 (= D215), G183 (= G216), S184 (= S217), C187 (= C220)
- binding : A129 (= A162), N130 (= N163), F131 (≠ I164), C158 (= C191), G159 (= G192), S160 (= S193), S184 (= S217), C187 (= C220), I212 (= I245), R318 (≠ G350), L321 (= L353), L365 (≠ S399), F426 (≠ Y461)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 78% coverage: 104:516/528 of query aligns to 64:471/478 of 3h0mA
- active site: K72 (= K112), S147 (= S193), S148 (= S194), S166 (≠ T212), T168 (= T214), G169 (≠ D215), G170 (= G216), S171 (= S217), Q174 (≠ C220)
- binding glutamine: M122 (≠ N163), G123 (≠ I164), D167 (≠ E213), T168 (= T214), G169 (≠ D215), G170 (= G216), S171 (= S217), F199 (≠ I245), Y302 (≠ L353), R351 (= R402), D418 (≠ S464)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 78% coverage: 104:516/528 of query aligns to 64:471/478 of 3h0lA
- active site: K72 (= K112), S147 (= S193), S148 (= S194), S166 (≠ T212), T168 (= T214), G169 (≠ D215), G170 (= G216), S171 (= S217), Q174 (≠ C220)
- binding asparagine: G123 (≠ I164), S147 (= S193), G169 (≠ D215), G170 (= G216), S171 (= S217), Y302 (≠ L353), R351 (= R402), D418 (≠ S464)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 87% coverage: 58:516/528 of query aligns to 24:479/485 of 2f2aA
- active site: K79 (= K112), S154 (= S193), S155 (= S194), S173 (≠ T212), T175 (= T214), G176 (≠ D215), G177 (= G216), S178 (= S217), Q181 (≠ C220)
- binding glutamine: G130 (≠ I164), S154 (= S193), D174 (≠ E213), T175 (= T214), G176 (≠ D215), S178 (= S217), F206 (≠ I245), Y309 (≠ L353), Y310 (= Y354), R358 (= R402), D425 (≠ S464)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 87% coverage: 58:516/528 of query aligns to 24:479/485 of 2dqnA
- active site: K79 (= K112), S154 (= S193), S155 (= S194), S173 (≠ T212), T175 (= T214), G176 (≠ D215), G177 (= G216), S178 (= S217), Q181 (≠ C220)
- binding asparagine: M129 (≠ N163), G130 (≠ I164), T175 (= T214), G176 (≠ D215), S178 (= S217), Y309 (≠ L353), Y310 (= Y354), R358 (= R402), D425 (≠ S464)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 77% coverage: 104:512/528 of query aligns to 87:498/508 of 3a1iA
- active site: K95 (= K112), S170 (= S193), S171 (= S194), G189 (≠ T212), Q191 (≠ T214), G192 (≠ D215), G193 (= G216), A194 (≠ S217), I197 (≠ C220)
- binding benzamide: F145 (≠ H168), S146 (= S169), G147 (≠ I170), Q191 (≠ T214), G192 (≠ D215), G193 (= G216), A194 (≠ S217), W327 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 88% coverage: 58:520/528 of query aligns to 18:465/468 of 3kfuE
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 83% coverage: 92:528/528 of query aligns to 70:475/605 of Q936X2
- K91 (= K112) mutation to A: Loss of activity.
- S165 (≠ A200) mutation to A: Loss of activity.
- S189 (= S217) mutation to A: Loss of activity.
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, 83% coverage: 84:520/528 of query aligns to 177:597/607 of Q7XJJ7
- K205 (= K112) mutation to A: Loss of activity.
- SS 281:282 (= SS 193:194) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TDGS 214:217) binding
- S305 (= S217) mutation to A: Loss of activity.
- R307 (≠ T219) mutation to A: Loss of activity.
- S360 (= S272) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 83% coverage: 84:520/528 of query aligns to 177:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A162), T258 (≠ I170), S281 (= S193), G302 (≠ T214), G303 (≠ D215), S305 (= S217), S472 (= S399), I532 (≠ G462), M539 (vs. gap)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 89% coverage: 44:511/528 of query aligns to 4:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 88% coverage: 55:521/528 of query aligns to 43:497/507 of Q84DC4
- K100 (= K112) mutation to A: Abolishes activity on mandelamide.
- S180 (= S193) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S194) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ D215) 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 (= S217) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ C220) 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 (≠ G346) 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 (≠ D411) 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.
