Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10008178m |
Family | CBM57 |
Protein Properties | Length: 1023 Molecular Weight: 113204 Isoelectric Point: 6.8974 |
Chromosome | Chromosome/Scaffold: 1 Start: 10181256 End: 10188172 |
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 | 420 | 604 | 2.8e-28 |
HINCGGENVNVTNSLGKITYQADNYKTNAATNQHFETWGISNTGHFTDDKSDDDTYVISTSLRATGDSPELYKTARRSALSLVYYAFCLENGAYNVKLHF MEIQFAEEELYSRSGWRIFDIYVQGELFLKDFNIKEEANGTLKPVVKEKKAVNVTDHLLEIRLYWAGKGTTFIPNRGYYGPLISA |
Full Sequence |
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Protein Sequence Length: 1023 Download |
MWTVFSALLL FFTIITSFFI VTSTTSTSPA LHPDELIALE EIATTLGIKR LNLSYEDPCR 60 LKTLMIIQEV GIVWNPGMNN TIVCDCSFNN NKTCHITDLI LRNFTLSGKV PPEVAKLRYL 120 RSIDLYRNYL TGSIPMEWAS LPYLTSISLS ANLLSGNLPV GLQNFKNLKA IGLEGNQFSG 180 PIPDELGNLT NLAVLFLSSN QLTGSLPSTL ARLVNLEEFW ICDNNFTGII PGYIGNWSRL 240 EKLHLYASGL RGPIPDEVVR LENLTELSIS DTIGINSFPI ISSNAIKTLI LRNVSLSGPI 300 PSYIWNMPNL KSLDLSFNKL TGEVQGVKNP PKYTYLTGNM LSGNIDSGVF SNSKSNIDLS 360 YNKFIWPSSC QEKSNINTYR SSYVKNNICL ISTMIVLLYR TGLLPCAGPM NCKNYQRSLH 420 INCGGENVNV TNSLGKITYQ ADNYKTNAAT NQHFETWGIS NTGHFTDDKS DDDTYVISTS 480 LRATGDSPEL YKTARRSALS LVYYAFCLEN GAYNVKLHFM EIQFAEEELY SRSGWRIFDI 540 YVQGELFLKD FNIKEEANGT LKPVVKEKKA VNVTDHLLEI RLYWAGKGTT FIPNRGYYGP 600 LISAISLCHH SLGPKCGAEK TKLHTNYPII FGVTGAFVAI TLLGLGLYTQ KRCRGDKKAR 660 EIELRAQGLQ TACFTWKQLQ AATNNFDQAN KLGEGGFGSV FKGELSDGTI IAVKQLSSTS 720 SQGNREFVNE IGMISGLNHP NLVKLYGCCV EKNQLMLVYE YMENNSLALV LCGENSLKLD 780 WATRQKICVG IARGLEFLHE GSMIRMVHRD IKTSNVLLDA DLNAKISDFG LARLHEEEHT 840 HINTKVAGTM GYMAPEYVLW GQLTEKADVY SFGVVAMEIV SGKSNTKHKG MVDHVSLMDW 900 ALTLQQRGDI LEIVDPMLEG NFNSKEAVRM INMALVCTNS SPSLRPTMSE AVLMLEGALE 960 ITPVVSDPGL YGQNWCSKLK NIIDTDGSSS TSGLTDQITR TTKSSVSGSD LYPLYPPSII 1020 QA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 3.0e-51 | 691 | 955 | 283 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 3.0e-53 | 690 | 956 | 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 | 3.0e-53 | 691 | 955 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 3.0e-53 | 691 | 955 | 278 | + 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 | 3.0e-54 | 418 | 605 | 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 | |
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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 | 4 | 1020 | 15 | 943 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
GenBank | AAG10622.1 | 0 | 38 | 1020 | 69 | 1005 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
GenBank | AAG50774.1 | 0 | 4 | 1021 | 15 | 970 | AC079288_3 receptor protein kinase, putative [Arabidopsis thaliana] |
RefSeq | NP_174266.2 | 0 | 4 | 1020 | 15 | 965 | ATP binding / kinase/ protein binding / protein kinase/ protein serine/threonine kinase/ protein tyrosine kinase [Arabidopsis thaliana] |
RefSeq | NP_174267.4 | 0 | 4 | 1021 | 15 | 1008 | 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 | 674 | 957 | 20 | 308 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3uim_A | 0 | 674 | 957 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 670 | 957 | 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 | 670 | 957 | 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 | 670 | 957 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |