SitesBLAST
Comparing WP_012466797.1 NCBI__GCF_000020465.1:WP_012466797.1 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)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
31% identity, 93% coverage: 16:265/269 of query aligns to 34:298/526 of 3dc2A
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
31% identity, 93% coverage: 16:265/269 of query aligns to 35:299/525 of 3ddnB
2eklA Structure of st1218 protein from sulfolobus tokodaii
31% identity, 77% coverage: 44:251/269 of query aligns to 68:289/312 of 2eklA
- active site: S100 (≠ Q75), R232 (= R197), D256 (= D220), E261 (= E225), H282 (= H244)
- binding nicotinamide-adenine-dinucleotide: I76 (≠ V52), S100 (≠ Q75), G148 (= G123), G150 (= G125), R151 (≠ N126), I152 (= I127), Y170 (≠ F144), D171 (= D145), I172 (= I146), L173 (vs. gap), H202 (= H167), V203 (≠ I168), T204 (≠ P169), I212 (≠ F177), T230 (= T195), S231 (≠ A196), D256 (= D220), G284 (≠ S246)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
27% identity, 85% coverage: 38:266/269 of query aligns to 59:316/334 of 3kb6B
- active site: S97 (≠ T76), R231 (= R197), D255 (= D220), E260 (vs. gap), H294 (= H244)
- binding lactic acid: S72 (≠ G51), V73 (= V52), G74 (= G53), Y96 (≠ Q75), R231 (= R197), H294 (= H244)
- binding nicotinamide-adenine-dinucleotide: V73 (= V52), Y96 (≠ Q75), V101 (≠ I80), G150 (= G125), R151 (≠ N126), I152 (= I127), D171 (= D145), V172 (≠ I146), P203 (= P169), T229 (= T195), A230 (= A196), R231 (= R197), H294 (= H244), A296 (≠ S246), Y297 (≠ S247)
Sites not aligning to the query:
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
28% identity, 78% coverage: 37:246/269 of query aligns to 59:291/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V52), T102 (= T84), G155 (= G123), G157 (= G125), R158 (≠ N126), T159 (≠ I127), D178 (= D145), P179 (vs. gap), Y180 (vs. gap), H210 (= H167), C211 (≠ I168), N212 (≠ P169), A238 (≠ T195), R240 (= R197), H289 (= H244), A291 (≠ S246)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
28% identity, 78% coverage: 37:246/269 of query aligns to 59:291/330 of 4lcjA
- active site: A98 (≠ Q75), R240 (= R197), D264 (= D220), E269 (= E225), H289 (= H244)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: I72 (≠ C50), G73 (= G51), S74 (≠ V52), G75 (= G53), R240 (= R197), H289 (= H244)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V52), T102 (= T84), I154 (= I122), G155 (= G123), G157 (= G125), R158 (≠ N126), T159 (≠ I127), D178 (= D145), Y180 (vs. gap), H210 (= H167), C211 (≠ I168), N212 (≠ P169), N214 (= N171), N217 (≠ T174), A238 (≠ T195), A239 (= A196), R240 (= R197), H289 (= H244)
Sites not aligning to the query:
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 60:314/331 of 1hl3A
- active site: S99 (≠ Q75), R241 (= R197), D265 (= D220), E270 (= E225), H290 (= H244)
- binding nicotinamide-adenine-dinucleotide: T103 (= T84), G158 (= G125), R159 (≠ N126), V160 (≠ I127), D179 (= D145), Y181 (vs. gap), H211 (= H167), C212 (≠ I168), G213 (≠ P169), N218 (≠ T174), T239 (= T195), A240 (= A196), R241 (= R197), D265 (= D220), H290 (= H244)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 60:314/331 of 1hkuA
- active site: S99 (≠ Q75), R241 (= R197), D265 (= D220), E270 (= E225), H290 (= H244)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ V52), T103 (= T84), G156 (= G123), G158 (= G125), R159 (≠ N126), V160 (≠ I127), Y178 (≠ F144), D179 (= D145), P180 (vs. gap), Y181 (vs. gap), C212 (≠ I168), N218 (≠ T174), T239 (= T195), A240 (= A196), R241 (= R197), H290 (= H244), W293 (≠ S247)
Sites not aligning to the query:
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 60:314/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 61:315/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (= T84), G157 (= G123), R160 (≠ N126), V161 (≠ I127), Y179 (≠ F144), D180 (= D145), P181 (vs. gap), Y182 (vs. gap), H212 (= H167), C213 (≠ I168), N219 (≠ T174), T240 (= T195), A241 (= A196), R242 (= R197), H291 (= H244), W294 (≠ S247)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 60:314/328 of 4u6sA
- active site: S99 (≠ Q75), R241 (= R197), D265 (= D220), E270 (= E225), H290 (= H244)
- binding nicotinamide-adenine-dinucleotide: T103 (= T84), G156 (= G123), G158 (= G125), R159 (≠ N126), V160 (≠ I127), Y178 (≠ F144), D179 (= D145), P180 (vs. gap), Y181 (vs. gap), H211 (= H167), C212 (≠ I168), G213 (≠ P169), N218 (≠ T174), T239 (= T195), A240 (= A196), R241 (= R197), H290 (= H244), W293 (≠ S247)
- binding 3-phenylpyruvic acid: I73 (≠ C50), G74 (= G51), S75 (≠ V52), G76 (= G53), R241 (= R197), W293 (≠ S247), M302 (≠ L256)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 60:314/328 of 4u6qA
- active site: S99 (≠ Q75), R241 (= R197), D265 (= D220), E270 (= E225), H290 (= H244)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: I73 (≠ C50), G74 (= G51), S75 (≠ V52), G76 (= G53), R241 (= R197), H290 (= H244), W293 (≠ S247), M302 (≠ L256)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ V52), T103 (= T84), G156 (= G123), R159 (≠ N126), V160 (≠ I127), Y178 (≠ F144), D179 (= D145), P180 (vs. gap), Y181 (vs. gap), H211 (= H167), C212 (≠ I168), G213 (≠ P169), N218 (≠ T174), T239 (= T195), A240 (= A196), R241 (= R197), H290 (= H244), W293 (≠ S247)
Sites not aligning to the query:
4lceA Ctbp1 in complex with substrate mtob (see paper)
27% identity, 86% coverage: 37:267/269 of query aligns to 59:313/327 of 4lceA
- active site: S98 (≠ Q75), R240 (= R197), D264 (= D220), E269 (= E225), H289 (= H244)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ K49), G73 (= G51), S74 (≠ V52), G75 (= G53), R240 (= R197), H289 (= H244), W292 (≠ S247)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V52), T102 (= T84), G155 (= G123), G157 (= G125), R158 (≠ N126), V159 (≠ I127), Y177 (≠ F144), D178 (= D145), P179 (vs. gap), Y180 (vs. gap), H210 (= H167), C211 (≠ I168), N214 (= N171), N217 (≠ T174), T238 (= T195), A239 (= A196), R240 (= R197), W292 (≠ S247)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
29% identity, 77% coverage: 42:249/269 of query aligns to 62:283/304 of 1wwkA
- active site: S96 (≠ Q75), R230 (= R197), D254 (= D220), E259 (= E225), H278 (= H244)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ T84), G146 (≠ Q124), F147 (≠ G125), G148 (≠ N126), R149 (≠ I127), I150 (≠ G128), Y168 (≠ F144), D169 (= D145), P170 (≠ I146), V201 (≠ I168), P202 (= P169), T207 (= T174), T228 (= T195), S229 (≠ A196), D254 (= D220), H278 (= H244), G280 (≠ S246)
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)
27% identity, 86% coverage: 37:267/269 of query aligns to 74:328/430 of Q9Z2F5
- S89 (≠ V52) binding
- IGLGRV 169:174 (≠ IGQGNI 122:127) binding
- G172 (= G125) mutation to E: Loss dimerization and of NAD binding.
- D193 (= D145) binding
- 226:232 (vs. 168:174, 43% identical) binding
- TAR 253:255 (= TAR 195:197) binding
- D279 (= D220) 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)
27% identity, 86% coverage: 37:267/269 of query aligns to 85:339/440 of Q13363
- C134 (≠ Y90) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ R94) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ Y97) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ YN 97:98) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ W106) 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 (≠ F113) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G123) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G125) 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 (= G128) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (= D145) 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 (= R197) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D220) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E225) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H244) 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)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
28% identity, 78% coverage: 37:246/269 of query aligns to 91:323/445 of P56545
- IGFGRT 186:191 (≠ IGQGNI 122:127) binding
- D210 (= D145) binding
- 243:249 (vs. 168:174, 43% identical) binding
- AAR 270:272 (≠ TAR 195:197) binding
- D296 (= D220) binding
Sites not aligning to the query:
6ttbA Crystal structure of NAD-dependent formate dehydrogenase from staphylococcus aureus in complex with NAD
32% identity, 69% coverage: 42:226/269 of query aligns to 77:274/331 of 6ttbA
- binding nicotinamide-adenine-dinucleotide: V87 (= V52), N111 (≠ Q75), V115 (≠ T84), F162 (≠ I122), G165 (= G125), R166 (≠ N126), I167 (= I127), Y185 (≠ D145), D186 (≠ I146), P187 (≠ A147), H214 (= H167), A215 (≠ I168), P216 (= P169), T221 (= T174), T242 (= T195), A243 (= A196), R244 (= R197)
Sites not aligning to the query:
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
27% identity, 76% coverage: 44:248/269 of query aligns to 56:273/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ N126), Y160 (≠ F144), D161 (= D145), P162 (≠ I146), I164 (≠ V148), L179 (= L154), T193 (≠ I168), P194 (= P169), S198 (≠ E173), L202 (≠ F177)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
26% identity, 77% coverage: 44:251/269 of query aligns to 64:284/297 of 6rj3A
Query Sequence
>WP_012466797.1 NCBI__GCF_000020465.1:WP_012466797.1
MKYWKNTATLDHLMPELLETVPSEYAEIAVIGSKPIDLKLMPCLKGIFKCGVGTDNVPFK
EAEQRGVVIGLPSDQTRRYIFEETANFAVYLIFRMLYNDLGTLDPWKKSSRLFLGNKKVL
VIGQGNIGKLVTAKLEPFVEVLTFDIAVNKEDELRSLISLADVVTLHIPLNEETHNFIDV
EKMAWMKDGAAIVNTARGPIVNEDALHEEILSGRLHAAFDVFWKEPYQGKLMKYDPESFF
MTPHVSSNCEDFLIGLAQDCREFVKSLYC
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