| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra004626 |
| Family | AA7 |
| Protein Properties | Length: 1477 Molecular Weight: 162733 Isoelectric Point: 8.2921 |
| Chromosome | Chromosome/Scaffold: 05 Start: 1119497 End: 1126238 |
| Description | Heat shock protein DnaJ with tetratricopeptide repeat |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 69 | 279 | 3.7e-24 |
| NRYQFPPLAILHPKSVSDISTVVRHILHLGSTSNLTVAARGHGHSLQGQALAHQGVVINMESLPSPDIKIYKGTQPYVDVSGGELWINILKETLKHGLSP KSWTDYLHLTVGGTLSNAGIGGQAVKHGPGGTLSNAGIGGQAFKHGPQINNVYQLEIVTGKGEAVTCSKKLNPELFHSVLGGLGQFGIITRARISLGPAP HMVKWIRVLYS | |||
| Full Sequence |
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| Protein Sequence Length: 1477 Download |
| MRLTSSLRFH RQNNKTFLRI FMILVLSCIP GRTNLCSNHS DTRSSLDSLD LEGYITFDDV 60 HNASKDFGNR YQFPPLAILH PKSVSDISTV VRHILHLGST SNLTVAARGH GHSLQGQALA 120 HQGVVINMES LPSPDIKIYK GTQPYVDVSG GELWINILKE TLKHGLSPKS WTDYLHLTVG 180 GTLSNAGIGG QAVKHGPGGT LSNAGIGGQA FKHGPQINNV YQLEIVTGKG EAVTCSKKLN 240 PELFHSVLGG LGQFGIITRA RISLGPAPHM VKWIRVLYSD FSTFSRDQEH LISKKKGFDF 300 VEGSVTINRT ELLNNWRSSF TPNDSTEASQ FKSDGKTLYC LEVVKYFNKE EANSMNQETE 360 KLLSELSYIP STLFSSVVPY IEFLDRVHLG EIKLRAKGLW EVPHPWLNLL VPKSSIFEFA 420 TEVFNNILTS NNNGPILIYP VNQSNIKLFF IWGMSPAAAV EIGSPPVEKV SPFFNPSSDS 480 AFFPESDQRT MDPSSSFHFG FEAGSGQKTK SRQKPRLVKV RKNGRKVKGA SFSGETPPGF 540 NPFAPPPSKG SLHMNGESPG DDKDKSFVFG AYGNSSGAKA TTTPGNAAVT PVSDEEEFST 600 PVGDFVFGSE STPCSESRRS DADSGKTGRE ACPDTCREPD IAQNGDGEAR DDDSEVNLFA 660 EMNKLNISEE AREYSNAPPA FIFGSSGKGD AECKGAACSF SSNGFGQSEN AADDQIPAFH 720 PGASNVNNFT STTFGTETSC DGFKVPLCDP SSLKSSLFPE MGRTPVHVRS KRSSKDQRSN 780 KVKGKKKQHE PNLCKDQASK GNESQEKLSS PGYSSPMDFS PYEGEKSSNQ FPTETPLHPS 840 HCSTNARDPP VFSAEDPGSI RMPQFSFSAS TSQGETSTKK LHAVKKYRRK VNNLFPKKNL 900 NTTMRNNQDK QEPASTSVMP GECEVWRLRG NQAYKNGDMR KAEECYTHGI NSSSPSDGSE 960 CSVKPLALCY GNRAAARISL GRLREAISDC DMAASLDPTY IKAYMRAANC YLVLGELGSA 1020 VQYFNKCMES SSSVCLDRRT TIESAEGLQQ AQRVADYTNR ASIFLEKRTP DGASDALVPI 1080 TNALSISSCS EKLLQMKAEA MLMIRRYKEV IELCENTLQT AERNFVSAGP NGIGSKHHSL 1140 MVWRWNMVSK SHFYLGNLEM SLDTLEKLQQ VGSSRNENQE ECRDSPASLV ATISELLRYK 1200 NAGNEAVRAG KYTEAVEQYT AALSRNVDSR PFAAICFCNR AAANQALVQI ADAIADCSLA 1260 MALDENYTKA VSRRATLHEM IRDYDQAASD LKRLISILVK QNGEKTKTSE TSADRSIIRK 1320 ELKQARQRLS VMEEKSKEGI ALDFFLIMGV KASDTAADIK KAYRKAALRH HPDKAAQILV 1380 RSESEGPWLK EILEEVHKGA DRLFKMIGEA YSVLSDPTKR SDYELEEEIR KAKASRESYR 1440 SRKAAEASTT SPYQTSPVRR YWRHSERTYR SSSPWW* 1500 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00226 | DnaJ | 4.0e-17 | 1343 | 1423 | 81 | + DnaJ domain. DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature. | ||
| pfam01565 | FAD_binding_4 | 1.0e-19 | 75 | 236 | 163 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
| COG0277 | GlcD | 3.0e-22 | 52 | 285 | 241 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam09265 | Cytokin-bind | 6.0e-84 | 268 | 444 | 181 | + Cytokinin dehydrogenase 1, FAD and cytokinin binding. Members of this family adopt an alpha+beta sandwich structure with an antiparallel beta-sheet, in a ferredoxin-like fold. They are predominantly found in plant cytokinin dehydrogenase 1, where they are capable of binding both FAD and cytokinin substrates. The substrate displays a 'plug-into-socket' binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin. | ||
| PLN02441 | PLN02441 | 0 | 11 | 444 | 443 | + cytokinin dehydrogenase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0009690 | cytokinin metabolic process |
| GO:0016491 | oxidoreductase activity |
| GO:0019139 | cytokinin dehydrogenase activity |
| GO:0031072 | heat shock protein binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAL32666.1 | 0 | 454 | 1476 | 1 | 1108 | Unknown protein [Arabidopsis thaliana] |
| DDBJ | BAD94294.1 | 0.0004 | 898 | 1020 | 258 | 376 | hypothetical protein [Arabidopsis thaliana] |
| DDBJ | BAD94294.1 | 0 | 918 | 1476 | 1 | 561 | hypothetical protein [Arabidopsis thaliana] |
| RefSeq | NP_850351.1 | 0 | 454 | 1476 | 1 | 1108 | DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_973659.1 | 0 | 454 | 1476 | 1 | 1077 | DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3s1d_A | 0 | 44 | 461 | 18 | 431 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3kjm_A | 0 | 44 | 461 | 18 | 431 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 2qpm_A | 0 | 44 | 461 | 18 | 431 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
| PDB | 3s1c_A | 0 | 44 | 461 | 18 | 431 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
| PDB | 3dq0_A | 0 | 44 | 461 | 18 | 431 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DY963441 | 320 | 53 | 370 | 0 |
| EG513940 | 285 | 823 | 1085 | 0 |
| DK542777 | 208 | 1269 | 1475 | 0 |
| ES837714 | 279 | 166 | 444 | 0 |
| EG513940 | 100 | 1188 | 1281 | 0.00005 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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