| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G126858_T02 |
| Family | CBM57 |
| Protein Properties | Length: 944 Molecular Weight: 104079 Isoelectric Point: 7.0941 |
| Chromosome | Chromosome/Scaffold: 10 Start: 142431765 End: 142442301 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 361 | 534 | 8.8e-25 |
| TVDCGSSRSVFASDNSMYQPDDANLGVASYYISSPPRWGVSNVGRFMDTSNGSYIVNSSRRFQNTLDSKLFQTARMSASTLRYYGFGLENGDYTVTLQFG EFDFEDLQTWKSVGRRVFDIYLQGERKEQNFNIKKAAKEAGEASTSYTAVKKQYTVPVTKNILEIHLFWAGKGT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 944 Download |
| MESAFKQMKG EFVGLLIRRE VMQGRFSSFL LFWVEPRGVI PLELSGCISQ VWSPWFKGDP 60 CVGAATDGTS IYADKMNPGI KCDCSDHNNT ICHITELKMN KLDVVGPIPE ELRNLSHLTT 120 LNLQQNYLTG PLPSFLGELT ALQQMSLSGN ALSGTIPKEL GNLVNLIILS LGTNNLTGSL 180 PSELGNLVKL EHMYIDSAGL SGPIPSSFSK LTRLKTLCAS DNDFTGKIPD YIGSWSNLTD 240 LRFQGNSFQG PLPSTLANLV QLTSLILRNC RIFGTLALVN FSKFTGLTLL DLSFNNIIGE 300 VPQALLNMNS LTLLDFSYNY LSGNLPSWAS HNLQFVLPAG LECLQRNTSC FLGSPQSSSF 360 TVDCGSSRSV FASDNSMYQP DDANLGVASY YISSPPRWGV SNVGRFMDTS NGSYIVNSSR 420 RFQNTLDSKL FQTARMSAST LRYYGFGLEN GDYTVTLQFG EFDFEDLQTW KSVGRRVFDI 480 YLQGERKEQN FNIKKAAKEA GEASTSYTAV KKQYTVPVTK NILEIHLFWA GKGTCCIPNQ 540 GDYGPTISAL SATLNTKKKG NKIGVIIGVV IGATVLGLAI LATLCVWRHK RRKVSLEQQE 600 LYNIVRIPNV FCYTYGELRT ATENFSSANL LGEGGYGSVY KGKLVDGSVV AIKQLSETSR 660 QGKKEFVAEI ETISRVQHRN LVKLFGFCLE GNKPLLVYEY MESGSLDKAL FGNGRLNLNW 720 STRYKICLGI ARGLAYLHEE SSIRIVHRDI KASNVLLDAT LNPKISDFGL AKLYDDKKTH 780 VSTKVAGTFG YLSPEYAMRG HMTEKVDIFA FGVVMLEIIA GRPNYDGKLD QDMAYLLEWV 840 WQLYEEDHPL DIADPKLTEF DSVELLRAIR IALLCIQSSP RQRPSMSRVV SMLTGDSEAP 900 EAVSKPSYVA EWQSNTEGTS SSVSTAEAVS VAPFLNPVVD DGR* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00220 | S_TKc | 7.0e-50 | 629 | 835 | 209 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
| cd00192 | PTKc | 6.0e-51 | 629 | 838 | 228 | + 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. | ||
| cd00180 | PKc | 2.0e-52 | 631 | 849 | 223 | + 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. | ||
| smart00221 | STYKc | 5.0e-55 | 631 | 838 | 215 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| smart00219 | TyrKc | 4.0e-55 | 631 | 838 | 215 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| 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 |
| EMBL | CAD41882.2 | 0 | 58 | 943 | 62 | 1025 | OSJNBa0093O08.1 [Oryza sativa (japonica cultivar-group)] |
| EMBL | CAJ86314.1 | 0 | 50 | 943 | 52 | 938 | H0525G02.11 [Oryza sativa (indica cultivar-group)] |
| GenBank | EEE61686.1 | 0 | 58 | 943 | 62 | 1001 | hypothetical protein OsJ_16159 [Oryza sativa Japonica Group] |
| RefSeq | NP_001053877.1 | 0 | 58 | 943 | 62 | 924 | Os04g0616300 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002448532.1 | 0 | 43 | 943 | 17 | 886 | hypothetical protein SORBIDRAFT_06g028570 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 613 | 899 | 20 | 312 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
| PDB | 3uim_A | 0 | 613 | 899 | 20 | 312 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 613 | 896 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 613 | 896 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 613 | 896 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
