SitesBLAST
Comparing 8501168 FitnessBrowser__Miya:8501168 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)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
39% identity, 77% coverage: 56:287/301 of query aligns to 52:301/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T78), T102 (≠ V106), G155 (= G150), G157 (= G152), R158 (= R153), T159 (≠ I154), D178 (= D173), P179 (= P174), Y180 (≠ F175), H210 (= H199), C211 (= C200), N212 (≠ S201), A238 (= A227), R240 (= R229), H289 (= H275), A291 (≠ G277), W292 (≠ S278)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
39% identity, 77% coverage: 56:287/301 of query aligns to 52:301/330 of 4lcjA
- active site: A98 (≠ P102), R240 (= R229), D264 (= D253), E269 (= E258), H289 (= H275)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: I72 (≠ C76), G73 (= G77), S74 (≠ T78), G75 (= G79), R240 (= R229), H289 (= H275), W292 (≠ S278)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T78), T102 (≠ V106), I154 (= I149), G155 (= G150), G157 (= G152), R158 (= R153), T159 (≠ I154), D178 (= D173), Y180 (≠ F175), H210 (= H199), C211 (= C200), N212 (≠ S201), N214 (≠ P203), N217 (≠ G206), A238 (= A227), A239 (= A228), R240 (= R229), H289 (= H275), W292 (≠ S278)
Sites not aligning to the query:
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
37% identity, 91% coverage: 11:284/301 of query aligns to 7:287/304 of 1wwkA
- active site: S96 (≠ P102), R230 (= R229), D254 (= D253), E259 (= E258), H278 (= H275)
- binding nicotinamide-adenine-dinucleotide: V100 (= V106), G146 (= G150), F147 (= F151), G148 (= G152), R149 (= R153), I150 (= I154), Y168 (≠ A172), D169 (= D173), P170 (= P174), V201 (≠ C200), P202 (≠ S201), T207 (≠ G206), T228 (≠ A227), S229 (≠ A228), D254 (= D253), H278 (= H275), G280 (= G277)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
39% identity, 76% coverage: 59:287/301 of query aligns to 87:333/445 of P56545
4lceA Ctbp1 in complex with substrate mtob (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 52:313/327 of 4lceA
- active site: S98 (≠ P102), R240 (= R229), D264 (= D253), E269 (= E258), H289 (= H275)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (= R75), G73 (= G77), S74 (≠ T78), G75 (= G79), R240 (= R229), H289 (= H275), W292 (≠ S278)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T78), T102 (≠ V106), G155 (= G150), G157 (= G152), R158 (= R153), V159 (≠ I154), Y177 (≠ A172), D178 (= D173), P179 (= P174), Y180 (≠ F175), H210 (= H199), C211 (= C200), N214 (≠ P203), N217 (≠ G206), T238 (≠ A227), A239 (= A228), R240 (= R229), W292 (≠ S278)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 53:314/328 of 4u6sA
- active site: S99 (≠ P102), R241 (= R229), D265 (= D253), E270 (= E258), H290 (= H275)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V106), G156 (= G150), G158 (= G152), R159 (= R153), V160 (≠ I154), Y178 (≠ A172), D179 (= D173), P180 (= P174), Y181 (≠ F175), H211 (= H199), C212 (= C200), G213 (≠ S201), N218 (≠ G206), T239 (≠ A227), A240 (= A228), R241 (= R229), H290 (= H275), W293 (≠ S278)
- binding 3-phenylpyruvic acid: I73 (≠ C76), G74 (= G77), S75 (≠ T78), G76 (= G79), R241 (= R229), W293 (≠ S278), M302 (= M287)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 53:314/328 of 4u6qA
- active site: S99 (≠ P102), R241 (= R229), D265 (= D253), E270 (= E258), H290 (= H275)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: I73 (≠ C76), G74 (= G77), S75 (≠ T78), G76 (= G79), R241 (= R229), H290 (= H275), W293 (≠ S278), M302 (= M287)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T78), T103 (≠ V106), G156 (= G150), R159 (= R153), V160 (≠ I154), Y178 (≠ A172), D179 (= D173), P180 (= P174), Y181 (≠ F175), H211 (= H199), C212 (= C200), G213 (≠ S201), N218 (≠ G206), T239 (≠ A227), A240 (= A228), R241 (= R229), H290 (= H275), W293 (≠ S278)
Sites not aligning to the query:
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 53:314/331 of 1hl3A
- active site: S99 (≠ P102), R241 (= R229), D265 (= D253), E270 (= E258), H290 (= H275)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V106), G158 (= G152), R159 (= R153), V160 (≠ I154), D179 (= D173), Y181 (≠ F175), H211 (= H199), C212 (= C200), G213 (≠ S201), N218 (≠ G206), T239 (≠ A227), A240 (= A228), R241 (= R229), D265 (= D253), H290 (= H275)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 53:314/331 of 1hkuA
