SitesBLAST
Comparing AO353_15000 FitnessBrowser__pseudo3_N2E3:AO353_15000 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, 76% coverage: 54:296/321 of query aligns to 49:297/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), G155 (= G159), G157 (= G161), R158 (≠ E162), T159 (≠ L163), D178 (≠ Q182), P179 (= P184), Y180 (≠ G185), H210 (= H208), C211 (= C209), N212 (≠ P210), A238 (≠ T236), R240 (= R238), H289 (= H288), A291 (= A290), W292 (= W291)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 49:297/330 of 4lcjA
- active site: A98 (≠ G103), R240 (= R238), D264 (= D262), E269 (= E267), H289 (= H288)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ S55), H51 (≠ N56), I72 (≠ A77), G73 (≠ A78), S74 (≠ T79), G75 (= G80), R240 (= R238), H289 (= H288), W292 (= W291)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), I154 (≠ L158), G155 (= G159), G157 (= G161), R158 (≠ E162), T159 (≠ L163), D178 (≠ Q182), Y180 (≠ G185), H210 (= H208), C211 (= C209), N212 (≠ P210), N214 (= N212), N217 (≠ T215), A238 (≠ T236), A239 (= A237), R240 (= R238), H289 (= H288), W292 (= W291)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 90% coverage: 17:306/321 of query aligns to 69:362/466 of P87228
- S87 (≠ T39) modified: Phosphoserine
- S258 (≠ N212) modified: Phosphoserine
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
30% identity, 93% coverage: 21:319/321 of query aligns to 12:325/334 of 3kb6B
- active site: S97 (≠ G103), R231 (= R238), D255 (= D262), E260 (vs. gap), H294 (= H288)
- binding lactic acid: F49 (≠ A53), S72 (≠ A78), V73 (≠ T79), G74 (= G80), Y96 (= Y102), R231 (= R238), H294 (= H288)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T79), Y96 (= Y102), V101 (= V107), G150 (= G161), R151 (≠ E162), I152 (≠ L163), D171 (≠ Q182), V172 (≠ L183), P203 (= P210), T229 (= T236), A230 (= A237), R231 (= R238), H294 (= H288), A296 (= A290), Y297 (≠ W291)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 50:298/328 of 4u6sA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G156 (= G159), G158 (= G161), R159 (≠ E162), V160 (≠ L163), Y178 (≠ G181), D179 (≠ Q182), P180 (vs. gap), Y181 (vs. gap), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
- binding 3-phenylpyruvic acid: Y51 (≠ S55), H52 (≠ N56), I73 (≠ A77), G74 (≠ A78), S75 (≠ T79), G76 (= G80), R241 (= R238), W293 (= W291)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 50:298/328 of 4u6qA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ S55), I73 (≠ A77), G74 (≠ A78), S75 (≠ T79), G76 (= G80), R241 (= R238), H290 (= H288), W293 (= W291)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T79), T103 (≠ V107), G156 (= G159), R159 (≠ E162), V160 (≠ L163), Y178 (≠ G181), D179 (≠ Q182), P180 (vs. gap), Y181 (vs. gap), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
Sites not aligning to the query:
6cdfA Human ctbp1 (28-378) (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 51:299/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V107), G157 (= G159), R160 (≠ E162), V161 (≠ L163), Y179 (≠ G181), D180 (≠ Q182), P181 (vs. gap), Y182 (vs. gap), H212 (= H208), C213 (= C209), N219 (≠ T215), T240 (= T236), A241 (= A237), R242 (= R238), H291 (= H288), W294 (= W291)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 50:298/332 of 6v89A
4lceA Ctbp1 in complex with substrate mtob (see paper)
39% identity, 76% coverage: 54:296/321 of query aligns to 49:297/327 of 4lceA
- active site: S98 (≠ G103), R240 (= R238), D264 (= D262), E269 (= E267), H289 (= H288)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ I76), G73 (≠ A78), S74 (≠ T79), G75 (= G80), R240 (= R238), H289 (= H288), W292 (= W291)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), G155 (= G159), G157 (= G161), R158 (≠ E162), V159 (≠ L163), Y177 (≠ G181), D178 (≠ Q182), P179 (vs. gap), Y180 (vs. gap), H210 (= H208), C211 (= C209), N214 (= N212), N217 (≠ T215), T238 (= T236), A239 (= A237), R240 (= R238), W292 (= W291)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
37% identity, 76% coverage: 54:296/321 of query aligns to 50:298/331 of 1hl3A
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G158 (= G161), R159 (≠ E162), V160 (≠ L163), D179 (≠ Q182), Y181 (≠ A188), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), D265 (= D262), H290 (= H288)
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, 76% coverage: 54:296/321 of query aligns to 50:298/331 of 1hkuA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T79), T103 (≠ V107), G156 (= G159), G158 (= G161), R159 (≠ E162), V160 (≠ L163), Y178 (≠ G181), D179 (≠ Q182), P180 (= P187), Y181 (≠ A188), C212 (= C209), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
Sites not aligning to the query:
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
38% identity, 76% coverage: 54:296/321 of query aligns to 81:329/445 of P56545
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, 76% coverage: 54:296/321 of query aligns to 64:312/430 of Q9Z2F5
- S89 (≠ T79) binding
- IGLGRV 169:174 (≠ LGHGEL 158:163) binding
- G172 (= G161) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ Q182) binding
- 226:232 (vs. 209:215, 71% identical) binding
- TAR 253:255 (= TAR 236:238) binding
- D279 (= D262) 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)
36% identity, 79% coverage: 54:307/321 of query aligns to 75:346/440 of Q13363
- C134 (≠ M113) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (= N117) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ T120) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ TR 120:121) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V129) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ C141) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ E149) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G159) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G161) 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 (= G164) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ Q182) 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 (= R238) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D262) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E267) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H288) 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)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 26:289/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (= L158), G147 (= G159), L148 (≠ H160), G149 (= G161), R150 (≠ E162), I151 (≠ L163), G152 (= G164), D170 (≠ L183), H201 (= H208), T202 (≠ C209), P203 (= P210)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 26:289/302 of 6rihA
7dkmA Phgdh covalently linked to oridonin (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 27:290/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (= T79), A102 (≠ V107), G148 (= G159), R151 (≠ E162), I152 (≠ L163), Y170 (≠ Q182), D171 (≠ L183), P172 (= P184), I173 (vs. gap), H202 (= H208), T203 (≠ C209), P204 (= P210), T209 (= T215), C230 (≠ T236), A231 (= A237), R232 (= R238), H279 (= H288), G281 (≠ A290)
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, 17, 18, 293
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 26:289/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 26:289/303 of 6plgA
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
33% identity, 83% coverage: 32:299/321 of query aligns to 27:290/305 of 6plfA
Query Sequence
>AO353_15000 FitnessBrowser__pseudo3_N2E3:AO353_15000
MTNNRRAVFLDHSSLDLGDLDLSGLQQCFDDLQLRSLTTPDNIVERLQGASVAISNKVPL
NAETLKACPELQLILIAATGTNNVDLAAARAQGITVSNCQGYGTPSVAQHTIMLLLNLAT
RLSDYQKAVAEGRWQQAKQFCLLDFPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVLL
GQLPGRPARADRLPLDELLPQIDALTLHCPLNEHTRNFIGARELALLKPGAFVVNTARGG
LIDEQALADALRNGHLGGAATDVLSVEPPTAGNPLLAADIPRLIVTPHNAWGSREARQRI
VGQLTENAQGFFSGTARRVVS
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