| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G011526_T01 |
| Family | CBM57 |
| Protein Properties | Length: 690 Molecular Weight: 75479.9 Isoelectric Point: 7.4724 |
| Chromosome | Chromosome/Scaffold: 7 Start: 94201889 End: 94238627 |
| 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 | 89 | 256 | 2.5e-29 |
| HINCGDKEATINGTKYEADTTPKGASLLYVSPGLNWAFSSTGNFMDDNINDDNYIATSASKLAVPNSDLYNKARLSPLSLTYYGLCMLSGSYTVNLHFAE IVFTNDSTYYSLGKRRFNVFIQGRMVLEDFDIEQSSGAAAKPVTKTFQTYVTNHTLEIQFYWAGRGTT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 690 Download |
| MGAVDYIYLS GNSLTGNIPG WLLRRNKIAD ISFNNFTMGS SGPSQCLQGS VNLVESYSAE 60 VNRLNSIHPC LKRNFPCVAS NGQYHSSLHI NCGDKEATIN GTKYEADTTP KGASLLYVSP 120 GLNWAFSSTG NFMDDNINDD NYIATSASKL AVPNSDLYNK ARLSPLSLTY YGLCMLSGSY 180 TVNLHFAEIV FTNDSTYYSL GKRRFNVFIQ GRMVLEDFDI EQSSGAAAKP VTKTFQTYVT 240 NHTLEIQFYW AGRGTTGIPY RGSYGPLISA ISVTPNFQIP LAVDPPKAGS REKRSSRASI 300 ALGIGIPIVA IFTALILGIY CIKKQRKSSM HEELRALDLQ IGSFTLRQIK AATRNFDAAN 360 KIGEGGFGSV YKGLLSDGTI IAVKQLSSRS KQGNREFVNE IGMISALQHP NLVKLYGCCT 420 EGNQLSLVYE YMENNCLARA LFVEQYRLRM DWGTRHKICL GIAKGLAYLH EESAIRIVHR 480 DIKASNILLD KDLNAKISDF GLAKLNEDDH THISTKVAGT IGYMAPEYAM RGYLTDKADV 540 YSFGVVVLEI VSGKSNTNYR PKEDFVYLLD WACVLHERGT LLELVDPDLG SNYSTEEALL 600 MLNVALLCTT AAPTLRPKMS KVVSLLEGSA PLQPLLSDLS LAANSLSSSG VRRNFWQNPG 660 ESQSLTAQAS CSDTNESSTI DIDGILLVS* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 1.0e-52 | 361 | 626 | 280 | + Protein tyrosine kinase. | ||
| smart00221 | STYKc | 2.0e-53 | 361 | 626 | 280 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| cd00192 | PTKc | 5.0e-54 | 360 | 627 | 287 | + 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 | 4.0e-55 | 361 | 626 | 279 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00180 | PKc | 2.0e-55 | 362 | 586 | 231 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004672 | protein kinase activity |
| GO:0005524 | ATP binding |
| GO:0006468 | protein phosphorylation |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC84403.1 | 0 | 1 | 686 | 331 | 1019 | hypothetical protein OsI_30981 [Oryza sativa Indica Group] |
| GenBank | EEE69521.1 | 0 | 1 | 686 | 331 | 1019 | hypothetical protein OsJ_28982 [Oryza sativa Japonica Group] |
| RefSeq | XP_002278131.1 | 0 | 1 | 679 | 321 | 993 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002306015.1 | 0 | 1 | 681 | 292 | 969 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532988.1 | 0 | 1 | 689 | 238 | 921 | conserved hypothetical protein [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 340 | 630 | 16 | 310 | A Chain A, Crystal Structure Of Insect Beta-N-Acetyl-D-Hexosaminidase Ofhex1 V327g Complexed With Pugnac |
| PDB | 3uim_A | 0 | 340 | 630 | 16 | 310 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 340 | 630 | 24 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 340 | 630 | 24 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 340 | 630 | 24 | 318 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
