SitesBLAST
Comparing RR42_RS03960 FitnessBrowser__Cup4G11:RR42_RS03960 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 19 hits to proteins with known functional sites (download)
Q88H32 Ornithine cyclodeaminase; OCD; EC 4.3.1.12 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
61% identity, 93% coverage: 6:338/358 of query aligns to 1:334/350 of Q88H32
- R45 (= R50) binding
- K69 (= K74) binding
- T84 (= T89) binding
- R112 (= R117) binding ; binding
- AQ 139:140 (= AQ 144:145) binding
- D161 (= D166) binding
- T202 (= T207) binding
- VGGD 225:228 (= VGGD 230:233) binding
- D228 (= D233) binding
- K232 (= K237) binding
- S293 (= S298) binding
- V294 (= V299) binding
- K331 (≠ R335) binding
1x7dA Crystal structure analysis of ornithine cyclodeaminase complexed with NAD and ornithine to 1.6 angstroms (see paper)
61% identity, 93% coverage: 7:338/358 of query aligns to 1:333/340 of 1x7dA
- active site: E55 (= E61), D227 (= D233)
- binding nicotinamide-adenine-dinucleotide: T83 (= T89), R111 (= R117), T112 (= T118), G137 (= G143), A138 (= A144), Q139 (= Q145), D160 (= D166), T161 (≠ I167), V200 (≠ I206), T201 (= T207), A202 (= A208), I209 (= I215), V224 (= V230), G225 (= G231), D227 (= D233), K231 (= K237), S292 (= S298), V293 (= V299), G294 (= G300)
- binding L-ornithine: R44 (= R50), V53 (= V59), E55 (= E61), M57 (= M63), K68 (= K74), V70 (= V76), N71 (= N77), G72 (= G78), R111 (= R117), D227 (= D233), V293 (= V299)
1u7hA Structure and a proposed mechanism for ornithine cyclodeaminase from pseudomonas putida (see paper)
61% identity, 93% coverage: 7:338/358 of query aligns to 1:333/341 of 1u7hA
- active site: E55 (= E61), D227 (= D233)
- binding nicotinamide-adenine-dinucleotide: T83 (= T89), R111 (= R117), T112 (= T118), G137 (= G143), A138 (= A144), Q139 (= Q145), D160 (= D166), T161 (≠ I167), V200 (≠ I206), T201 (= T207), A202 (= A208), I209 (= I215), V224 (= V230), G225 (= G231), D227 (= D233), K231 (= K237), S292 (= S298), V293 (= V299), G294 (= G300)
1omoA Alanine dehydrogenase dimer w/bound NAD (archaeal) (see paper)
32% identity, 72% coverage: 72:327/358 of query aligns to 63:319/320 of 1omoA
- active site: D219 (= D233)
- binding nicotinamide-adenine-dinucleotide: T109 (= T118), G134 (= G143), T135 (≠ A144), Q136 (= Q145), Y156 (= Y165), D157 (= D166), V158 (≠ I167), R159 (≠ D168), T195 (≠ D209), P196 (≠ K210), G217 (= G231), D219 (= D233), K223 (= K237), S290 (= S298), T291 (≠ V299), G292 (= G300)
Sites not aligning to the query:
O28608 Alanine dehydrogenase; AlaDH; EC 1.4.1.1 from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) (see paper)
32% identity, 72% coverage: 72:327/358 of query aligns to 63:319/322 of O28608
6t3eB Structure of thermococcus litoralis delta(1)-pyrroline-2-carboxylate reductase in complex with nadh and l-proline (see paper)
30% identity, 76% coverage: 57:327/358 of query aligns to 48:325/325 of 6t3eB
- binding 1,4-dihydronicotinamide adenine dinucleotide: S82 (≠ T89), T111 (= T118), G136 (= G143), V137 (≠ A144), Q138 (= Q145), D159 (= D166), I160 (= I167), A199 (= A208), T200 (≠ D209), T201 (≠ K210), A202 (≠ T211), V206 (≠ I215), V221 (= V230), G222 (= G231), W223 (≠ G232), S296 (= S298), V297 (= V299), G298 (= G300)
- binding proline: M54 (= M63), K67 (= K74), R110 (= R117)
Sites not aligning to the query:
5gzlA Cyclodeaminase_pa
