SitesBLAST
Comparing 6938708 FitnessBrowser__SB2B:6938708 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)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
36% identity, 81% coverage: 56:311/317 of query aligns to 54:321/334 of 3kb6B
- active site: S97 (≠ G99), R231 (= R237), D255 (= D260), E260 (= E265), H294 (= H284)
- binding lactic acid: S72 (≠ A74), V73 (≠ T75), G74 (= G76), Y96 (= Y98), R231 (= R237), H294 (= H284)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T75), Y96 (= Y98), V101 (= V103), G150 (= G157), R151 (≠ D158), I152 (= I159), D171 (≠ S178), V172 (≠ R179), P203 (= P209), T229 (= T235), A230 (= A236), R231 (= R237), H294 (= H284), A296 (= A286), Y297 (≠ W287)
Sites not aligning to the query:
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
36% identity, 87% coverage: 35:311/317 of query aligns to 35:315/334 of 5aovA
- active site: L100 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H288 (= H284)
- binding glyoxylic acid: M52 (≠ N52), L53 (vs. gap), L53 (vs. gap), Y74 (≠ L73), A75 (= A74), V76 (≠ T75), G77 (= G76), R241 (= R237), H288 (= H284)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T75), T104 (≠ V103), F158 (= F156), G159 (= G157), R160 (≠ D158), I161 (= I159), S180 (= S178), R181 (= R179), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (= T214), I239 (≠ T235), A240 (= A236), R241 (= R237), H288 (= H284), G290 (≠ A286)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
36% identity, 78% coverage: 70:316/317 of query aligns to 79:334/336 of 5z20F
- active site: S108 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H302 (= H284)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y98), G160 (= G157), Q161 (≠ D158), I162 (= I159), Y180 (≠ H177), D181 (≠ S178), P182 (vs. gap), C212 (= C208), P213 (= P209), T218 (= T214), T239 (= T235), G240 (≠ A236), R241 (= R237), H302 (= H284), A304 (= A286)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 87% coverage: 35:311/317 of query aligns to 34:314/332 of 6biiA
- active site: L99 (≠ G99), R240 (= R237), D264 (= D260), E269 (= E265), H287 (= H284)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ T75), T103 (≠ V103), G156 (= G155), F157 (= F156), G158 (= G157), R159 (≠ D158), I160 (= I159), A179 (≠ S178), R180 (= R179), S181 (= S180), K183 (= K181), V211 (≠ C208), P212 (= P209), E216 (≠ D213), T217 (= T214), V238 (≠ T235), A239 (= A236), R240 (= R237), D264 (= D260), H287 (= H284), G289 (≠ A286)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
32% identity, 85% coverage: 37:305/317 of query aligns to 38:310/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T75), T102 (≠ V103), G155 (= G155), G157 (= G157), R158 (≠ D158), T159 (≠ I159), D178 (≠ S178), P179 (≠ R179), Y180 (≠ S180), H210 (= H207), C211 (= C208), N212 (≠ P209), A238 (≠ T235), R240 (= R237), H289 (= H284), A291 (= A286), W292 (= W287)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
32% identity, 85% coverage: 37:305/317 of query aligns to 38:310/330 of 4lcjA
- active site: A98 (≠ G99), R240 (= R237), D264 (= D260), E269 (= E265), H289 (= H284)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ T51), H51 (≠ N52), I72 (≠ L73), G73 (≠ A74), S74 (≠ T75), G75 (= G76), R240 (= R237), H289 (= H284), W292 (= W287)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T75), T102 (≠ V103), I154 (≠ V154), G155 (= G155), G157 (= G157), R158 (≠ D158), T159 (≠ I159), D178 (≠ S178), Y180 (≠ S180), H210 (= H207), C211 (= C208), N212 (≠ P209), N214 (≠ T211), N217 (≠ T214), A238 (≠ T235), A239 (= A236), R240 (= R237), H289 (= H284), W292 (= W287)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 39:311/328 of 4u6sA
- active site: S99 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H290 (= H284)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V103), G156 (= G155), G158 (= G157), R159 (≠ D158), V160 (≠ I159), Y178 (≠ H177), D179 (≠ S178), P180 (vs. gap), Y181 (vs. gap), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H284), W293 (= W287)
- binding 3-phenylpyruvic acid: Y51 (≠ T51), H52 (≠ N52), I73 (≠ L73), G74 (≠ A74), S75 (≠ T75), G76 (= G76), R241 (= R237), W293 (= W287), M302 (≠ L296)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 39:311/328 of 4u6qA
- active site: S99 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H290 (= H284)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ T51), I73 (≠ L73), G74 (≠ A74), S75 (≠ T75), G76 (= G76), R241 (= R237), H290 (= H284), W293 (= W287), M302 (≠ L296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T75), T103 (≠ V103), G156 (= G155), R159 (≠ D158), V160 (≠ I159), Y178 (≠ H177), D179 (≠ S178), P180 (vs. gap), Y181 (vs. gap), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H284), W293 (= W287)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 39:311/332 of 6v89A
4lceA Ctbp1 in complex with substrate mtob (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 38:310/327 of 4lceA
- active site: S98 (≠ G99), R240 (= R237), D264 (= D260), E269 (= E265), H289 (= H284)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V72), G73 (≠ A74), S74 (≠ T75), G75 (= G76), R240 (= R237), H289 (= H284), W292 (= W287)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T75), T102 (≠ V103), G155 (= G155), G157 (= G157), R158 (≠ D158), V159 (≠ I159), Y177 (≠ H177), D178 (≠ S178), P179 (vs. gap), Y180 (vs. gap), H210 (= H207), C211 (= C208), N214 (≠ T211), N217 (≠ T214), T238 (= T235), A239 (= A236), R240 (= R237), W292 (= W287)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
32% identity, 85% coverage: 37:305/317 of query aligns to 70:342/445 of P56545
