| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os04g52640.1 |
| Family | CBM57 |
| Protein Properties | Length: 1023 Molecular Weight: 111596 Isoelectric Point: 6.2221 |
| Chromosome | Chromosome/Scaffold: 4 Start: 31317589 End: 31328040 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 413 | 583 | 6.1e-29 |
| FAVDCGSTRFISGSRNSSYQADATNLGAASYHVTEPLTWGISNVGKFMDTPNGTTIINNARQFQATLDSELFQTARMSPSSLRYYGIGLQNGNYTVSLQF AEFGFEDTESWKSRGRRVFDIYVQGERKEKDFDIKKEAGGKSYTAVKKDYIVSVTRNFVEIHLFWAGKGTC | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1023 Download |
| MALSVLLLLL AAVAQAQKAP TATTDRIEAE ALKAVFEKLD QKAEWNTTGD PCSGAATDST 60 DINDSSINPA IKCDCSDQNN TVCHITGLKI YDKDATGQIP GELRNLTHLT HLNLSHNFLV 120 GTIPSFIGEL AAMQYMTFGI NALSGSIPKE LGNLTNLVSL GFSSNNFSGS LPSELGSLFK 180 LEELFIDSAG LSGELPSSLS KLTRMKILWA SDNNFTGQIP DYIGSWNLTD LRFQGNSFQG 240 PLPANLSNLV QLTNLRIGDI ASGSSSSLAF ISNMTSLNTL ILRNCMVSDS LALIDFSKFA 300 SLTLLDLSFN NITGQVPQTL LNLNFLSYLF LGNNNLTGSL PSSKIRSLRN LDFSYNQLSG 360 NFPFWVSEED LQLNLVANNF MVNISNNSAL PSGLECLQQN TPCFLGSPHS ASFAVDCGST 420 RFISGSRNSS YQADATNLGA ASYHVTEPLT WGISNVGKFM DTPNGTTIIN NARQFQATLD 480 SELFQTARMS PSSLRYYGIG LQNGNYTVSL QFAEFGFEDT ESWKSRGRRV FDIYVQGERK 540 EKDFDIKKEA GGKSYTAVKK DYIVSVTRNF VEIHLFWAGK GTCCIPTQGY YGPTISALSL 600 SPNFTPTIGN VAEQNSSTSK TVVIVAVAIG VTILGLVALV GIFLWRKKRR KLSLEQQELY 660 SIVGRPNIFS YGELRSATEN FSSSNRLGEG GYGAVYKGKL MDGRIVAVKQ LSQTSHQGKK 720 QFATEIETIS RVQHRNLVKL YGCCLEGNNP LLVYEYMENG SLDKALFGTE KLHIGWPARF 780 EICLGIARGL AYLHEESSIR VVHRDIKASN VLLDANLNPK ISDFGLAKLY DDKMTHVSTK 840 VAGTFGYLAP EYAMRGHMTE KVDVFAFGVV LLETLAGRPN YDDVLEEDKI YIFEWVWRLY 900 ESERALDIVD PNLTEFNSEE VLRAIHVALL CTQGSPHRRP SMSRVVAMLT GDAEVGEVAA 960 KPSYITEWQI KGGGTTTTTT GSSSTSSSAA NGQWSSAPPP PRATSSPKMS SPFLSSVVDE 1020 GR* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00069 | Pkinase | 2.0e-52 | 686 | 910 | 239 | + Protein kinase domain. | ||
| cd00192 | PTKc | 6.0e-53 | 685 | 950 | 288 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
| smart00219 | TyrKc | 2.0e-56 | 687 | 949 | 273 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 5.0e-57 | 687 | 949 | 275 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| pfam11721 | Malectin | 2.0e-57 | 412 | 598 | 189 | + Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0000166 | nucleotide binding |
| GO:0004672 | protein kinase activity |
| GO:0005515 | protein binding |
| GO:0005524 | ATP binding |
| GO:0005886 | plasma membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAD41882.2 | 0 | 24 | 1022 | 32 | 1025 | OSJNBa0093O08.1 [Oryza sativa (japonica cultivar-group)] |
| EMBL | CAD41886.2 | 0 | 18 | 934 | 18 | 951 | OSJNBa0093O08.5 [Oryza sativa (japonica cultivar-group)] |
| GenBank | EEE61686.1 | 0 | 24 | 1022 | 32 | 1001 | hypothetical protein OsJ_16159 [Oryza sativa Japonica Group] |
| GenBank | EEE61690.1 | 0 | 18 | 1022 | 18 | 984 | hypothetical protein OsJ_16163 [Oryza sativa Japonica Group] |
| RefSeq | NP_001053881.1 | 0 | 18 | 934 | 18 | 934 | Os04g0616700 [Oryza sativa (japonica cultivar-group)] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 663 | 953 | 14 | 310 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
| PDB | 3uim_A | 0 | 663 | 953 | 14 | 310 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 663 | 953 | 22 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 663 | 953 | 22 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 663 | 953 | 22 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