36% identity, 85% coverage: 53:356/358 of query aligns to 59:356/357 of 5gzlA
- binding lysine: I65 (≠ V59), E67 (= E61), D240 (= D233), R267 (≠ I260), E268 (= E261)
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G78), T97 (= T89), I98 (≠ V90), T126 (= T118), G151 (= G143), A152 (= A144), Q153 (= Q145), D174 (= D166), T175 (≠ I167), H179 (≠ A171), A212 (≠ I206), T213 (= T207), S214 (≠ A208), V222 (≠ L216), V237 (= V230), G238 (= G231), A239 (≠ G232), D240 (= D233), K244 (= K237), S305 (= S298), T306 (≠ V299), G307 (= G300)
Sites not aligning to the query:
5gziA Cyclodeaminase_pa
35% identity, 84% coverage: 53:354/358 of query aligns to 59:354/354 of 5gziA
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G78), T97 (= T89), R125 (= R117), T126 (= T118), G151 (= G143), A152 (= A144), Q153 (= Q145), D174 (= D166), T175 (≠ I167), H179 (≠ A171), A212 (≠ I206), T213 (= T207), S214 (≠ A208), V215 (≠ D209), V237 (= V230), G238 (= G231), A239 (≠ G232), S305 (= S298), T306 (≠ V299), G307 (= G300)
- binding (2S)-piperidine-2-carboxylic acid: K81 (= K74), R125 (= R117), A239 (≠ G232), T306 (≠ V299), G307 (= G300)
Sites not aligning to the query:
5yu4A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
35% identity, 80% coverage: 53:338/358 of query aligns to 55:341/344 of 5yu4A
- binding 2,4-diaminobutyric acid: E63 (= E61), K77 (= K74), R121 (= R117), T302 (≠ V299), G303 (= G300)
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G78), T93 (= T89), I94 (≠ V90), R121 (= R117), T122 (= T118), G147 (= G143), A148 (= A144), Q149 (= Q145), D170 (= D166), T171 (≠ I167), H175 (≠ A171), A208 (≠ I206), T209 (= T207), S210 (≠ A208), V211 (≠ D209), V218 (≠ L216), V233 (= V230), A235 (≠ G232), S301 (= S298), T302 (≠ V299), G303 (= G300)
5yu3A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
35% identity, 80% coverage: 53:338/358 of query aligns to 55:341/344 of 5yu3A
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G78), T93 (= T89), I94 (≠ V90), T122 (= T118), G147 (= G143), A148 (= A144), Q149 (= Q145), D170 (= D166), T171 (≠ I167), A208 (≠ I206), T209 (= T207), S210 (≠ A208), V211 (≠ D209), V233 (= V230), A235 (≠ G232), S301 (= S298), T302 (≠ V299), G303 (= G300)
- binding proline: M65 (= M63), K77 (= K74), R121 (= R117)
4bv9A Crystal structure of the NADPH form of mouse mu-crystallin. (see paper)
33% identity, 63% coverage: 87:313/358 of query aligns to 80:298/303 of 4bv9A
- active site: S220 (≠ D233)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S82 (≠ T89), H83 (≠ V90), T111 (= T118), G134 (= G141), G136 (= G143), V137 (≠ A144), Q138 (= Q145), N159 (≠ D166), R160 (≠ I167), T161 (≠ D168), V195 (≠ I206), T196 (= T207), M197 (≠ A208), A198 (≠ T211), V217 (= V230), G218 (= G231), S283 (= S298), L284 (≠ V299), G285 (= G300)
- binding pyruvic acid: R110 (= R117)
Sites not aligning to the query:
4bvaA Crystal structure of the NADPH-t3 form of mouse mu-crystallin. (see paper)
34% identity, 61% coverage: 95:313/358 of query aligns to 87:297/303 of 4bvaA
- active site: S219 (≠ D233)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T106 (= T114), R109 (= R117), T110 (= T118), G135 (= G143), V136 (≠ A144), Q137 (= Q145), N158 (≠ D166), R159 (≠ I167), T160 (≠ D168), N163 (≠ A171), V194 (≠ I206), T195 (= T207), M196 (≠ A208), A197 (≠ T211), V216 (= V230), S282 (= S298), L283 (≠ V299), G284 (= G300)