6cdfA Human ctbp1 (28-378) (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 40:312/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V103), G157 (= G155), R160 (≠ D158), V161 (≠ I159), Y179 (≠ H177), D180 (≠ S178), P181 (vs. gap), Y182 (vs. gap), H212 (= H207), C213 (= C208), N219 (≠ T214), T240 (= T235), A241 (= A236), R242 (= R237), H291 (= H284), W294 (= W287)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 39:311/331 of 1hl3A
- active site: S99 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H290 (= H284)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V103), G158 (= G157), R159 (≠ D158), V160 (≠ I159), D179 (≠ S178), Y181 (vs. gap), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), D265 (= D260), H290 (= H284)
- binding : E39 (= E37)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
33% identity, 85% coverage: 37:305/317 of query aligns to 39:311/331 of 1hkuA
- active site: S99 (≠ G99), R241 (= R237), D265 (= D260), E270 (= E265), H290 (= H284)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T75), T103 (≠ V103), G156 (= G155), G158 (= G157), R159 (≠ D158), V160 (≠ I159), Y178 (≠ H177), D179 (≠ S178), P180 (vs. gap), Y181 (vs. gap), C212 (= C208), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H284), W293 (= W287)
Sites not aligning to the query:
Q9Z2F5 C-terminal-binding protein 1; CtBP1; 50 kDa BFA-dependent ADP-ribosylation substrate; BARS-50; C-terminal-binding protein 3; CtBP3; EC 1.1.1.- from Rattus norvegicus (Rat) (see 3 papers)
33% identity, 85% coverage: 37:305/317 of query aligns to 53:325/430 of Q9Z2F5
- V55 (≠ I39) mutation to R: Strongly reduces interaction with E1A.
- S89 (≠ T75) binding
- IGLGRV 169:174 (≠ VGFGDI 154:159) binding
- G172 (= G157) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ S178) binding
- 226:232 (vs. 208:214, 29% identical) binding
- TAR 253:255 (= TAR 235:237) binding
- D279 (= D260) binding
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
33% identity, 85% coverage: 37:305/317 of query aligns to 64:336/440 of Q13363
- V66 (≠ I39) mutation to R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.
- C134 (≠ A109) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ H113) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ S116) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ SR 116:117) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V125) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ F138) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ S145) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G155) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G157) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-186.; mutation to V: Strongly reduces E1A binding; when associated with V-181 and A-204.
- G186 (≠ A160) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ S178) mutation to A: Strongly reduces E1A binding; when associated with V-181 and V-183.; mutation to L: Reduced proteolytic processing mediated by CAPN3.
- R266 (= R237) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D260) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E265) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H284) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295.
Sites not aligning to the query:
- 52 A→E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.
- 375:376 Cleavage; by CAPN1
- 387:388 Cleavage; by CAPN1
- 409:410 Cleavage; by CAPN1 and CAPN3
- 422 modified: Phosphoserine; by HIPK2; S→A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance.
- 428 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 78% coverage: 48:295/317 of query aligns to 45:289/304 of 1wwkA
- active site: S96 (≠ G99), R230 (= R237), D254 (= D260), E259 (= E265), H278 (= H284)
- binding nicotinamide-adenine-dinucleotide: V100 (= V103), G146 (= G155), F147 (= F156), G148 (= G157), R149 (≠ D158), I150 (= I159), Y168 (≠ H177), D169 (vs. gap), P170 (vs. gap), V201 (≠ C208), P202 (= P209), T207 (= T214), T228 (= T235), S229 (≠ A236), D254 (= D260), H278 (= H284), G280 (≠ A286)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
33% identity, 84% coverage: 48:313/317 of query aligns to 32:324/330 of 4cukA
- active site: S101 (≠ G99), R234 (= R237), D258 (= D260), E263 (= E265), H295 (= H284)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y98), G153 (= G157), K154 (≠ D158), I155 (= I159), F173 (≠ H177), D174 (≠ S178), P175 (≠ R179), H204 (= H207), C205 (= C208), P206 (= P209), N211 (≠ T214), T232 (= T235), Y260 (≠ L262), H295 (= H284), A297 (= A286)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
30% identity, 79% coverage: 67:316/317 of query aligns to 70:327/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y98), I106 (≠ V103), V154 (≠ F156), G155 (= G157), H156 (≠ D158), I157 (= I159), Y175 (≠ H177), D176 (≠ S178), H205 (= H207), T206 (≠ C208), P207 (= P209), A233 (≠ T235), A234 (= A236), D259 (= D260), H295 (= H284), A297 (= A286)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
34% identity, 84% coverage: 48:313/317 of query aligns to 45:306/526 of 3dc2A
Sites not aligning to the query:
Query Sequence
>6938708 FitnessBrowser__SB2B:6938708
MTAICVLDGFTLNPGDLDWSPLADIGPFDVHDRTPKELILSRAAGARFLLTNKTVLDAAT
LEAMPSLEYIGVLATGTNVVDVAAAKRLGIAVTNVPGYGPDAVAQMGFAHVLHHMSRVSA
HHDAVTQGQWSGQADFCFTLGQLESLSGKTLGLVGFGDIARQMARIGMAFGMKLLVHSRS
KPTDLPEGAKFVALDTLFAESDVLSLHCPLTDDTRDMVNRESLALMKQGALLINTARGGL
VDEVALADALNAGRVRAGVDVLSTEPPAPNNPLLHAANISITPHNAWATVKARQKLLDIA
VENLRAFSRGESVNRVD
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