- active site: S99 (≠ P102), R241 (= R229), D265 (= D253), E270 (= E258), H290 (= H275)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T78), T103 (≠ V106), G156 (= G150), G158 (= G152), R159 (= R153), V160 (≠ I154), Y178 (≠ A172), D179 (= D173), P180 (= P174), Y181 (≠ F175), C212 (= C200), N218 (≠ G206), T239 (≠ A227), A240 (= A228), R241 (= R229), H290 (= H275), W293 (≠ S278)
Sites not aligning to the query:
6cdfA Human ctbp1 (28-378) (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 54:315/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V106), G157 (= G150), R160 (= R153), V161 (≠ I154), Y179 (≠ A172), D180 (= D173), P181 (= P174), Y182 (≠ F175), H212 (= H199), C213 (= C200), N219 (≠ G206), T240 (≠ A227), A241 (= A228), R242 (= R229), H291 (= H275), W294 (≠ S278)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
36% identity, 81% coverage: 56:299/301 of query aligns to 53:314/332 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)
36% identity, 80% coverage: 59:299/301 of query aligns to 70:328/430 of Q9Z2F5
- S89 (≠ T78) binding
- IGLGRV 169:174 (≠ IGFGRI 149:154) binding
- G172 (= G152) mutation to E: Loss dimerization and of NAD binding.
- D193 (= D173) binding
- 226:232 (vs. 200:206, 29% identical) binding
- TAR 253:255 (≠ AAR 227:229) binding
- D279 (= D253) 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)
35% identity, 80% coverage: 59:299/301 of query aligns to 81:339/440 of Q13363
- C134 (≠ G112) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ D116) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R119) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ RL 119:120) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (= L128) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (vs. gap) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (vs. gap) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G150) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G152) 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 (= G155) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (= D173) 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 (= R229) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D253) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E258) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H275) 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)
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 15:299/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ P102), A100 (≠ V106), R149 (= R153), I150 (= I154), Y168 (≠ A172), D169 (= D173), P170 (= P174), I171 (≠ F175), H200 (= H199), T201 (≠ C200), P202 (≠ S201), T207 (≠ G206), C228 (≠ A227), A229 (= A228), R230 (= R229), H277 (= H275), G279 (= G277)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 16:300/301 of 6rj5A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 13:297/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G152), I148 (= I154), Y166 (≠ A172), D167 (= D173), P168 (= P174), I169 (≠ F175), I170 (≠ A176), H198 (= H199), T199 (≠ C200), L208 (≠ I209), R228 (= R229)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 16:300/303 of 6plgA
7dkmA Phgdh covalently linked to oridonin (see paper)
35% identity, 89% coverage: 19:286/301 of query aligns to 17:290/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (= T78), A102 (≠ V106), G148 (= G150), R151 (= R153), I152 (= I154), Y170 (≠ A172), D171 (= D173), P172 (= P174), I173 (≠ F175), H202 (= H199), T203 (≠ C200), P204 (≠ S201), T209 (≠ G206), C230 (≠ A227), A231 (= A228), R232 (= R229), H279 (= H275), G281 (= G277)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: K17 (≠ R19), I18 (≠ L20)
Sites not aligning to the query:
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: 14, 293
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 16:300/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I149), G147 (= G150), L148 (≠ F151), G149 (= G152), R150 (= R153), I151 (= I154), G152 (= G155), D170 (= D173), H201 (= H199), T202 (≠ C200), P203 (≠ S201)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
34% identity, 93% coverage: 19:297/301 of query aligns to 16:300/302 of 6rihA
Query Sequence
>8501168 FitnessBrowser__Miya:8501168
MKVAITTSSFAKFSDEPLRLLREAGIEYVLNPTGRAITEDEAIELLQGCIGVAAGTEPLT
RRVMQALPELKVISRCGTGMDSVDRAAAAELGIAVRNTPDAPTLAVAELTLGYALDLMRL
VSRMDRELRAGTWKKRMGNLLAGKKVGLIGFGRIGRATGKLFEAFGCEVAFADPFAESDT
NARMEVDALLAWADIVSLHCSKPEGGGYILDEHRLGLMRPGTWVINAARGGLIDEAALHA
LLASGHLAGAALDVFAKEPYEGPLRDLPNVILTPHVGSYAVEARVKMETDTIRNLLDALP
R
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