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Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10015239 |
Family | CBM57 |
Protein Properties | Length: 975 Molecular Weight: 107924 Isoelectric Point: 6.2495 |
Chromosome | Chromosome/Scaffold: 924 Start: 106287 End: 111619 |
Description | receptor-like kinase in flowers 1 |
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 | 365 | 536 | 4.7e-29 |
LHVNSGGKDLTVKENKTTILYEGDSQMLGGTARYFLNEQSYWGISSTGDFMDDNDYQNTRYTVAIQSSSIPELYQTARIAPISLTYFHHCLENGKYTVKL HFAEIVFSNDRTYTSLGKRVFDVYVQGKLEQKDLNIEDQAGGAQRPLVVPILNVNVTSNSLEIRFYYAGKGT |
Full Sequence |
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Protein Sequence Length: 975 Download |
MGTKYWQFNA DTCDVEEVGM TKVPPRNAEH TIECTCNNGS NTDCHVVRMA LKNHNLPGNL 60 PPQLVKLPYL QQVDFAYNYL NGSVPREWSS MQLSSISVLV NRLSGKIPKE LGNITTLTYL 120 SLEANQFSGT VPPELGELVN LETLMLSSNQ LTGPLPVSFA GLMNLTDFRI NDNSLNGRIP 180 NFIQNWKKLT RLEMQGSGLE GPIPPSISQL TNLVELRITD ISGPSQGFPE LVNATGILRF 240 ILRNCSLSGE LPDYVWLMKN MEMLDVSFNK LTGKIPTTIP SERLRFVFLT DNLLSGDVPD 300 SILKQGSNID LSYNNFELQG PGQPACQDNM NLNMNLYRSS SAANNTSRSL PCTNTFTCPR 360 YSNCLHVNSG GKDLTVKENK TTILYEGDSQ MLGGTARYFL NEQSYWGISS TGDFMDDNDY 420 QNTRYTVAIQ SSSIPELYQT ARIAPISLTY FHHCLENGKY TVKLHFAEIV FSNDRTYTSL 480 GKRVFDVYVQ GKLEQKDLNI EDQAGGAQRP LVVPILNVNV TSNSLEIRFY YAGKGTTRIP 540 DRGVYGPIIS AISVVSDDKA CSKLDGGGGK KGTTYAIFGV LGAFSLVIVI LGALWWKGYL 600 PGKCAKRKGF DEDDLPKGTF TLKQIRAATN DFDHANKIGE GGFGPVYKGV LPDGTLIAVK 660 QLSSKSRQGN REFLNEIGMI SCLRHPNLVK LHGFCVEGDQ LLVVYEYMVN NSLARVLFGR 720 ENCELKLDWP TRFKICVGIA KGLAFLHEES VIKIVHRDIK ATNVLLDEDL NPKISDFGLA 780 RLDEEEKTHV STRVAGTIGY MAPEYALWGH LSYKADVYSF GVLMLEIVSG KNNNNFMPSN 840 NCVCLLDWAC HLQQNGNLLP IIDETLRSDV KKDEAEIMIK VGLLCTNAAS SLRPTMSEVV 900 SMLEGRIPVP DTIPEPSSYA EDLRLKALRD LRKHGEGNSQ TQSHGFSQNT TADTCNSSLD 960 TTTQEFFEIK SAPH* 1020 |
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-52 | 637 | 903 | 286 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 2.0e-52 | 637 | 903 | 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 | 8.0e-53 | 636 | 904 | 291 | + 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 | 6.0e-53 | 637 | 903 | 280 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 2.0e-56 | 364 | 552 | 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 |
RefSeq | NP_174268.7 | 0 | 1 | 942 | 57 | 991 | RKF1 (RECEPTOR-LIKE KINASE IN FLOWERS 1); ATP binding / kinase/ protein serine/threonine kinase/ receptor signaling protein serine/threonine kinase [Arabidopsis thaliana] |
RefSeq | NP_850955.5 | 0 | 1 | 942 | 42 | 976 | RKF1 (RECEPTOR-LIKE KINASE IN FLOWERS 1); ATP binding / kinase/ protein serine/threonine kinase/ receptor signaling protein serine/threonine kinase [Arabidopsis thaliana] |
RefSeq | XP_002264679.1 | 0 | 1 | 972 | 16 | 1004 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305711.1 | 0 | 1 | 951 | 11 | 914 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522277.1 | 0 | 1 | 969 | 1 | 913 | 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 | 905 | 20 | 308 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 3uim_A | 0 | 620 | 905 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 620 | 905 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 620 | 905 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 620 | 905 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |