SitesBLAST
Comparing Pf1N1B4_3300 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3300 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, 95% coverage: 26:588/592 of query aligns to 42:602/605 of Q936X2
- K91 (= K76) mutation to A: Loss of activity.
- S165 (= S150) mutation to A: Loss of activity.
- S189 (= S174) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
50% identity, 70% coverage: 38:449/592 of query aligns to 34:440/461 of 4gysB
- active site: K72 (= K76), S146 (= S150), S147 (= S151), T165 (= T169), T167 (= T171), A168 (= A172), G169 (= G173), S170 (= S174), V173 (= V177)
- binding malonate ion: A120 (= A124), G122 (= G126), S146 (= S150), T167 (= T171), A168 (= A172), S170 (= S174), S193 (≠ A197), G194 (= G198), V195 (= V199), R200 (= R204), Y297 (= Y306), R305 (= R314)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 74% coverage: 7:443/592 of query aligns to 7:462/478 of 3h0mA
- active site: K72 (= K76), S147 (≠ G149), S148 (= S150), S166 (≠ T169), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), Q174 (≠ V177)
- binding glutamine: M122 (≠ T125), G123 (= G126), D167 (= D170), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), F199 (≠ A202), Y302 (vs. gap), R351 (≠ P331), D418 (≠ N402)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 74% coverage: 7:443/592 of query aligns to 7:462/478 of 3h0lA
- active site: K72 (= K76), S147 (≠ G149), S148 (= S150), S166 (≠ T169), T168 (= T171), G169 (≠ A172), G170 (= G173), S171 (= S174), Q174 (≠ V177)
- binding asparagine: G123 (= G126), S147 (≠ G149), G169 (≠ A172), G170 (= G173), S171 (= S174), Y302 (vs. gap), R351 (≠ P331), D418 (≠ N402)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 73% coverage: 10:443/592 of query aligns to 5:450/468 of 3kfuE
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)
39% identity, 28% coverage: 68:231/592 of query aligns to 28:197/425 of Q9FR37
- K36 (= K76) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S150) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S151) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D170) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S174) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N182) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 64% coverage: 67:443/592 of query aligns to 72:472/487 of 1m21A
- active site: K81 (= K76), S160 (= S150), S161 (= S151), T179 (= T169), T181 (= T171), D182 (≠ A172), G183 (= G173), S184 (= S174), C187 (≠ V177)
- binding : A129 (= A124), N130 (≠ T125), F131 (vs. gap), C158 (≠ G148), G159 (= G149), S160 (= S150), S184 (= S174), C187 (≠ V177), I212 (≠ A202), R318 (= R303), L321 (= L304), L365 (≠ V336), F426 (vs. gap)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 74% coverage: 13:448/592 of query aligns to 137:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A124), T258 (≠ L127), S281 (= S150), G302 (≠ T171), G303 (≠ A172), S305 (= S174), S472 (≠ V329), I532 (≠ L397), M539 (= M404)
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)
28% identity, 64% coverage: 68:448/592 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 150:151) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 171:174) binding
- S305 (= S174) mutation to A: Loss of activity.
- R307 (= R176) mutation to A: Loss of activity.
- S360 (≠ L229) mutation to A: No effect.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 66% coverage: 68:457/592 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K76), S170 (= S150), S171 (= S151), G189 (≠ T169), Q191 (≠ T171), G192 (≠ A172), G193 (= G173), A194 (≠ S174), I197 (≠ V177)
- binding benzamide: F145 (≠ T125), S146 (≠ G126), G147 (≠ L127), Q191 (≠ T171), G192 (≠ A172), G193 (= G173), A194 (≠ S174), W327 (≠ L305)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 73% coverage: 18:452/592 of query aligns to 19:478/485 of 2f2aA
- active site: K79 (= K76), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (≠ A172), G177 (= G173), S178 (= S174), Q181 (≠ V177)
- binding glutamine: G130 (= G126), S154 (= S150), D174 (= D170), T175 (= T171), G176 (≠ A172), S178 (= S174), F206 (≠ A202), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ A335), D425 (≠ F403)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 73% coverage: 18:452/592 of query aligns to 19:478/485 of 2dqnA
- active site: K79 (= K76), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (≠ A172), G177 (= G173), S178 (= S174), Q181 (≠ V177)
- binding asparagine: M129 (≠ T125), G130 (= G126), T175 (= T171), G176 (≠ A172), S178 (= S174), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ A335), D425 (≠ F403)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 74% coverage: 18:458/592 of query aligns to 41:497/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A172) 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 (= S174) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V177) 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 (≠ A302) 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 (= Q352) 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 (≠ G398) 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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 33% coverage: 68:260/592 of query aligns to 30:227/450 of 4n0iA
- active site: K38 (= K76), S116 (= S150), S117 (= S151), T135 (= T169), T137 (= T171), G138 (≠ A172), G139 (= G173), S140 (= S174), L143 (≠ V177)
- binding glutamine: G89 (= G126), T137 (= T171), G138 (≠ A172), S140 (= S174), Y168 (≠ A202)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
31% identity, 39% coverage: 67:295/592 of query aligns to 73:340/564 of 6te4A
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
26% identity, 65% coverage: 73:455/592 of query aligns to 66:463/593 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.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 75% coverage: 5:447/592 of query aligns to 2:407/412 of 1o9oA
- active site: K62 (= K76), A131 (vs. gap), S132 (= S151), T150 (= T169), T152 (= T171), G153 (≠ A172), G154 (= G173), S155 (= S174), R158 (≠ V177)
- binding 3-amino-3-oxopropanoic acid: G130 (vs. gap), T152 (= T171), G153 (≠ A172), G154 (= G173), S155 (= S174), R158 (≠ V177), P359 (≠ G398)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 75% coverage: 5:447/592 of query aligns to 2:407/412 of 1ocmA
- active site: K62 (= K76), S131 (= S150), S132 (= S151), T152 (= T171), G153 (≠ A172), G154 (= G173), S155 (= S174)
- binding pyrophosphate 2-: R113 (= R131), S131 (= S150), Q151 (≠ D170), T152 (= T171), G153 (≠ A172), G154 (= G173), S155 (= S174), R158 (≠ V177), P359 (≠ G398)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
39% identity, 24% coverage: 67:207/592 of query aligns to 65:207/457 of 6c6gA
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)
30% identity, 34% coverage: 1:199/592 of query aligns to 73:266/579 of Q9TUI8
- S217 (= S150) mutation to A: Loss of activity.
- S218 (= S151) mutation to A: Lowers activity by at least 98%.
- D237 (= D170) mutation D->E,N: Loss of activity.
- S241 (= S174) mutation to A: Loss of activity.
- C249 (≠ N182) mutation to A: Loss of activity.
Query Sequence
>Pf1N1B4_3300 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3300
MNINLQLDALRNAYHQGQITPRQLLLNLREKAAALNPDYHLFIHLLSVEELEPYLAALDG
RDPGSLPLYGVPFAIKDNIDLAGIPTTAACPAFAYVPERSATVVEQLLALGAIPLGKTNL
DQFATGLNGSRSPYGACPNSVLPEYPSGGSSAGSSLAVALGVASFSLGTDTAGSGRVPAA
LNNLVGLKASKGLISTAGVVPACRTLDCVTTFTATAREASQLLALTAHLDPRDEYSRSNP
LWNDGSAFGTPRPLRFGVPRAQDLAFFGCPEGPLLFGDAIDQLKAMGGEAVELDLSPFLE
AARLLYEGPWVAERYSVAGELMEQHPQAVLPVIRAVLDKAPAVTGVQTFRAQYRLQALKA
LCDKALEGLDCVVTPTIGRPVTRAELAAEPVLRNSELGYYTNFMNLLDYAAVAVPSGFMG
NGLPWGVTLFGRVFTDQYLLSVADTLQRQQGLAAPAPTNIARNDRARLVVCGAHLDGLAL
NWQLKQRGARLLEATHSSPDYQLYALAGGPPYRPGMVRVKEGGAAIAVEVWELPSSELGS
FLTAIPAPLGLGKVQLADGRWESGFICEPYGLEGAVDISHLGGWRAYLNDRR
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