SitesBLAST
Comparing WP_018231092.1 NCBI__GCF_000378965.1:WP_018231092.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
37% identity, 80% coverage: 58:313/319 of query aligns to 57:314/334 of 5aovA
- active site: L100 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H287)
- binding glyoxylic acid: Y74 (≠ A75), A75 (= A76), V76 (≠ T77), G77 (= G78), R241 (= R237), H288 (= H287)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T77), T104 (≠ V105), F158 (≠ Y158), G159 (= G159), R160 (≠ V160), I161 (≠ L161), S180 (≠ E180), R181 (≠ S181), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (= T214), I239 (≠ T235), A240 (= A236), R241 (= R237), H288 (= H287), G290 (≠ A289)
Sites not aligning to the query:
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
37% identity, 86% coverage: 39:313/319 of query aligns to 40:304/304 of 1wwkA
- active site: S96 (≠ A101), R230 (= R237), D254 (= D261), E259 (= E266), H278 (= H287)
- binding nicotinamide-adenine-dinucleotide: V100 (= V105), G146 (= G157), F147 (≠ Y158), G148 (= G159), R149 (≠ V160), I150 (≠ L161), Y168 (≠ V183), D169 (≠ S184), P170 (= P185), V201 (≠ C208), P202 (= P209), T207 (= T214), T228 (= T235), S229 (≠ A236), D254 (= D261), H278 (= H287), G280 (≠ A289)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
34% identity, 80% coverage: 58:313/319 of query aligns to 54:320/334 of 3kb6B
- active site: S97 (≠ A101), R231 (= R237), D255 (= D261), E260 (= E266), H294 (= H287)
- binding lactic acid: S72 (≠ A76), V73 (≠ T77), G74 (= G78), Y96 (= Y100), R231 (= R237), H294 (= H287)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T77), Y96 (= Y100), V101 (= V105), G150 (= G159), R151 (≠ V160), I152 (≠ L161), D171 (vs. gap), V172 (vs. gap), P203 (= P209), T229 (= T235), A230 (= A236), R231 (= R237), H294 (= H287), A296 (= A289), Y297 (≠ W290)
Sites not aligning to the query:
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
37% identity, 84% coverage: 46:313/319 of query aligns to 43:315/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T77), T102 (≠ V105), G155 (= G157), G157 (= G159), R158 (≠ V160), T159 (≠ L161), D178 (≠ E180), P179 (≠ S181), Y180 (≠ L182), H210 (= H207), C211 (= C208), N212 (≠ P209), A238 (≠ T235), R240 (= R237), H289 (= H287), A291 (= A289), W292 (= W290)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
37% identity, 84% coverage: 46:313/319 of query aligns to 43:315/330 of 4lcjA
- active site: A98 (= A101), R240 (= R237), D264 (= D261), E269 (= E266), H289 (= H287)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ T53), H51 (≠ N54), I72 (≠ A75), G73 (≠ A76), S74 (≠ T77), G75 (= G78), R240 (= R237), H289 (= H287), W292 (= W290)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T77), T102 (≠ V105), I154 (= I156), G155 (= G157), G157 (= G159), R158 (≠ V160), T159 (≠ L161), D178 (≠ E180), Y180 (≠ L182), H210 (= H207), C211 (= C208), N212 (≠ P209), N214 (≠ T211), N217 (≠ T214), A238 (≠ T235), A239 (= A236), R240 (= R237), H289 (= H287), W292 (= W290)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
42% identity, 80% coverage: 65:319/319 of query aligns to 72:334/336 of 5z20F
- active site: S108 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H302 (= H287)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y100), G160 (= G159), Q161 (≠ V160), I162 (≠ L161), Y180 (≠ A179), D181 (≠ E180), P182 (≠ S181), C212 (= C208), P213 (= P209), T218 (= T214), T239 (= T235), G240 (≠ A236), R241 (= R237), H302 (= H287), A304 (= A289)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
37% identity, 84% coverage: 46:313/319 of query aligns to 75:347/445 of P56545
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
37% identity, 80% coverage: 58:313/319 of query aligns to 56:313/332 of 6biiA
- active site: L99 (≠ A101), R240 (= R237), D264 (= D261), E269 (= E266), H287 (= H287)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ T77), T103 (≠ V105), G156 (= G157), F157 (≠ Y158), G158 (= G159), R159 (≠ V160), I160 (≠ L161), A179 (≠ E180), R180 (≠ S181), S181 (≠ L182), K183 (≠ S184), V211 (≠ C208), P212 (= P209), E216 (≠ R213), T217 (= T214), V238 (≠ T235), A239 (= A236), R240 (= R237), D264 (= D261), H287 (= H287), G289 (≠ A289)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
37% identity, 82% coverage: 52:313/319 of query aligns to 50:316/331 of 1hl3A
- active site: S99 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H287)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V105), G158 (= G159), R159 (≠ V160), V160 (≠ L161), D179 (≠ E180), Y181 (≠ L182), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), D265 (= D261), H290 (= H287)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
37% identity, 82% coverage: 52:313/319 of query aligns to 50:316/331 of 1hkuA
- active site: S99 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H287)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T77), T103 (≠ V105), G156 (= G157), G158 (= G159), R159 (≠ V160), V160 (≠ L161), Y178 (≠ A179), D179 (≠ E180), P180 (≠ S181), Y181 (≠ L182), C212 (= C208), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H287), W293 (= W290)
Sites not aligning to the query:
4lceA Ctbp1 in complex with substrate mtob (see paper)
37% identity, 81% coverage: 56:313/319 of query aligns to 53:315/327 of 4lceA
- active site: S98 (≠ A101), R240 (= R237), D264 (= D261), E269 (= E266), H289 (= H287)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V74), G73 (≠ A76), S74 (≠ T77), G75 (= G78), R240 (= R237), H289 (= H287), W292 (= W290)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T77), T102 (≠ V105), G155 (= G157), G157 (= G159), R158 (≠ V160), V159 (≠ L161), Y177 (≠ A179), D178 (≠ E180), P179 (≠ S181), Y180 (≠ L182), H210 (= H207), C211 (= C208), N214 (≠ T211), N217 (≠ T214), T238 (= T235), A239 (= A236), R240 (= R237), W292 (= W290)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
37% identity, 81% coverage: 56:313/319 of query aligns to 54:316/328 of 4u6sA
- active site: S99 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H287)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V105), G156 (= G157), G158 (= G159), R159 (≠ V160), V160 (≠ L161), Y178 (≠ A179), D179 (≠ E180), P180 (≠ S181), Y181 (≠ L182), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H287), W293 (= W290)
- binding 3-phenylpyruvic acid: I73 (≠ A75), G74 (≠ A76), S75 (≠ T77), G76 (= G78), R241 (= R237), W293 (= W290), M302 (≠ V299)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
37% identity, 81% coverage: 56:313/319 of query aligns to 54:316/328 of 4u6qA
- active site: S99 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H287)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: I73 (≠ A75), G74 (≠ A76), S75 (≠ T77), G76 (= G78), R241 (= R237), H290 (= H287), W293 (= W290), M302 (≠ V299)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T77), T103 (≠ V105), G156 (= G157), R159 (≠ V160), V160 (≠ L161), Y178 (≠ A179), D179 (≠ E180), P180 (≠ S181), Y181 (≠ L182), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H287), W293 (= W290)
Sites not aligning to the query:
6cdfA Human ctbp1 (28-378) (see paper)
37% identity, 82% coverage: 54:313/319 of query aligns to 53:317/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V105), G157 (= G157), R160 (≠ V160), V161 (≠ L161), Y179 (≠ A179), D180 (≠ E180), P181 (≠ S181), Y182 (≠ L182), H212 (= H207), C213 (= C208), N219 (≠ T214), T240 (= T235), A241 (= A236), R242 (= R237), H291 (= H287), W294 (= W290)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
37% identity, 82% coverage: 52:313/319 of query aligns to 50:316/332 of 6v89A
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)
37% identity, 82% coverage: 54:313/319 of query aligns to 66:330/430 of Q9Z2F5
- S89 (≠ T77) binding
- IGLGRV 169:174 (≠ IGYGVL 156:161) binding
- G172 (= G159) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ E180) binding
- 226:232 (vs. 208:214, 43% identical) binding
- TAR 253:255 (= TAR 235:237) binding
- D279 (= D261) binding
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
37% identity, 82% coverage: 52:313/319 of query aligns to 75:341/440 of Q13363
- C134 (≠ A111) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ S115) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ T118) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ TR 118:119) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V127) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ C139) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ E147) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G157) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G159) 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 (= G162) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ E180) 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 (= D261) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E266) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H287) 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.
- 66 V→R: Loss of interaction with SIMC1. Reduced 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)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
32% identity, 73% coverage: 69:301/319 of query aligns to 70:309/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V154 (≠ Y158), G155 (= G159), H156 (≠ V160), I157 (≠ L161), Y175 (≠ A179), D176 (≠ E180), H205 (= H207), T206 (≠ C208), P207 (= P209), A233 (≠ T235), A234 (= A236), D259 (= D261), H295 (= H287), A297 (= A289)
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
35% identity, 80% coverage: 58:313/319 of query aligns to 57:314/333 of 2dbqA
- active site: L100 (≠ A101), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H287)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T77), T104 (≠ V105), L158 (vs. gap), G159 (vs. gap), R160 (vs. gap), I161 (vs. gap), S180 (vs. gap), R181 (vs. gap), T182 (vs. gap), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (= T214), I239 (≠ T235), A240 (= A236), R241 (= R237), D265 (= D261), H288 (= H287), G290 (≠ A289)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
35% identity, 80% coverage: 58:313/319 of query aligns to 57:314/334 of O58320
- LGRI 158:161 (vs. gap) binding
- SRT 180:182 (vs. gap) binding
- IAR 239:241 (≠ TAR 235:237) binding
- HIG 288:290 (≠ HIA 287:289) binding
Query Sequence
>WP_018231092.1 NCBI__GCF_000378965.1:WP_018231092.1
MTQLGVFLDLETVDRDDLDLSKLRAALPHWTFHAFTDSRDVAARLEGAQVAVTNKVVLDE
AALAAAPELRLICVAATGTNNVDLEAARRRDITVCNVRDYATAAVAQHVFALILSLTTRL
TAYQRDVAEGRWQASRQFCLLDHPIRELAGLTLGIIGYGVLGQGTAQAARAFGLRVAVAE
SLVSPGGDPDRWPLERLLAESDIISLHCPLTERTHHLIDAGALAAMKSDALLINTARGAI
VDNAALAAALREGEIGGAGIDVLEQEPPPADHPLLAPDIPNLIVTPHIAWAAREARQRVL
DQVEENIRAYLAGTPRHVV
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