SitesBLAST
Comparing Pf1N1B4_2954 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2954 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)
37% identity, 88% coverage: 29:309/321 of query aligns to 27:322/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), G155 (= G159), G157 (= G161), R158 (≠ E162), T159 (≠ L163), D178 (≠ Q182), P179 (vs. gap), Y180 (vs. gap), H210 (= H208), C211 (= C209), N212 (≠ P210), A238 (≠ T236), R240 (= R238), H289 (= H288), A291 (= A290), W292 (= W291)
- binding : F27 (= F29), C28 (≠ S30), E35 (≠ T38), H37 (≠ P40)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
37% identity, 88% coverage: 29:309/321 of query aligns to 27:322/330 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 (≠ T77), 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 (vs. gap), H210 (= H208), C211 (= C209), N212 (≠ P210), N214 (= N212), N217 (≠ T215), A238 (≠ T236), A239 (= A237), R240 (= R238), H289 (= H288), W292 (= W291)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
36% identity, 88% coverage: 29:309/321 of query aligns to 59:354/445 of P56545
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
37% identity, 83% coverage: 29:296/321 of query aligns to 28:298/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
37% identity, 83% coverage: 29:296/321 of query aligns to 29:299/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V107), G157 (= G159), R160 (≠ E162), V161 (≠ L163), Y179 (vs. gap), D180 (vs. gap), P181 (vs. gap), Y182 (vs. gap), H212 (= H208), C213 (= C209), N219 (≠ T215), T240 (= T236), A241 (= A237), R242 (= R238), H291 (= H288), W294 (= W291)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
36% identity, 83% coverage: 29:296/321 of query aligns to 28:298/331 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)
- binding : F28 (= F29), C29 (≠ S30), E36 (≠ T38), H38 (≠ P40), E39 (≠ D41)
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, 83% coverage: 29:296/321 of query aligns to 28:298/331 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:
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
37% identity, 83% coverage: 29:296/321 of query aligns to 28:298/328 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 (vs. gap), D179 (vs. gap), 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 (≠ T77), 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)
37% identity, 83% coverage: 29:296/321 of query aligns to 28:298/328 of 4u6qA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ S55), I73 (≠ T77), 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 (vs. gap), D179 (vs. gap), 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:
4lceA Ctbp1 in complex with substrate mtob (see paper)
37% identity, 83% coverage: 29:296/321 of query aligns to 27:297/327 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 (vs. gap), D178 (vs. gap), P179 (vs. gap), Y180 (vs. gap), H210 (= H208), C211 (= C209), N214 (= N212), N217 (≠ T215), T238 (= T236), A239 (= A237), R240 (= R238), W292 (= W291)
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)
35% identity, 89% coverage: 29:315/321 of query aligns to 42:331/430 of Q9Z2F5
- V55 (= V43) mutation to R: Strongly reduces interaction with E1A.
- 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.
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
35% identity, 89% coverage: 29:315/321 of query aligns to 53:342/440 of Q13363
- V66 (= V43) mutation to R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.
- 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.
- 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)
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)
30% identity, 91% coverage: 22:313/321 of query aligns to 69:369/466 of P87228
- S87 (≠ P40) modified: Phosphoserine
- S258 (≠ N212) modified: Phosphoserine
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
34% identity, 82% coverage: 54:315/321 of query aligns to 48:305/525 of 3ddnB
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
33% identity, 80% coverage: 60:315/321 of query aligns to 57:315/334 of 5aovA
- active site: L100 (≠ G103), R241 (= R238), D265 (= D262), E270 (≠ P268), H288 (= H288)
- binding glyoxylic acid: Y74 (≠ T77), A75 (= A78), V76 (≠ T79), G77 (= G80), R241 (= R238), H288 (= H288)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T79), T104 (≠ V107), F158 (≠ H160), G159 (= G161), R160 (≠ E162), I161 (≠ L163), S180 (≠ Q182), R181 (≠ I183), A211 (≠ H208), V212 (≠ C209), P213 (= P210), T218 (= T215), I239 (≠ T236), A240 (= A237), R241 (= R238), H288 (= H288), G290 (≠ A290)
Sites not aligning to the query:
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
34% identity, 82% coverage: 54:315/321 of query aligns to 47:304/526 of 3dc2A
Sites not aligning to the query:
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
35% identity, 76% coverage: 72:314/321 of query aligns to 77:328/336 of 5z20F
- active site: S108 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H302 (= H288)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y102), G160 (= G161), Q161 (≠ E162), I162 (≠ L163), Y180 (vs. gap), D181 (vs. gap), P182 (vs. gap), C212 (= C209), P213 (= P210), T218 (= T215), T239 (= T236), G240 (≠ A237), R241 (= R238), H302 (= H288), A304 (= A290)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
30% identity, 88% coverage: 32:314/321 of query aligns to 22:304/304 of 1wwkA
- active site: S96 (≠ G103), R230 (= R238), D254 (= D262), E259 (= E267), H278 (= H288)
- binding nicotinamide-adenine-dinucleotide: V100 (= V107), G146 (= G159), F147 (≠ H160), G148 (= G161), R149 (≠ E162), I150 (≠ L163), Y168 (vs. gap), D169 (vs. gap), P170 (vs. gap), V201 (≠ C209), P202 (= P210), T207 (= T215), T228 (= T236), S229 (≠ A237), D254 (= D262), H278 (= H288), G280 (≠ A290)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
32% identity, 87% coverage: 22:300/321 of query aligns to 20:300/406 of 2p9eA
- active site: N104 (≠ G103), R236 (= R238), D260 (= D262), E265 (= E267), H288 (= H288)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G161), H157 (≠ E162), I158 (≠ L163), Y176 (≠ G181), D177 (≠ Q182), I178 (= I183), H206 (= H208), V207 (≠ C209), P208 (= P210), S212 (≠ H214), A234 (≠ T236), S235 (≠ A237), R236 (= R238), H288 (= H288), G290 (≠ A290)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
30% identity, 91% coverage: 19:311/321 of query aligns to 24:334/346 of 4zgsA
- active site: S111 (≠ G103), R244 (= R238), D268 (= D262), E273 (= E267), H311 (= H288)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y102), G163 (= G161), A164 (≠ E162), I165 (≠ L163), D184 (≠ Q182), C215 (= C209), P216 (= P210), L218 (≠ N212), S220 (≠ H214), T221 (= T215), S243 (≠ A237), H311 (= H288), F314 (≠ W291)
Query Sequence
>Pf1N1B4_2954 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2954
MTNSRRAVFLDHPSLDLGDLNLNPLRECFSDLQLFAQTMPDQVIERLKGASVAISNKIVI
DAAAMAASPELKLILITATGTNNVDLAAARAHGITVCNCQGYGTPSVAQHTIMLLLNLAT
RLADYQKAVAEGRWQQAKQFCLLDYPIVELEGKTLGLLGHGELGSAVARLAEAFGMRVML
GQIPGRPARPDRLPLDELLPQIDALTLHCPLNEHTRHFIGARELASMKPGAFVVNTARGG
LIDEQALADALRNGHLGGAATDVLSVEPPTAGNPLLAQDIPRLIVTPHNAWGSREARQRI
VGQLTENARGYFSGQALRVVS
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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