SitesBLAST
Comparing H281DRAFT_05357 FitnessBrowser__Burk376:H281DRAFT_05357 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)
Q14894 Ketimine reductase mu-crystallin; NADP-regulated thyroid-hormone-binding protein; EC 1.5.1.25 from Homo sapiens (Human) (see paper)
27% identity, 88% coverage: 39:311/311 of query aligns to 42:313/314 of Q14894
2i99A Crystal structure of human mu_crystallin at 2.6 angstrom (see paper)
27% identity, 88% coverage: 39:311/311 of query aligns to 41:312/312 of 2i99A
- active site: G59 (≠ L56), S228 (≠ F225)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D81 (≠ G76), S90 (≠ T84), H91 (≠ I85), R118 (= R112), T119 (= T113), G142 (= G136), A143 (≠ T137), G144 (= G138), V145 (≠ T139), Q146 (= Q140), N167 (≠ G161), R168 (≠ S162), T169 (≠ A163), V203 (≠ L201), T204 (= T202), L205 (≠ T203), A206 (≠ S204), V225 (= V222), G226 (= G223), S291 (= S290), L292 (≠ V291), G293 (= G292)
4bv9A Crystal structure of the NADPH form of mouse mu-crystallin. (see paper)
27% identity, 86% coverage: 39:307/311 of query aligns to 40:300/303 of 4bv9A
- active site: G58 (≠ L56), S220 (≠ F225)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S82 (≠ T84), H83 (≠ I85), T111 (= T113), G134 (= G136), G136 (= G138), V137 (≠ T139), Q138 (= Q140), N159 (≠ G161), R160 (≠ S162), T161 (≠ A163), V195 (≠ L201), T196 (= T202), M197 (≠ T203), A198 (≠ S204), V217 (= V222), G218 (= G223), S283 (= S290), L284 (≠ V291), G285 (= G292)
- binding pyruvic acid: R45 (= R44), M60 (= M58), K73 (= K69), R110 (= R112)
4bvaA Crystal structure of the NADPH-t3 form of mouse mu-crystallin. (see paper)
27% identity, 88% coverage: 39:311/311 of query aligns to 41:303/303 of 4bvaA
- active site: G59 (≠ L56), S219 (≠ F225)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T106 (= T109), R109 (= R112), T110 (= T113), G135 (= G138), V136 (≠ T139), Q137 (= Q140), N158 (≠ G161), R159 (≠ S162), T160 (≠ A163), N163 (≠ R166), V194 (≠ L201), T195 (= T202), M196 (≠ T203), A197 (≠ S204), V216 (= V222), S282 (= S290), L283 (≠ V291), G284 (= G292)
- binding 3,5,3'triiodothyronine: R46 (= R44), F57 (≠ I54), G59 (≠ L56), V76 (= V71), F78 (≠ V73), S219 (≠ F225), R220 (≠ T226), W223 (≠ M229), E247 (= E253)
6t3eB Structure of thermococcus litoralis delta(1)-pyrroline-2-carboxylate reductase in complex with nadh and l-proline (see paper)
26% identity, 94% coverage: 16:306/311 of query aligns to 11:312/325 of 6t3eB
- binding 1,4-dihydronicotinamide adenine dinucleotide: S82 (≠ T84), T111 (= T113), G136 (= G138), V137 (≠ T139), Q138 (= Q140), D159 (≠ G161), I160 (≠ S162), A199 (≠ L201), T200 (= T202), T201 (= T203), A202 (≠ S204), V206 (= V208), V221 (= V222), G222 (= G223), W223 (≠ A224), S296 (= S290), V297 (= V291), G298 (= G292)
- binding proline: R39 (= R44), M54 (= M58), K67 (= K69), R110 (= R112)
1omoA Alanine dehydrogenase dimer w/bound NAD (archaeal) (see paper)
28% identity, 91% coverage: 24:306/311 of query aligns to 21:306/320 of 1omoA
- active site: R52 (≠ L56), D219 (≠ F225)
- binding nicotinamide-adenine-dinucleotide: T109 (= T113), G134 (= G138), T135 (= T139), Q136 (= Q140), Y156 (vs. gap), D157 (vs. gap), V158 (= V159), R159 (≠ K160), T195 (= T202), P196 (≠ T203), G217 (= G223), D219 (≠ F225), K223 (≠ M229), S290 (= S290), T291 (≠ V291), G292 (= G292)
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)
28% identity, 91% coverage: 24:306/311 of query aligns to 21:306/322 of O28608
Q9FLY0 Protein SAR DEFICIENT 4; Ornithine cyclodeaminase-like protein; AtOCD from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 77% coverage: 69:306/311 of query aligns to 71:319/325 of Q9FLY0
- G89 (= G87) mutation to E: In sard4-3; compromises systemic acquired resistance (SAR).