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.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
27% identity, 88% coverage: 55:520/528 of query aligns to 20:558/564 of 6te4A
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 80% coverage: 78:500/528 of query aligns to 39:427/461 of 4gysB
- active site: K72 (= K112), S146 (= S193), S147 (= S194), T165 (= T212), T167 (= T214), A168 (≠ D215), G169 (= G216), S170 (= S217), V173 (≠ C220)
- binding malonate ion: A120 (= A162), G122 (≠ S169), S146 (= S193), T167 (= T214), A168 (≠ D215), S170 (= S217), S193 (≠ T240), G194 (≠ H241), V195 (≠ I242), R200 (≠ H247), Y297 (= Y354), R305 (= R376)
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)
41% identity, 27% coverage: 139:278/528 of query aligns to 64:201/425 of Q9FR37
- S113 (= S193) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S194) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (≠ E213) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S217) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N225) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
- 214 S→T: Slightly reduces catalytic activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 35% coverage: 102:286/528 of query aligns to 28:209/450 of 4n0iA
- active site: K38 (= K112), S116 (= S193), S117 (= S194), T135 (= T212), T137 (= T214), G138 (≠ D215), G139 (= G216), S140 (= S217), L143 (≠ C220)
- binding glutamine: G89 (≠ S169), T137 (= T214), G138 (≠ D215), S140 (= S217), Y168 (≠ I245)
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)
27% identity, 87% coverage: 57:514/528 of query aligns to 23:476/490 of 4yjiA
- active site: K79 (= K112), S158 (= S193), S159 (= S194), G179 (≠ T214), G180 (≠ D215), G181 (= G216), A182 (≠ S217)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N114), G132 (≠ N163), S158 (= S193), G179 (≠ T214), G180 (≠ D215), A182 (≠ S217)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 89% coverage: 53:523/528 of query aligns to 18:451/457 of 5h6sC
- active site: K77 (= K112), S152 (= S193), S153 (= S194), L173 (≠ T214), G174 (≠ D215), G175 (= G216), S176 (= S217)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A162), R128 (= R165), W129 (≠ S166), S152 (= S193), L173 (≠ T214), G174 (≠ D215), S176 (= S217), W306 (≠ L365), F338 (= F395)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 45% coverage: 58:296/528 of query aligns to 23:251/482 of 3a2qA
- active site: K69 (= K112), S147 (= S193), S148 (= S194), N166 (≠ T212), A168 (≠ T214), A169 (≠ D215), G170 (= G216), A171 (≠ S217), I174 (≠ C220)
- binding 6-aminohexanoic acid: G121 (≠ A162), G121 (≠ A162), N122 (= N163), S147 (= S193), A168 (≠ T214), A168 (≠ T214), A169 (≠ D215), A171 (≠ S217)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 74% coverage: 104:494/528 of query aligns to 54:390/412 of 1o9oA
- active site: K62 (= K112), A131 (≠ S193), S132 (= S194), T150 (= T212), T152 (= T214), G153 (≠ D215), G154 (= G216), S155 (= S217), R158 (≠ C220)
- binding 3-amino-3-oxopropanoic acid: G130 (= G192), T152 (= T214), G153 (≠ D215), G154 (= G216), S155 (= S217), R158 (≠ C220), P359 (≠ D459)
Query Sequence
>CCNA_02558 FitnessBrowser__Caulo:CCNA_02558
MAVGAWRAEIFDPMLAAVRPPESRPRLGKRFMTKFAILAGAAAIALLAGNACAQTSEEAT
KAALATIQQRNPVLRAVIATNPNALTAAKALDAERKAGKVRSALHGVPILLKDNIESADP
LPTTAGSLALKDNITGRDAPVAKRLRDAGLVILGKANLSEWANIRSNHSISGWSAVGGTV
RNPYALDRSACGSSSGSGAAVAAGLAPLAIGTETDGSITCPAAINGLVGLKPTVGLVSRT
HIVPISHSQDTAGPMTLTVEDTAKVLTIIAGSDPTDPATKEADARKTDYAAGLSKTALKG
VTLAVARFYTGYSPKTDAVFERALKELEAQGATLVDVKAFDEGPIGRAEGVVLYTELKAD
LAAYLASTDPKKVPTRTLADVIAFNKATPKEFEWFGQESFERAEKTKGLDDPEYLKALAD
SKRLAGPEGIDKILKDTGAVAIIAPTTGPAWTIDPLNGDNYGGSSTTLPAVAGYPHLTVP
MGDVSGLPVGLSFIGPAWSEKLLLNLGYAYEQATKHRKAPTFKATIAP
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