SitesBLAST
Comparing RR42_RS28435 FitnessBrowser__Cup4G11:RR42_RS28435 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)
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, 87% coverage: 21:460/508 of query aligns to 140:589/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 158:159) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 179:182) binding
- S305 (= S182) mutation to A: Loss of activity.
- R307 (= R184) mutation to A: Loss of activity.
- S360 (≠ V237) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 87% coverage: 21:460/508 of query aligns to 140:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G132), T258 (≠ A135), S281 (= S158), G302 (≠ T179), G303 (= G180), S305 (= S182), S472 (≠ N342), I532 (≠ G400), M539 (≠ Y407)
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)
31% identity, 89% coverage: 10:461/508 of query aligns to 6:475/490 of 4yjiA
- active site: K79 (= K83), S158 (= S158), S159 (= S159), G179 (≠ T179), G180 (= G180), G181 (= G181), A182 (≠ S182)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L85), G132 (= G132), S158 (= S158), G179 (≠ T179), G180 (= G180), A182 (≠ S182)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 90% coverage: 6:462/508 of query aligns to 2:476/485 of 2f2aA
- active site: K79 (= K83), S154 (= S158), S155 (= S159), S173 (= S177), T175 (= T179), G176 (= G180), G177 (= G181), S178 (= S182), Q181 (≠ I185)
- binding glutamine: G130 (= G134), S154 (= S158), D174 (= D178), T175 (= T179), G176 (= G180), S178 (= S182), F206 (≠ G210), Y309 (vs. gap), Y310 (≠ F303), R358 (≠ N342), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 90% coverage: 6:462/508 of query aligns to 2:476/485 of 2dqnA
- active site: K79 (= K83), S154 (= S158), S155 (= S159), S173 (= S177), T175 (= T179), G176 (= G180), G177 (= G181), S178 (= S182), Q181 (≠ I185)
- binding asparagine: M129 (≠ A133), G130 (= G134), T175 (= T179), G176 (= G180), S178 (= S182), Y309 (vs. gap), Y310 (≠ F303), R358 (≠ N342), D425 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 90% coverage: 15:472/508 of query aligns to 5:466/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 90% coverage: 7:462/508 of query aligns to 2:469/478 of 3h0mA
- active site: K72 (= K83), S147 (= S158), S148 (= S159), S166 (= S177), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), Q174 (≠ I185)
- binding glutamine: M122 (≠ A133), G123 (= G134), D167 (= D178), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), F199 (≠ G210), Y302 (vs. gap), R351 (≠ N342), D418 (≠ P412)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 90% coverage: 7:462/508 of query aligns to 2:469/478 of 3h0lA
- active site: K72 (= K83), S147 (= S158), S148 (= S159), S166 (= S177), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), Q174 (≠ I185)
- binding asparagine: G123 (= G134), S147 (= S158), G169 (= G180), G170 (= G181), S171 (= S182), Y302 (vs. gap), R351 (≠ N342), D418 (≠ P412)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 89% coverage: 11:460/508 of query aligns to 6:445/457 of 5h6sC
- active site: K77 (= K83), S152 (= S158), S153 (= S159), L173 (≠ T179), G174 (= G180), G175 (= G181), S176 (= S182)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G132), R128 (≠ G134), W129 (≠ A135), S152 (= S158), L173 (≠ T179), G174 (= G180), S176 (= S182), W306 (≠ L315), F338 (vs. gap)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 91% coverage: 8:471/508 of query aligns to 3:478/482 of 3a2qA
- active site: K69 (= K83), S147 (= S158), S148 (= S159), N166 (≠ S177), A168 (≠ T179), A169 (≠ G180), G170 (= G181), A171 (≠ S182), I174 (= I185)
- binding 6-aminohexanoic acid: G121 (= G132), G121 (= G132), N122 (≠ A133), S147 (= S158), A168 (≠ T179), A168 (≠ T179), A169 (≠ G180), A171 (≠ S182), C313 (≠ A322)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 83% coverage: 19:442/508 of query aligns to 10:431/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 76% coverage: 73:460/508 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K83), S170 (= S158), S171 (= S159), G189 (≠ S177), Q191 (≠ T179), G192 (= G180), G193 (= G181), A194 (≠ S182), I197 (= I185)
- binding benzamide: F145 (≠ A133), S146 (≠ G134), G147 (≠ A135), Q191 (≠ T179), G192 (= G180), G193 (= G181), A194 (≠ S182), W327 (≠ C298)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 85% coverage: 54:483/508 of query aligns to 42:453/461 of 4gysB
- active site: K72 (= K83), S146 (= S158), S147 (= S159), T165 (≠ S177), T167 (= T179), A168 (≠ G180), G169 (= G181), S170 (= S182), V173 (≠ I185)
- binding malonate ion: A120 (≠ G132), G122 (= G134), S146 (= S158), T167 (= T179), A168 (≠ G180), S170 (= S182), S193 (= S205), G194 (≠ R206), V195 (≠ K207), R200 (≠ T212), Y297 (≠ R316), R305 (≠ T324)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 87% coverage: 18:459/508 of query aligns to 36:487/507 of Q84DC4
- K100 (= K83) 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 (= G180) 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 (≠ I185) 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 (≠ C298) 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 (≠ S354) 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 (≠ L410) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 78% coverage: 75:471/508 of query aligns to 83:475/605 of Q936X2
- K91 (= K83) mutation to A: Loss of activity.
- S165 (= S158) mutation to A: Loss of activity.
- S189 (= S182) mutation to A: Loss of activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
40% identity, 44% coverage: 23:244/508 of query aligns to 19:246/487 of 1m21A
- active site: K81 (= K83), S160 (= S158), S161 (= S159), T179 (≠ S177), T181 (= T179), D182 (≠ G180), G183 (= G181), S184 (= S182), C187 (≠ I185)
- binding : A129 (= A135), N130 (= N136), F131 (≠ S137), C158 (≠ G156), G159 (= G157), S160 (= S158), S184 (= S182), C187 (≠ I185), I212 (= I214)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 88% coverage: 15:463/508 of query aligns to 7:411/412 of 1o9oA
- active site: K62 (= K83), A131 (≠ S158), S132 (= S159), T150 (≠ S177), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ I185)
- binding 3-amino-3-oxopropanoic acid: G130 (= G157), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ I185), P359 (≠ E404)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 88% coverage: 15:463/508 of query aligns to 7:411/412 of 1ocmA
- active site: K62 (= K83), S131 (= S158), S132 (= S159), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182)
- binding pyrophosphate 2-: R113 (= R138), S131 (= S158), Q151 (≠ D178), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ I185), P359 (≠ E404)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 46% coverage: 11:244/508 of query aligns to 6:243/564 of 6te4A
Sites not aligning to the query:
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
28% identity, 52% coverage: 4:269/508 of query aligns to 71:331/579 of Q9TUI8
- S217 (= S158) mutation to A: Loss of activity.
- S218 (= S159) mutation to A: Lowers activity by at least 98%.
- D237 (= D178) mutation D->E,N: Loss of activity.
- S241 (= S182) mutation to A: Loss of activity.
- C249 (= C190) mutation to A: Loss of activity.
Query Sequence
>RR42_RS28435 FitnessBrowser__Cup4G11:RR42_RS28435
MTQTDSLLAQSAVALRRLIGSKEISPVELLEACIARIEAVNPFINAITATCYERAREEAR
AAERAVLDGAPLGLLHGLPLGVKDLEATAGLLTTYGSPLYRDNVPSADNVLVARLRAAGA
IVTGKTNIPEMGAGANSRNAVWGATGNPFNPNLNAGGSSGGSAAALATDMLPVCTGSDTG
GSLRIPAAKCGVVGFRPSPGVVPSSRKLLGWTPISVVGPMGRTVADACLQLAASAGVSAS
DPLTYALDPMSFLLPANVDLGSLRVGWTEDFGVCAVDNQIRQVFRDKIAAMRHLFRSCDE
IQFDLGDAHRCFDVLRAESFVAGTREAYQRDPQSLGPNTRANYEMGAAMSLSDSAWAQAE
QTRILGRFQAAFEDYDVILSPTTPVSPFPWTNLYAETINGEKQENYYRWLAPTYVVTLTT
HPAISLPCGLDHAGMPFGLQVVGRFRADHHTLGVAHAMEQAFAGSAALRRPLPRLDQLRA
AQPGLKSIVTAPPVLDGSSGGAASVSAV
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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