| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra033557 |
| Family | GT13 |
| Protein Properties | Length: 896 Molecular Weight: 101897 Isoelectric Point: 6.8211 |
| Chromosome | Chromosome/Scaffold: 06 Start: 26242459 End: 26248389 |
| Description | calcium-dependent protein kinase 26 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT13 | 22 | 411 | 0 |
| IQMRLFQTQSQYADRLSSALESENHCTSQLRSLIDQVSTKQSRILALEGKGIAKLTQGGQGPLAAVVIMACSRADYLERTVNSVLKYQSPIASKYPLFIS QDGSNQAVKSKSLSYTQLTYMQHLDFEPVITERPGELIAYYKIARHYKWALDQLFYKHKFSRVIILEDFFDYFEAAARLMDRDGTIMAASSWNDNGQKQF VHDPYALYRSDFFPGLGWMLKRSTWDELSPKWPKAYPYIRLSISMAMRLKENHKGRQFVRPEVCRTYNFGEHGSSLGQFFSQYLEPIKLNDVKVDWNAMD LGYLTEGNYTKYFSGLVRQARPIQGSDLVLKAQNINGDVRIRYEDQAEFERIAGEFGIFEEWKDGVPRTAYKGIVVFRIQTTRRVFLHKR | |||
| Full Sequence |
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| Protein Sequence Length: 896 Download |
| MARVPCDLRF LLIPAAFMFI YIQMRLFQTQ SQYADRLSSA LESENHCTSQ LRSLIDQVST 60 KQSRILALEG KGIAKLTQGG QGPLAAVVIM ACSRADYLER TVNSVLKYQS PIASKYPLFI 120 SQDGSNQAVK SKSLSYTQLT YMQHLDFEPV ITERPGELIA YYKIARHYKW ALDQLFYKHK 180 FSRVIILEDF FDYFEAAARL MDRDGTIMAA SSWNDNGQKQ FVHDPYALYR SDFFPGLGWM 240 LKRSTWDELS PKWPKAYPYI RLSISMAMRL KENHKGRQFV RPEVCRTYNF GEHGSSLGQF 300 FSQYLEPIKL NDVKVDWNAM DLGYLTEGNY TKYFSGLVRQ ARPIQGSDLV LKAQNINGDV 360 RIRYEDQAEF ERIAGEFGIF EEWKDGVPRT AYKGIVVFRI QTTRRVFLHK REDTMKHSGG 420 NQACFVLGQK TPSIRDLYSL GHKLGQGQFG TTYMCREIST GREYACKSIT KRKLISKEDV 480 EDVRREIQIM HHLAGYKNIV TIKGAYEDPL YVHIVMELCS GGELFDRIIQ RGHYSERKAA 540 ELIKIIVGVV EACHSLGVMH RDLKPENFLL VNKDDDFSLK AIDFGLSVFF KPGQIFEDVV 600 GSPYYVAPEV LLKHYGPEAD VWTAGVILYI LVSGVPPFWA ETQQGIFDAV LKGHIDFDSD 660 PWPLISDSAK DLIRGMLCSR PSERLTAHQV LRHPWICENG VAPDRALDPA VLSRLKQFSA 720 MNKLKQMALR VIAESLSEEE IAGLKEMFKA MDTDNSGAIT FDELKAGLRR YGSTLKDTEI 780 RDLMEAADID KSGTIDYGEF IAATIHLNKL DREEHLLSAF SYFDKDGSGY ITIDELQQAC 840 AEQGMSDVFL EDVIKEVDQD NDGRIDYGEF VAMMQKGIAG RTMRQSINMS LRKNA* 900 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd05123 | STKc_AGC | 1.0e-60 | 444 | 695 | 264 | + Catalytic domain of AGC family Protein Serine/Threonine Kinases. Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase (PI3K). Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. | ||
| pfam00069 | Pkinase | 2.0e-86 | 438 | 696 | 265 | + Protein kinase domain. | ||
| smart00220 | S_TKc | 3.0e-92 | 438 | 696 | 261 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
| cd02514 | GT13_GLCNAC-TI | 2.0e-156 | 85 | 408 | 336 | + GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13. | ||
| pfam03071 | GNT-I | 0 | 13 | 408 | 430 | + GNT-I family. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localised to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus. | ||
| Gene Ontology | |
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| GO Term | Description |
| GO:0000139 | Golgi membrane |
| GO:0003827 | alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity |
| GO:0004672 | protein kinase activity |
| GO:0005524 | ATP binding |
| GO:0006468 | protein phosphorylation |
| Annotations - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAC49405.1 | 0 | 415 | 892 | 1 | 481 | calcium dependent protein kinase [Vigna radiata] |
| GenBank | AAL68972.1 | 0 | 410 | 892 | 67 | 552 | calmodulin-like-domain protein kinase CPK2 [Cucurbita maxima] |
| GenBank | ABY55551.1 | 0 | 414 | 892 | 66 | 547 | calcium-dependent protein kinase [Swainsona canescens] |
| Swiss-Prot | Q9SZM3 | 0 | 415 | 895 | 1 | 481 | CDPKQ_ARATH RecName: Full=Calcium-dependent protein kinase 26 |
| RefSeq | XP_002313574.1 | 0 | 410 | 892 | 69 | 554 | calcium dependent protein kinase 5 [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ncg_A | 0 | 438 | 875 | 24 | 480 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 3mwu_A | 0 | 438 | 875 | 24 | 480 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 3igo_A | 0 | 438 | 875 | 24 | 480 | A Chain A, Crystal Structure Of Cryptosporidium Parvum Cdpk1, Cgd3_920 |
| PDB | 3hzt_A | 0 | 434 | 876 | 2 | 459 | A Chain A, Crystal Structure Of Toxoplasma Gondii Cdpk3, Tgme49_105860 |
| PDB | 3v5t_A | 0 | 415 | 876 | 6 | 480 | A Chain A, Crystal Structure Of Toxoplasma Gondii Cdpk3, Tgme49_105860 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO780321 | 394 | 502 | 892 | 0 |
| HO797287 | 491 | 409 | 893 | 0 |
| HO450185 | 462 | 426 | 884 | 0 |
| BU103685 | 351 | 426 | 776 | 0 |
| HO780321 | 66 | 440 | 505 | 3e-26 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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