SitesBLAST
Comparing RR42_RS36060 FitnessBrowser__Cup4G11:RR42_RS36060 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)
34% identity, 98% coverage: 12:468/468 of query aligns to 1:466/468 of 3kfuE
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 97% coverage: 4:459/468 of query aligns to 3:476/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ M176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ S82), G132 (= G129), S158 (= S155), G179 (≠ M176), G180 (= G177), A182 (≠ S179)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 97% coverage: 4:456/468 of query aligns to 3:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (≠ M176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ N182)
- binding glutamine: G130 (= G131), S154 (= S155), D174 (= D175), T175 (≠ M176), G176 (= G177), S178 (= S179), F206 (≠ A207), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ T335), D425 (≠ W406)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 97% coverage: 4:456/468 of query aligns to 3:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (≠ M176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ N182)
- binding asparagine: M129 (≠ A130), G130 (= G131), T175 (≠ M176), G176 (= G177), S178 (= S179), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ T335), D425 (≠ W406)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:457/468 of query aligns to 9:467/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (≠ M176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ N182)
- binding glutamine: M122 (≠ A130), G123 (= G131), D167 (= D175), T168 (≠ M176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ A207), Y302 (≠ F309), R351 (vs. gap), D418 (≠ W406)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:457/468 of query aligns to 9:467/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (≠ M176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ N182)
- binding asparagine: G123 (= G131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (≠ F309), R351 (vs. gap), D418 (≠ W406)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 93% coverage: 25:457/468 of query aligns to 23:445/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ M176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ G131), W129 (≠ S132), S152 (= S155), L173 (≠ M176), G174 (= G177), S176 (= S179), W306 (≠ F309), F338 (≠ K333)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 97% coverage: 7:461/468 of query aligns to 1:453/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 84% coverage: 70:461/468 of query aligns to 85:502/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ S174), Q191 (≠ M176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ N182)
- binding benzamide: F145 (≠ A130), S146 (≠ G131), G147 (≠ S132), Q191 (≠ M176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ L312)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 95% coverage: 20:463/468 of query aligns to 19:483/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (≠ S174), T181 (≠ M176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ N182)
- binding : A129 (≠ G129), N130 (≠ A130), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ N182), I212 (≠ A204), R318 (≠ P300), L321 (vs. gap), L365 (= L342), F426 (≠ M400)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 87% coverage: 50:457/468 of query aligns to 175:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ S132), S281 (= S155), G302 (≠ M176), G303 (= G177), S305 (= S179), S472 (≠ N339), I532 (≠ M400), M539 (= M407)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 99% coverage: 6:468/468 of query aligns to 4:480/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ S174), A168 (≠ M176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ N182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (≠ A130), S147 (= S155), A168 (≠ M176), A168 (≠ M176), A169 (≠ G177), A171 (≠ S179), C313 (≠ A319)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 87% coverage: 50:457/468 of query aligns to 175:589/607 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 (≠ MGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ D234) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 97% coverage: 2:456/468 of query aligns to 23:487/507 of Q84DC4
- T31 (≠ V10) 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 (= G177) 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 (≠ N182) 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 (≠ L312) 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 (≠ A354) 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 (≠ M407) 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.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
35% identity, 50% coverage: 3:236/468 of query aligns to 1:241/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 89% coverage: 23:440/468 of query aligns to 18:422/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (≠ S174), T167 (≠ M176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ N182)
- binding malonate ion: A120 (≠ G129), G122 (= G131), S146 (= S155), T167 (≠ M176), A168 (≠ G177), S170 (= S179), S193 (vs. gap), G194 (vs. gap), V195 (≠ M201), R200 (≠ H206), Y297 (≠ R313), R305 (≠ Y321)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 84% coverage: 71:461/468 of query aligns to 82:466/605 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.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 85% coverage: 64:460/468 of query aligns to 46:411/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (≠ S174), T152 (≠ M176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ N182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (≠ M176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ N182), P359 (= P401)
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)
29% identity, 65% coverage: 11:312/468 of query aligns to 81:375/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (= C187) mutation to A: Loss of activity.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 96% coverage: 11:460/468 of query aligns to 6:411/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (≠ M176), G153 (= G177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ G131), S131 (= S155), Q151 (≠ D175), T152 (≠ M176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ N182), P359 (= P401)
Query Sequence
>RR42_RS36060 FitnessBrowser__Cup4G11:RR42_RS36060
MEDICYLGAVEMARAIRTRELGVREVVDAHIARILRINPAINAIVTTTFDEAQAAADAAD
TALARGAVPGPLFGLPVAHKDSFLSAGVRTTFGSAVYRDFVPAQDSAVVARQRAAGAIML
GKTNLPEFGAGSHTFNAVFGATRNPYRKDVSAGGSSGGSAAALAAGMVALADGSDMGGSL
RNPASFCNVVGLRASIGRVPMTPASHAFNTLTVGGPMGRSVADVALMFSVLAGDDPADPL
AIAADASDFATLPRIDGKGLRVAVSPTLGGLPFEPAVSRMLQEGIRQCQALGCTVDEAEP
DFSGADHAFEVLRALAFAANYGAARAKHGEQMKETVRWNIDLGLAQDGAAMAEAARAHSR
MFARMQALLTRYDFLIAPVSQVTPFAVETEYPQHIEGVPMPSYIGWMRSCYRITITGHPA
ISVPCGFTDDGLPVGLQIVGKYRGERALLAFAQMFEQANAAGRIRPAL
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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