SitesBLAST
Comparing RR42_RS27330 FitnessBrowser__Cup4G11:RR42_RS27330 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4bvaA Crystal structure of the NADPH-t3 form of mouse mu-crystallin. (see paper)
34% identity, 71% coverage: 78:298/310 of query aligns to 86:297/303 of 4bvaA
- active site: S219 (= S212)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T106 (= T98), R109 (= R101), T110 (= T102), G135 (= G127), V136 (≠ T128), Q137 (= Q129), N158 (≠ D150), R159 (≠ P151), T160 (≠ Y152), N163 (≠ A155), V194 (≠ A187), T195 (≠ S188), M196 (≠ R189), A197 (≠ S190), V216 (≠ I209), S282 (= S283), L283 (≠ V284), G284 (= G285)
- binding 3,5,3'triiodothyronine: S219 (= S212), R220 (≠ L213), W223 (≠ T216), E247 (= E241)
Sites not aligning to the query:
4bv9A Crystal structure of the NADPH form of mouse mu-crystallin. (see paper)
34% identity, 71% coverage: 78:298/310 of query aligns to 87:298/303 of 4bv9A
- active site: S220 (= S212)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T111 (= T102), G134 (= G125), G136 (= G127), V137 (≠ T128), Q138 (= Q129), N159 (≠ D150), R160 (≠ P151), T161 (≠ Y152), V195 (≠ A187), T196 (≠ S188), M197 (≠ R189), A198 (≠ S190), V217 (≠ I209), G218 (= G210), S283 (= S283), L284 (≠ V284), G285 (= G285)
- binding pyruvic acid: R110 (= R101)
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)
33% identity, 71% coverage: 78:298/310 of query aligns to 96:307/314 of Q14894
- GAGVQA 143:148 (≠ GAGTQG 125:130) binding
- N168 (vs. gap) binding
- R169 (vs. gap) binding
2i99A Crystal structure of human mu_crystallin at 2.6 angstrom (see paper)
33% identity, 71% coverage: 78:298/310 of query aligns to 95:306/312 of 2i99A
- active site: S228 (= S212)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R118 (= R101), T119 (= T102), G142 (= G125), A143 (= A126), G144 (= G127), V145 (≠ T128), Q146 (= Q129), N167 (vs. gap), R168 (vs. gap), T169 (vs. gap), V203 (≠ A187), T204 (≠ S188), L205 (≠ R189), A206 (≠ S190), V225 (≠ I209), G226 (= G210), S291 (= S283), L292 (≠ V284), G293 (= G285)
Sites not aligning to the query:
6t3eB Structure of thermococcus litoralis delta(1)-pyrroline-2-carboxylate reductase in complex with nadh and l-proline (see paper)
26% identity, 97% coverage: 1:300/310 of query aligns to 1:313/325 of 6t3eB
- binding 1,4-dihydronicotinamide adenine dinucleotide: S82 (= S75), T111 (= T102), G136 (= G127), V137 (≠ T128), Q138 (= Q129), D159 (= D150), I160 (vs. gap), A199 (= A187), T200 (≠ S188), T201 (≠ R189), A202 (≠ S190), V206 (≠ L194), V221 (≠ I209), G222 (= G210), W223 (≠ S211), S296 (= S283), V297 (= V284), G298 (= G285)
- binding proline: R39 (= R39), M54 (≠ L52), K67 (= K65), R110 (= R101)
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, 96% coverage: 2:300/310 of query aligns to 4:307/322 of O28608
1omoA Alanine dehydrogenase dimer w/bound NAD (archaeal) (see paper)
28% identity, 96% coverage: 2:300/310 of query aligns to 4:307/320 of 1omoA
- active site: R52 (≠ S50), D219 (≠ S212)
- binding nicotinamide-adenine-dinucleotide: T109 (= T102), G134 (= G127), T135 (= T128), Q136 (= Q129), Y156 (≠ S149), D157 (= D150), V158 (≠ P151), R159 (≠ Y152), T195 (≠ S188), P196 (≠ R189), G217 (= G210), D219 (≠ S212), K223 (≠ T216), S290 (= S283), T291 (≠ V284), G292 (= G285)
6rqaB Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
32% identity, 70% coverage: 78:294/310 of query aligns to 89:304/322 of 6rqaB
- binding nicotinamide-adenine-dinucleotide: T113 (= T102), G138 (= G127), Q140 (= Q129), P162 (= P151), H163 (≠ Y152), I199 (≠ A187), T200 (≠ S188), S201 (≠ R189), S202 (= S190), M221 (≠ I209), G222 (= G210), D224 (≠ S212), K228 (≠ T216), G293 (≠ S283), T294 (≠ V284), G295 (= G285)
Sites not aligning to the query:
6rqaA Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
32% identity, 70% coverage: 78:294/310 of query aligns to 89:304/322 of 6rqaA
- binding nicotinamide-adenine-dinucleotide: T113 (= T102), G138 (= G127), H139 (≠ T128), Q140 (= Q129), N161 (≠ D150), P162 (= P151), H163 (≠ Y152), M166 (≠ R160), I199 (≠ A187), T200 (≠ S188), S201 (≠ R189), S202 (= S190), M221 (≠ I209), G222 (= G210), D224 (≠ S212), K228 (≠ T216), G293 (≠ S283)
Sites not aligning to the query:
A1B8Z0 Iminosuccinate reductase; EC 1.4.1.- from Paracoccus denitrificans (strain Pd 1222) (see paper)
32% identity, 70% coverage: 78:294/310 of query aligns to 87:302/320 of A1B8Z0
1x7dA Crystal structure analysis of ornithine cyclodeaminase complexed with NAD and ornithine to 1.6 angstroms (see paper)
34% identity, 72% coverage: 84:305/310 of query aligns to 94:314/340 of 1x7dA
- active site: D227 (≠ S212)
- binding nicotinamide-adenine-dinucleotide: R111 (= R101), T112 (= T102), G137 (= G127), A138 (≠ T128), Q139 (= Q129), D160 (vs. gap), T161 (≠ S149), V200 (= V185), T201 (= T186), A202 (= A187), I209 (≠ L194), V224 (≠ I209), G225 (= G210), D227 (≠ S212), K231 (≠ T216), S292 (= S283), V293 (= V284), G294 (= G285)
- binding L-ornithine: R111 (= R101), D227 (≠ S212), V293 (= V284)
Sites not aligning to the query:
1u7hA Structure and a proposed mechanism for ornithine cyclodeaminase from pseudomonas putida (see paper)
34% identity, 72% coverage: 84:305/310 of query aligns to 94:314/341 of 1u7hA
- active site: D227 (≠ S212)
- binding nicotinamide-adenine-dinucleotide: R111 (= R101), T112 (= T102), G137 (= G127), A138 (≠ T128), Q139 (= Q129), D160 (vs. gap), T161 (≠ S149), V200 (= V185), T201 (= T186), A202 (= A187), I209 (≠ L194), V224 (≠ I209), G225 (= G210), D227 (≠ S212), K231 (≠ T216), S292 (= S283), V293 (= V284), G294 (= G285)
Sites not aligning to the query:
Q88H32 Ornithine cyclodeaminase; OCD; EC 4.3.1.12 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
34% identity, 72% coverage: 84:305/310 of query aligns to 95:315/350 of Q88H32
- R112 (= R101) binding ; binding
- AQ 139:140 (≠ TQ 128:129) binding
- D161 (vs. gap) binding
- T202 (= T186) binding
- VGGD 225:228 (≠ IGSS 209:212) binding
- D228 (≠ S212) binding
- K232 (≠ T216) binding
- S293 (= S283) binding
- V294 (= V284) binding
Sites not aligning to the query:
- 45 binding
- 69 binding
- 84 binding
- 331 binding
Q9FLY0 Protein SAR DEFICIENT 4; Ornithine cyclodeaminase-like protein; AtOCD from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 82% coverage: 46:299/310 of query aligns to 69:319/325 of Q9FLY0
- G89 (= G72) mutation to E: In sard4-3; compromises systemic acquired resistance (SAR).
- G138 (= G125) mutation to D: In sard4-4; compromises systemic acquired resistance (SAR).
- S205 (≠ V185) mutation to N: In sard4-1; compromises systemic acquired resistance (SAR).
