Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr2g074840.1 |
Family | CBM57 |
Protein Properties | Length: 975 Molecular Weight: 107909 Isoelectric Point: 6.8164 |
Chromosome | Chromosome/Scaffold: 2 Start: 22760236 End: 22768438 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 380 | 564 | 8.8e-28 |
LYINCGGKHAIVKKRSYDDDSDSSGAAKFHVSPTGNWAFSSTGIFIDGDQLGETYFPRNITTLTMADTELYMTARGSPISLTYYAFCLANGGYTVNLHFA EIMFTDDQTYASLGRRVFDIYLQGNPVQKDFNIAKEAGGVGKKVIKQFKDIVVSSNTLEIRLYWAGKGTQSLPNRSVYGPLISAI |
Full Sequence |
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Protein Sequence Length: 975 Download |
MARSTQFFFL SFILIWSISL TAFGATTIHP DEKKALEVIA KSLGKNDWNF DIDPCSNQPN 60 WATPKPAHPS PRLNIVENNV TCNCSISADN FCHVVEITLK GQNLPGTLPP ELNRLRYLQI 120 IDFSRNYLNG TIPKEWGSMM NIRNISLPSN RLTGSIPVEI ANISTLIQLD LTANQMSGII 180 PRELGNLTQI RTLKMSSNNF TGELPATLAK LTTLRDFEIS DNQFSGKVPD FIKNWTNIGT 240 LTIQGSGLSG PIPSEISLLR NLSELYVILR NCKINGTLPK YLGTIPTLKH LDLSFNNISG 300 TIPDTFDDIN GAKFIFLTGN LLTGSVPAWK KNVDVDLSYN NLSISQGNQI CQSDKLNSFV 360 FARLPKIFSH DLLNPALYSL YINCGGKHAI VKKRSYDDDS DSSGAAKFHV SPTGNWAFSS 420 TGIFIDGDQL GETYFPRNIT TLTMADTELY MTARGSPISL TYYAFCLANG GYTVNLHFAE 480 IMFTDDQTYA SLGRRVFDIY LQGNPVQKDF NIAKEAGGVG KKVIKQFKDI VVSSNTLEIR 540 LYWAGKGTQS LPNRSVYGPL ISAISVESDS PPGSISTVAV VGIVVAAIVI IILVFGILWW 600 KGCFGKKNSL ARELNSLDVQ TGIFTLRQIK AATDNFDVSN KIGEGGFGPV YKGCLPNGTL 660 IAVKQLSSKS KQGNREFLNE IGMISALQHP YLVKLHGCCV EGDQLMLVYE YLENNSLARA 720 LFGPEEHQIK LDWSRRQKIC VGIAKGLAYL HEESRLKVVH RDIKATNVLL DTNLDPKISD 780 FGLAKLDEED NTHISTRIVG TYGYMAPEYA MHGKLTDKAD VYSFGIVALE IVSGRSNTMY 840 RSKEEAFYLL EWAQLLHERG DLLEIVDKRL GSDFNKKEAM VMINVGLLCT NDTSNLRPPM 900 SSVVSMLEGR TVVPEFVSES NEVMDEKKLQ EMSQYYSQID ENSKVSKSQS RSLSIKDQCT 960 GSCPLDSSSW DEKN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 2.0e-47 | 641 | 834 | 203 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 4.0e-48 | 641 | 833 | 201 | + 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 | 1.0e-48 | 641 | 833 | 201 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 1.0e-48 | 642 | 831 | 194 | + 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. | ||
pfam11721 | Malectin | 6.0e-53 | 378 | 564 | 190 | + 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 | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005515 | protein binding |
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 | AAU10526.1 | 0 | 24 | 957 | 26 | 984 | putative receptor-like protein kinase 2 [Glycine max] |
EMBL | CBI20124.1 | 0 | 3 | 974 | 38 | 1036 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283578.1 | 0 | 25 | 974 | 25 | 984 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283596.1 | 0 | 32 | 974 | 64 | 1036 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002524514.1 | 0 | 8 | 974 | 6 | 1007 | ATP binding protein, putative [Ricinus communis] |
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 | 3ulz_A | 0 | 620 | 924 | 16 | 323 | A Chain A, The Crystal Structure Of A Cyanogenic Beta-Glucosidase From White Clover (Trifolium Repens L.), A Family 1 Glycosyl-Hydrolase |
PDB | 3uim_A | 0 | 620 | 924 | 16 | 323 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 620 | 924 | 24 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 620 | 924 | 24 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 620 | 924 | 24 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |