SitesBLAST
Comparing RR42_RS09095 FitnessBrowser__Cup4G11:RR42_RS09095 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)
28% identity, 98% coverage: 5:441/447 of query aligns to 8:474/485 of 2f2aA
- active site: K79 (= K75), S154 (= S153), S155 (= S154), S173 (= S172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding glutamine: G130 (≠ S127), S154 (= S153), D174 (= D173), T175 (= T174), G176 (= G175), S178 (= S177), F206 (≠ L205), Y309 (≠ L287), Y310 (≠ A288), R358 (= R326), D425 (≠ A389)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 98% coverage: 5:441/447 of query aligns to 8:474/485 of 2dqnA
- active site: K79 (= K75), S154 (= S153), S155 (= S154), S173 (= S172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding asparagine: M129 (≠ F126), G130 (≠ S127), T175 (= T174), G176 (= G175), S178 (= S177), Y309 (≠ L287), Y310 (≠ A288), R358 (= R326), D425 (≠ A389)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 89% coverage: 44:442/447 of query aligns to 172:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ G128), S281 (= S153), G302 (≠ T174), G303 (= G175), S305 (= S177), S472 (≠ A324), I532 (≠ F385), M539 (≠ L392)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 89% coverage: 44:442/447 of query aligns to 172:590/607 of Q7XJJ7
- K205 (= K75) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 174:177) binding
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 98% coverage: 5:444/447 of query aligns to 7:470/478 of 3h0mA
- active site: K72 (= K75), S147 (= S153), S148 (= S154), S166 (= S172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding glutamine: M122 (≠ F126), G123 (≠ S127), D167 (= D173), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), F199 (≠ L205), Y302 (vs. gap), R351 (= R326), D418 (≠ N388)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 98% coverage: 5:444/447 of query aligns to 7:470/478 of 3h0lA
- active site: K72 (= K75), S147 (= S153), S148 (= S154), S166 (= S172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding asparagine: G123 (≠ S127), S147 (= S153), G169 (= G175), G170 (= G176), S171 (= S177), Y302 (vs. gap), R351 (= R326), D418 (≠ N388)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 91% coverage: 39:443/447 of query aligns to 64:490/507 of Q84DC4
- K100 (= K75) mutation to A: Abolishes activity on mandelamide.
- S180 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G175) 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 (= S177) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I180) 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 (≠ A291) 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 (≠ A331) 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 (≠ L392) 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)
29% identity, 90% coverage: 42:443/447 of query aligns to 3:425/425 of Q9FR37
- K36 (= K75) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S153) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S154) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D173) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S177) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C185) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A247) mutation to T: Slightly reduces catalytic activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 75% coverage: 39:375/447 of query aligns to 38:380/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 88% coverage: 51:445/447 of query aligns to 51:443/461 of 4gysB
- active site: K72 (= K75), S146 (= S153), S147 (= S154), T165 (≠ S172), T167 (= T174), A168 (≠ G175), G169 (= G176), S170 (= S177), V173 (≠ I180)
- binding malonate ion: A120 (= A125), G122 (≠ S127), S146 (= S153), T167 (= T174), A168 (≠ G175), S170 (= S177), S193 (≠ D200), G194 (= G201), V195 (≠ A202), R200 (≠ Y207), Y297 (≠ A295), R305 (≠ E303)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 96% coverage: 12:442/447 of query aligns to 32:499/508 of 3a1iA
- active site: K95 (= K75), S170 (= S153), S171 (= S154), G189 (≠ S172), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), I197 (= I180)
- binding benzamide: F145 (= F126), S146 (= S127), G147 (= G128), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), W327 (≠ I293)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 90% coverage: 8:409/447 of query aligns to 10:421/457 of 5h6sC
- active site: K77 (= K75), S152 (= S153), S153 (= S154), L173 (≠ T174), G174 (= G175), G175 (= G176), S176 (= S177)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ S127), W129 (≠ G128), S152 (= S153), L173 (≠ T174), G174 (= G175), S176 (= S177), W306 (≠ N294), F338 (≠ V323)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
43% identity, 37% coverage: 66:230/447 of query aligns to 72:237/487 of 1m21A
- active site: K81 (= K75), S160 (= S153), S161 (= S154), T179 (≠ S172), T181 (= T174), D182 (≠ G175), G183 (= G176), S184 (= S177), C187 (≠ I180)
- binding : A129 (= A125), N130 (vs. gap), F131 (= F126), C158 (≠ G151), G159 (= G152), S160 (= S153), S184 (= S177), C187 (≠ I180), I212 (≠ L205)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
29% identity, 98% coverage: 6:441/447 of query aligns to 3:455/468 of 3kfuE
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 97% coverage: 8:440/447 of query aligns to 7:407/412 of 1o9oA
- active site: K62 (= K75), A131 (≠ S153), S132 (= S154), T150 (≠ S172), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ I180)
- binding 3-amino-3-oxopropanoic acid: G130 (= G152), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ I180), P359 (≠ A382)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
25% identity, 97% coverage: 8:440/447 of query aligns to 7:407/412 of 1ocmA
- active site: K62 (= K75), S131 (≠ R148), S132 (≠ I149), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177)
- binding pyrophosphate 2-: R113 (≠ S127), S131 (≠ R148), Q151 (≠ D173), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ I180), P359 (≠ A382)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
35% identity, 43% coverage: 51:241/447 of query aligns to 58:260/564 of 6te4A
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 99% coverage: 3:444/447 of query aligns to 20:467/605 of Q936X2
- K91 (= K75) mutation to A: Loss of activity.
- S165 (= S153) mutation to A: Loss of activity.
- S189 (= S177) mutation to A: Loss of activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
27% identity, 85% coverage: 68:447/447 of query aligns to 62:458/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
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)
33% identity, 43% coverage: 8:201/447 of query aligns to 82:265/579 of Q9TUI8
- S217 (≠ G151) mutation to A: Loss of activity.
- S218 (≠ G152) mutation to A: Lowers activity by at least 98%.
- D237 (= D173) mutation D->E,N: Loss of activity.
- S241 (= S177) mutation to A: Loss of activity.
- C249 (= C185) mutation to A: Loss of activity.
Query Sequence
>RR42_RS09095 FitnessBrowser__Cup4G11:RR42_RS09095
MPTDIHTLQTRLRDGAISRADVIAQAAQHAQQPDAHAVFLHTTFDTAAQVAKAADAATRA
GKPLHPLAGLPVSVKDLFNIAGEASRAGSPVRSDALAATADATVVRRLRESGAALVGRTN
MTEFAFSGVGINPHFGTPVNPADKQVARIPGGSSSGAAVSVALGLAVAGLGSDTGGSIRI
PAALCGLTGFKPTARRVPLDGAFPLSYTLDTACAMARTVQDCVLVDSVIADQAVLPVIKA
AAGIRLAIPRQVLLDGLDDTVARAFDRALGRLSAAGVQIEHIDLPELAELASINAGGGFT
AAEAHAIHRHVLATRREQYDPRVASRIDRGAAMSAADYVDLMRARLDWIARVAARIEGFD
AVTCPTVPMVAPPIAPLVADDALFFRTNALLLRNTSAFNFLDGCSISLPCHQPDELPVGL
MLSHGALRDAQLLGTAIALESIIKPAA
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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