4mp6A Staphyloferrin b precursor biosynthetic enzyme sbnb bound to citrate and NAD+ (see paper)
28% identity, 73% coverage: 75:300/310 of query aligns to 94:321/334 of 4mp6A
- active site: M236 (≠ S212)
- binding nicotinamide-adenine-dinucleotide: R120 (= R101), T121 (= T102), G146 (= G127), L147 (≠ T128), I148 (≠ Q129), D170 (= D150), Q171 (≠ P151), C211 (≠ A187), T212 (≠ S188), V213 (≠ R189), I233 (= I209), G306 (= G285)
Sites not aligning to the query:
4mpdA Staphyloferrin b precursor biosynthetic enzyme sbnb bound a- ketoglutarate and NAD+ (see paper)
28% identity, 72% coverage: 77:300/310 of query aligns to 84:305/318 of 4mpdA
Sites not aligning to the query:
4m54A The structure of the staphyloferrin b precursor biosynthetic enzyme sbnb bound to n-(1-amino-1-carboxyl-2-ethyl)-glutamic acid and nadh (see paper)
27% identity, 73% coverage: 75:300/310 of query aligns to 89:297/310 of 4m54A
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)
32% identity, 70% coverage: 90:306/310 of query aligns to 110:321/344 of 5yu4A
- binding 2,4-diaminobutyric acid: R121 (= R101), T302 (≠ V284), G303 (= G285)
- binding nicotinamide-adenine-dinucleotide: R121 (= R101), T122 (= T102), G147 (= G127), A148 (≠ T128), Q149 (= Q129), D170 (= D150), T171 (≠ A153), H175 (≠ M157), A208 (= A187), T209 (≠ S188), S210 (≠ R189), V211 (vs. gap), V218 (≠ L194), V233 (≠ I209), A235 (≠ S211), S301 (= S283), T302 (≠ V284), G303 (= G285)
Sites not aligning to the query:
5yu3A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
32% identity, 70% coverage: 90:306/310 of query aligns to 110:321/344 of 5yu3A
- binding nicotinamide-adenine-dinucleotide: T122 (= T102), G147 (= G127), A148 (≠ T128), Q149 (= Q129), D170 (= D150), T171 (≠ A153), A208 (= A187), T209 (≠ S188), S210 (≠ R189), V211 (vs. gap), V233 (≠ I209), A235 (≠ S211), S301 (= S283), T302 (≠ V284), G303 (= G285)
- binding proline: R121 (= R101)
Sites not aligning to the query:
5gziA Cyclodeaminase_pa
32% identity, 70% coverage: 90:306/310 of query aligns to 114:325/354 of 5gziA
- binding nicotinamide-adenine-dinucleotide: R125 (= R101), T126 (= T102), G151 (= G127), A152 (≠ T128), Q153 (= Q129), D174 (= D150), T175 (≠ A153), H179 (≠ M157), A212 (= A187), T213 (≠ S188), S214 (≠ R189), V215 (vs. gap), V237 (≠ I209), G238 (= G210), A239 (≠ S211), S305 (= S283), T306 (≠ V284), G307 (= G285)
- binding (2S)-piperidine-2-carboxylic acid: R125 (= R101), A239 (≠ S211), T306 (≠ V284), G307 (= G285)
Sites not aligning to the query:
Query Sequence
>RR42_RS27330 FitnessBrowser__Cup4G11:RR42_RS27330
MLHITDEMIDRHVSPADAQQVMLDAFRSFGQGKAAMQERIRTEAGGVKLSTLGAVIPEQQ
VAGAKVYTTIKGQFSFVILIFSTEDGRPLASFDAGAITRLRTAACSVLAARHLARPGAEV
LALFGAGTQGVQHARQLAAALPLKRILLSDPYADAAMPERLARQCGIPVDLAEPDQAVAQ
ADIVVTASRSTTPLFSGHSLKPGAFVAAIGSSLPHTRELDDVALSRAARLVVEWRPQSMR
EAGDIVLADPAVLPADKVVELADVVTGSVKPRGNDTDILIYKSVGVGLEDVALAGFAYRQ
IEAAGEARAA
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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