- G138 (= G136) mutation to D: In sard4-4; compromises systemic acquired resistance (SAR).
- S205 (≠ I199) mutation to N: In sard4-1; compromises systemic acquired resistance (SAR).
5yu4A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
36% identity, 46% coverage: 39:181/311 of query aligns to 38:192/344 of 5yu4A
- binding 2,4-diaminobutyric acid: E63 (≠ L56), K77 (= K69), R121 (= R112)
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ V73), T93 (= T84), I94 (= I85), R121 (= R112), T122 (= T113), G147 (= G138), A148 (≠ T139), Q149 (= Q140), D170 (≠ G161), T171 (≠ S162), H175 (≠ R166)
Sites not aligning to the query:
- binding 2,4-diaminobutyric acid: 302, 303
- binding nicotinamide-adenine-dinucleotide: 208, 209, 210, 211, 218, 233, 235, 301, 302, 303
5yu3A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
36% identity, 46% coverage: 39:181/311 of query aligns to 38:192/344 of 5yu3A
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ V73), T93 (= T84), I94 (= I85), T122 (= T113), G147 (= G138), A148 (≠ T139), Q149 (= Q140), D170 (≠ G161), T171 (≠ S162)
- binding proline: M65 (= M58), K77 (= K69), R121 (= R112)
Sites not aligning to the query:
5gzlA Cyclodeaminase_pa
36% identity, 46% coverage: 39:181/311 of query aligns to 42:196/357 of 5gzlA
- binding lysine: G55 (= G52), E57 (vs. gap), I65 (= I54), E67 (≠ L56)
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ V73), T97 (= T84), I98 (= I85), T126 (= T113), G151 (= G138), A152 (≠ T139), Q153 (= Q140), D174 (≠ G161), T175 (≠ S162), H179 (≠ R166)
Sites not aligning to the query:
- binding lysine: 240, 267, 268
- binding nicotinamide-adenine-dinucleotide: 212, 213, 214, 222, 237, 238, 239, 240, 244, 305, 306, 307
5gziA Cyclodeaminase_pa
36% identity, 46% coverage: 39:181/311 of query aligns to 42:196/354 of 5gziA
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ V73), T97 (= T84), R125 (= R112), T126 (= T113), G151 (= G138), A152 (≠ T139), Q153 (= Q140), D174 (≠ G161), T175 (≠ S162), H179 (≠ R166)
- binding (2S)-piperidine-2-carboxylic acid: R53 (≠ N50), K81 (= K69), R125 (= R112)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 212, 213, 214, 215, 237, 238, 239, 305, 306, 307
- binding (2S)-piperidine-2-carboxylic acid: 239, 306, 307
7cxuB Crystal structure of cmnk in complex with NAD+ (see paper)
27% identity, 57% coverage: 69:246/311 of query aligns to 75:246/327 of 7cxuB
- binding nicotinamide-adenine-dinucleotide: R90 (≠ T84), R118 (= R112), G144 (= G138), A145 (≠ T139), Q146 (= Q140), D168 (≠ G161), T169 (≠ S162), R173 (= R166), L204 (≠ V198), T205 (≠ I199), T206 (≠ A200), V226 (≠ I220)
Sites not aligning to the query:
1x7dA Crystal structure analysis of ornithine cyclodeaminase complexed with NAD and ornithine to 1.6 angstroms (see paper)
31% identity, 39% coverage: 21:141/311 of query aligns to 27:140/340 of 1x7dA
- active site: E55 (≠ L56)
- binding nicotinamide-adenine-dinucleotide: T83 (= T84), R111 (= R112), T112 (= T113), G137 (= G138), A138 (≠ T139), Q139 (= Q140)
- binding L-ornithine: R44 (= R38), V53 (≠ I54), E55 (≠ L56), M57 (= M58), K68 (= K69), V70 (= V71), N71 (= N72), G72 (≠ V73), R111 (= R112)
Sites not aligning to the query:
- active site: 227
- binding nicotinamide-adenine-dinucleotide: 160, 161, 200, 201, 202, 209, 224, 225, 227, 231, 292, 293, 294
- binding L-ornithine: 227, 293
1u7hA Structure and a proposed mechanism for ornithine cyclodeaminase from pseudomonas putida (see paper)
31% identity, 39% coverage: 21:141/311 of query aligns to 27:140/341 of 1u7hA
Sites not aligning to the query:
- active site: 227
- binding nicotinamide-adenine-dinucleotide: 160, 161, 200, 201, 202, 209, 224, 225, 227, 231, 292, 293, 294
Q88H32 Ornithine cyclodeaminase; OCD; EC 4.3.1.12 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
31% identity, 39% coverage: 21:141/311 of query aligns to 28:141/350 of Q88H32
- R45 (= R38) binding
- K69 (= K69) binding
- T84 (= T84) binding
- R112 (= R112) binding ; binding
- AQ 139:140 (≠ TQ 139:140) binding
Sites not aligning to the query:
- 161 binding
- 202 binding
- 225:228 binding
- 228 binding
- 232 binding
- 293 binding
- 294 binding
- 331 binding
A1B8Z0 Iminosuccinate reductase; EC 1.4.1.- from Paracoccus denitrificans (strain Pd 1222) (see paper)
25% identity, 75% coverage: 75:306/311 of query aligns to 73:307/320 of A1B8Z0
6rqaB Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
25% identity, 75% coverage: 75:306/311 of query aligns to 75:309/322 of 6rqaB
- binding Tb-Xo4: N76 (≠ G76)
- binding nicotinamide-adenine-dinucleotide: T113 (= T113), G138 (= G138), Q140 (= Q140), P162 (≠ K160), H163 (≠ G161), I199 (≠ L201), T200 (= T202), S201 (≠ T203), S202 (= S204), M221 (≠ V222), G222 (= G223), D224 (≠ F225), K228 (≠ M229), G293 (≠ S290), T294 (≠ V291), G295 (= G292)
Sites not aligning to the query:
6rqaA Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
25% identity, 75% coverage: 75:306/311 of query aligns to 75:309/322 of 6rqaA
- binding nicotinamide-adenine-dinucleotide: H85 (≠ I85), T113 (= T113), G138 (= G138), H139 (≠ T139), Q140 (= Q140), N161 (≠ V159), P162 (≠ K160), H163 (≠ G161), M166 (≠ P164), I199 (≠ L201), T200 (= T202), S201 (≠ T203), S202 (= S204), M221 (≠ V222), G222 (= G223), D224 (≠ F225), K228 (≠ M229), G293 (≠ S290)
Query Sequence
>H281DRAFT_05357 FitnessBrowser__Burk376:H281DRAFT_05357
MTRPTTQIFDAAATARLTPYAALVDALKSASIEYAQQRIASPERLVVPLNQGGILLSMPA
TSPDLAIHKLVNVCPGNGSRGLPTIHGQVMAFDADTGETLFILDGPTVTGRRTAAMSMLG
VRTFAAAAPREFVLIGTGTQALNHLEAIGELYPDARVWVKGSAPARAEAFCAANRGKAFE
VRPLADPDAALPESVDTVIALTTSRQPVYQEAPRASRLVIGVGAFTPEMVEIGARTIADS
ALFVDDEAGAKHEAGDFIQAGVDWSDVRGIAAVLDNSMPLPARTPIVFKSVGCAAWDLAA
CRVAREALGGG
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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