- binding 3,5,3'triiodothyronine: S219 (≠ D233), R220 (≠ C234), W223 (≠ K237), E247 (= E261)
Sites not aligning to the query:
Q14894 Ketimine reductase mu-crystallin; NADP-regulated thyroid-hormone-binding protein; EC 1.5.1.25 from Homo sapiens (Human) (see paper)
31% identity, 72% coverage: 58:313/358 of query aligns to 57:307/314 of Q14894
2i99A Crystal structure of human mu_crystallin at 2.6 angstrom (see paper)
31% identity, 72% coverage: 58:313/358 of query aligns to 56:306/312 of 2i99A
- active site: G59 (≠ E61), S228 (≠ D233)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D81 (vs. gap), S90 (≠ T89), H91 (≠ V90), R118 (= R117), T119 (= T118), G142 (= G141), A143 (≠ N142), G144 (= G143), V145 (≠ A144), Q146 (= Q145), N167 (≠ D166), R168 (≠ I167), T169 (≠ D168), V203 (≠ I206), T204 (= T207), L205 (≠ A208), A206 (≠ T211), V225 (= V230), G226 (= G231), S291 (= S298), L292 (≠ V299), G293 (= G300)
A1B8Z0 Iminosuccinate reductase; EC 1.4.1.- from Paracoccus denitrificans (strain Pd 1222) (see paper)
33% identity, 59% coverage: 111:322/358 of query aligns to 104:313/320 of A1B8Z0
6rqaB Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
34% identity, 54% coverage: 111:305/358 of query aligns to 106:300/322 of 6rqaB
- binding nicotinamide-adenine-dinucleotide: T113 (= T118), G138 (= G143), Q140 (= Q145), P162 (≠ I167), H163 (≠ D168), I199 (= I206), T200 (= T207), S201 (≠ A208), S202 (≠ T211), M221 (≠ V230), G222 (= G231), D224 (= D233), K228 (= K237), G293 (≠ S298), T294 (≠ V299), G295 (= G300)
Sites not aligning to the query:
6rqaA Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
34% identity, 54% coverage: 111:305/358 of query aligns to 106:300/322 of 6rqaA
- binding nicotinamide-adenine-dinucleotide: T113 (= T118), G138 (= G143), H139 (≠ A144), Q140 (= Q145), N161 (≠ D166), P162 (≠ I167), H163 (≠ D168), M166 (≠ A171), I199 (= I206), T200 (= T207), S201 (≠ A208), S202 (≠ T211), M221 (≠ V230), G222 (= G231), D224 (= D233), K228 (= K237), G293 (≠ S298)
Sites not aligning to the query:
Q9FLY0 Protein SAR DEFICIENT 4; Ornithine cyclodeaminase-like protein; AtOCD from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 67% coverage: 74:313/358 of query aligns to 71:318/325 of Q9FLY0
- G89 (≠ A92) mutation to E: In sard4-3; compromises systemic acquired resistance (SAR).
- G138 (= G141) mutation to D: In sard4-4; compromises systemic acquired resistance (SAR).
- S205 (= S204) mutation to N: In sard4-1; compromises systemic acquired resistance (SAR).
7cxuB Crystal structure of cmnk in complex with NAD+ (see paper)
23% identity, 72% coverage: 71:329/358 of query aligns to 72:326/327 of 7cxuB
- binding nicotinamide-adenine-dinucleotide: R90 (≠ T89), R118 (= R117), G144 (= G143), A145 (= A144), Q146 (= Q145), D168 (= D166), T169 (≠ I167), R173 (≠ A171), L204 (≠ I206), T205 (= T207), T206 (≠ K210), V226 (= V230), F296 (≠ V299)
Query Sequence
>RR42_RS03960 FitnessBrowser__Cup4G11:RR42_RS03960
MKEIAMTRFLDAADVAALVRATGVANTIAQMAHHIRQDFVRWEAFDKSARLATHSVDGVI
ELMPVSDAVQYAFKYVNGHPRNAQNAMPTVMAFGVLAEVASGFPLLLCDLTLATALRTAA
TSALAAQVMARPGAATLALIGNGAQAEFQALAFHAMVGIREIRAYDIDPAATARLARNLQ
GVPGLKVAAVDSVRTAVQGADIISTITADKTRATILTPDLVAPGVHINAVGGDCPGKTEL
HPQILRQARIVVEYAPQTRIEGEIQQLPADTPVTELWEILSGRVAGRTETGQVTVFDSVG
FALEDYSALRWLHAAAHAQHRGSHVELVATPPDPRNLYGWMMDAGAPQPVREPLAALA
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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