Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10008435m |
Family | CBM57 |
Protein Properties | Length: 725 Molecular Weight: 80616.8 Isoelectric Point: 7.128 |
Chromosome | Chromosome/Scaffold: 1 Start: 10188663 End: 10194896 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 128 | 312 | 2.9e-27 |
HVNCGGENVTIETSSGKITYQADNSEIKAATYQHFKNWGISNTGDFVDDAIDDDVYVVSTSSTPSGDSPDLYKTARRSALSLVYYAFCLENGAYNVKLHF MEIQFAEEELYNRLGRRIFDVYVQGELFLKDFNIKESANGTLKPTVKEKKAVNVSDHLLEIRLYWAGKGTTLIPKRGHYGPLISA |
Full Sequence |
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Protein Sequence Length: 725 Download |
MYSLCLGFRI LRNLSLSGTI PSYIWSKPVL RTLDLSFNKL TGEVHGIKIA PLYIYLTSNM 60 LSGNIDPSVL QNKKSNIDLS YNNFSWSTSC QEKSNINTYR SSYLKKNLTE LFPCGVPMNC 120 KNYQRSLHVN CGGENVTIET SSGKITYQAD NSEIKAATYQ HFKNWGISNT GDFVDDAIDD 180 DVYVVSTSST PSGDSPDLYK TARRSALSLV YYAFCLENGA YNVKLHFMEI QFAEEELYNR 240 LGRRIFDVYV QGELFLKDFN IKESANGTLK PTVKEKKAVN VSDHLLEIRL YWAGKGTTLI 300 PKRGHYGPLI SAISLCHSSL EPQCGAARTE HHTNHSLIFG LTGAVVTIIL LVLGIYAGRR 360 CRGDNNTRER ELRSQGLQMV CFTWRQLQAA TNNFDEANKL GEGGFGSVFK GELPDGTIIA 420 VKQLSSKSCQ GNREFVNEIG MISGLNHPNL VKLYGGCVEK NQLLLVYEYM ENNSLALALF 480 GKSSLKLCWE ARRKICVGIA SGLEFLHEGS TIRMVHRDIK TPNVLLDTDL NAKISDFGLA 540 RLHEKENTHI STNIAGTIGY MAPEYALRGH LTEKADVYSF GVVAMEIVSG NSITKQQGRA 600 DNFSLINWAL TLEQRGDILE IVDPMLEGKF NSKEAVRMIK VSLVCTNANP SLRPLMSEAV 660 KMLEGKMEIT QVLSDHAVYG HDLHFSKLME RTPEASSMSD YDLYPDNSES ATLNSTVEFS 720 SSSL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00180 | PKc | 1.0e-48 | 400 | 587 | 192 | + 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. | ||
pfam07714 | Pkinase_Tyr | 2.0e-49 | 399 | 590 | 199 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 1.0e-50 | 399 | 663 | 271 | + 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 | 7.0e-51 | 399 | 663 | 271 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 2.0e-52 | 126 | 313 | 191 | + 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: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 | AAG10621.1 | 0 | 3 | 710 | 288 | 941 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
GenBank | AAG10622.1 | 0 | 10 | 720 | 321 | 1013 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
GenBank | AAG50772.1 | 0 | 10 | 724 | 263 | 920 | AC079288_1 receptor-like serine/threonine kinase (RFK1), putative [Arabidopsis thaliana] |
RefSeq | NP_174266.2 | 0 | 3 | 710 | 288 | 963 | ATP binding / kinase/ protein binding / protein kinase/ protein serine/threonine kinase/ protein tyrosine kinase [Arabidopsis thaliana] |
RefSeq | NP_174267.4 | 0 | 6 | 705 | 291 | 1000 | kinase [Arabidopsis thaliana] |
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 | 378 | 665 | 16 | 308 | A Chain A, Solution Structure Of The Second Rna-Binding Domain Of Hu2af65 |
PDB | 3uim_A | 0 | 378 | 665 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 378 | 665 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 378 | 665 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 378 | 665 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |