SitesBLAST
Comparing GFF2305 FitnessBrowser__psRCH2:GFF2305 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)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
46% identity, 96% coverage: 25:599/600 of query aligns to 37:605/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (= S152) mutation to A: Loss of activity.
- S189 (= S176) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
51% identity, 64% coverage: 69:449/600 of query aligns to 63:440/461 of 4gysB
- active site: K72 (= K78), S146 (= S152), S147 (= S153), T165 (= T171), T167 (= T173), A168 (= A174), G169 (= G175), S170 (= S176), V173 (= V179)
- binding malonate ion: A120 (= A126), G122 (= G128), S146 (= S152), T167 (= T173), A168 (= A174), S170 (= S176), S193 (≠ A199), G194 (= G200), V195 (= V201), R200 (= R206), Y297 (= Y306), R305 (= R314)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 73% coverage: 9:443/600 of query aligns to 7:462/478 of 3h0mA
- active site: K72 (= K78), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), Q174 (≠ V179)
- binding glutamine: M122 (≠ T127), G123 (= G128), D167 (= D172), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), F199 (≠ A204), Y302 (vs. gap), R351 (≠ V336), D418 (= D396)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 73% coverage: 9:443/600 of query aligns to 7:462/478 of 3h0lA
- active site: K72 (= K78), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), Q174 (≠ V179)
- binding asparagine: G123 (= G128), S147 (= S152), G169 (≠ A174), G170 (= G175), S171 (= S176), Y302 (vs. gap), R351 (≠ V336), D418 (= D396)
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)
26% identity, 68% coverage: 38:446/600 of query aligns to 4:421/425 of Q9FR37
- K36 (= K78) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S152) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S153) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D172) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S176) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N184) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ P242) mutation to T: Slightly reduces catalytic activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
39% identity, 29% coverage: 69:242/600 of query aligns to 72:250/487 of 1m21A
- active site: K81 (= K78), S160 (= S152), S161 (= S153), T179 (= T171), T181 (= T173), D182 (≠ A174), G183 (= G175), S184 (= S176), C187 (≠ V179)
- binding : A129 (= A126), N130 (≠ T127), F131 (vs. gap), C158 (≠ G150), G159 (= G151), S160 (= S152), S184 (= S176), C187 (≠ V179), I212 (≠ A204)
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)
26% identity, 73% coverage: 8:447/600 of query aligns to 130:588/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 152:153) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 173:176) binding
- S305 (= S176) mutation to A: Loss of activity.
- R307 (= R178) mutation to A: Loss of activity.
- S360 (≠ L231) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 74% coverage: 8:448/600 of query aligns to 130:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A126), T258 (≠ L129), S281 (= S152), G302 (≠ T173), G303 (≠ A174), S305 (= S176), S472 (≠ V336), I532 (≠ V391), M539 (≠ G398)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 34% coverage: 5:210/600 of query aligns to 26:238/507 of Q84DC4
- T31 (≠ A10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A174) 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 (= S176) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V179) 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.
Sites not aligning to the query:
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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.
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 73% coverage: 19:456/600 of query aligns to 12:467/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
27% identity, 64% coverage: 70:451/600 of query aligns to 87:501/508 of 3a1iA
- active site: K95 (= K78), S170 (= S152), S171 (= S153), G189 (≠ T171), Q191 (≠ T173), G192 (≠ A174), G193 (= G175), A194 (≠ S176), I197 (≠ V179)
- binding benzamide: F145 (≠ T127), S146 (≠ G128), G147 (≠ L129), Q191 (≠ T173), G192 (≠ A174), G193 (= G175), A194 (≠ S176), W327 (≠ L305)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 66% coverage: 57:452/600 of query aligns to 58:478/485 of 2f2aA
- active site: K79 (= K78), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (≠ A174), G177 (= G175), S178 (= S176), Q181 (≠ V179)
- binding glutamine: G130 (= G128), S154 (= S152), D174 (= D172), T175 (= T173), G176 (≠ A174), S178 (= S176), F206 (≠ A204), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ V336), D425 (≠ G398)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 66% coverage: 57:452/600 of query aligns to 58:478/485 of 2dqnA
- active site: K79 (= K78), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (≠ A174), G177 (= G175), S178 (= S176), Q181 (≠ V179)
- binding asparagine: M129 (≠ T127), G130 (= G128), T175 (= T173), G176 (≠ A174), S178 (= S176), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ V336), D425 (≠ G398)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 29% coverage: 70:240/600 of query aligns to 30:204/450 of 4n0iA
- active site: K38 (= K78), S116 (= S152), S117 (= S153), T135 (= T171), T137 (= T173), G138 (≠ A174), G139 (= G175), S140 (= S176), L143 (≠ V179)
- binding glutamine: G89 (= G128), T137 (= T173), G138 (≠ A174), S140 (= S176), Y168 (≠ A204)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 74% coverage: 7:448/600 of query aligns to 2:412/412 of 1ocmA
- active site: K62 (= K78), S131 (= S152), S132 (= S153), T152 (= T173), G153 (≠ A174), G154 (= G175), S155 (= S176)
- binding pyrophosphate 2-: R113 (= R133), S131 (= S152), Q151 (≠ D172), T152 (= T173), G153 (≠ A174), G154 (= G175), S155 (= S176), R158 (≠ V179), P359 (vs. gap)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 74% coverage: 7:448/600 of query aligns to 2:412/412 of 1o9oA
- active site: K62 (= K78), A131 (≠ S152), S132 (= S153), T150 (= T171), T152 (= T173), G153 (≠ A174), G154 (= G175), S155 (= S176), R158 (≠ V179)
- binding 3-amino-3-oxopropanoic acid: G130 (= G151), T152 (= T173), G153 (≠ A174), G154 (= G175), S155 (= S176), R158 (≠ V179), P359 (vs. gap)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
31% identity, 38% coverage: 69:295/600 of query aligns to 73:340/564 of 6te4A
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)
36% identity, 32% coverage: 18:209/600 of query aligns to 12:207/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 32% coverage: 4:196/600 of query aligns to 2:196/457 of 5h6sC
- active site: K77 (= K78), S152 (= S152), S153 (= S153), L173 (≠ T173), G174 (≠ A174), G175 (= G175), S176 (= S176)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A126), R128 (≠ G128), W129 (≠ L129), S152 (= S152), L173 (≠ T173), G174 (≠ A174), S176 (= S176)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
33% identity, 29% coverage: 40:214/600 of query aligns to 36:208/593 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.
Query Sequence
>GFF2305 FitnessBrowser__psRCH2:GFF2305
MTTTFDLRLATLSAAYREGTTTPRQLILELRAKAAKLNGEFNAFIHLLSAAELEPFLATL
EGKAPAELPLYGIPFAIKDNIDLAGIPTTAACPAFAYTPETSATLVEQLIALGAVPLGKT
NLDQFATGLNGTRSPYGECRNSVHPDYPSGGSSAGSSLAVALGLASFALGTDTAGSGRVP
AALNNLVGLKASKGLISTAGVVPACRTLDCVTFFTATAAEASQLLALTARLDPRDEYSRS
NPLWNDGSAFGQVKSFRFGVPSQLEFLGCAESPALFAATIEQLKAIGGEPVEVDFAPFLE
AARLLYEGPWVAERYSVAGELIEQQPDAVLPVIKAVLEKAPGTTAVQLFQAQYRLQQLKA
ICDRIMAEVDCVLTPAYPRPVTLAELHAEPVKRNSDLGYYTNFMNMLDYAAVAVPAGVMR
NGLPWGVTLFGRVFTDQYLLSLADALQRQHGIALIGGQSITSPAPQNPARNDRARVVVCG
AHLDGLPLNWQLRQRGGRLLETTRSSPDYKLYALAGGPPLRPGMVRVAEGGAAVEVEVWE
LPSLELGSFLTGIPAPLGLGKVQLADGRWETGFICEPYGLDGAQDITELGGWRAYLKSRG
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