Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G162800.2 |
Family | CBM57 |
Protein Properties | Length: 1008 Molecular Weight: 112713 Isoelectric Point: 6.4671 |
Chromosome | Chromosome/Scaffold: 10 Start: 46905906 End: 46917925 |
Description | receptor-like kinase in flowers 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 405 | 592 | 7.4e-23 |
LHVNCGGKGTRIKEHKTNILYEGDGDVEGGAAKYYIKEDTYWGFSSTGDFMDDNDFQNTRYTVSKPLSNISELYTTARRAPISLTYFHYCLENGNYTITF NFAELQFTPDEAYNSLGRRIFDIYVQEKLVWKDFNIESEAKGSLKPLVKQISNVSVTTNFLAIRFFWDGKGTTRIPQRSAYGPLVSAI |
Full Sequence |
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Protein Sequence Length: 1008 Download |
MVTKKLFVFW IIAMGCFSLL RYSESKVPEE EVDALEEITT AMGSTYWKFI GDSCEIEMVG 60 VTLVPPKNSE HEISCECEAD GTVCHVVRIA IKGYNLPGIL PPQLVKLPYL REIDFAYNYL 120 NGTIPIEWAS MKLTSISLLV NRLSGEIPKY LGNITTLTYL SLEANQFSGP VPPELGNLVN 180 LTTLMLSSNQ LTGNLPVTFS LLKNLTDLRI NDNNFNGTIP GFILNWEQLS RLEMHASGLT 240 GPIPVSLSPL RNLLVLRISD ISGPSQDFPV LRDMKGLVTL VLRSCNISGE IPDYIWAMKN 300 LEMLDLSFNK LVGKIPTRIS SDRLRFVFLS GNMLSGDVPD SILKQGSSID LSYNNFEWQG 360 PEKPVCQENM NLNLNLFCSS SSRNNLRGAL PCKKDFTCPQ YSNCLHVNCG GKGTRIKEHK 420 TNILYEGDGD VEGGAAKYYI KEDTYWGFSS TGDFMDDNDF QNTRYTVSKP LSNISELYTT 480 ARRAPISLTY FHYCLENGNY TITFNFAELQ FTPDEAYNSL GRRIFDIYVQ EKLVWKDFNI 540 ESEAKGSLKP LVKQISNVSV TTNFLAIRFF WDGKGTTRIP QRSAYGPLVS AISVISDSKP 600 CSKRKNNGSS YAIVVGVLGS CLVLFTLGIL WWKGHLLVKY WRKEDTKEDS SSGNFTLKQI 660 KVATDDFDPA NKIGEGGFGP VYKGQLSDGT RIAVKQLSSK SRQGNREFLN EIGMISCLQH 720 PNLVKLHGFC VEGDQLLLVY EYMENNSLAR ALFGSENNQL ELDWPTRLRI CIGIAKGLAF 780 LHEESRLKIV HRDIKATNVL LDSDLNPKIS DFGLARLDEE EKTHITTRVA GTIGYMAPEY 840 ALWGHLTHKA DVYSFGVLTT ELVSGKNTNN FMPSKKFVCL LDWACHLLQS GNFIALLDER 900 LRSEVKKEEV QLMVKVALLC TNASASLRPT MSEVVNMLEG RTSVPDPIPE PSSFTEDLRF 960 KAMRDLQQQK EDHSRSQTQN STSVHSFYSS STSNSSNEIK PDSGFCQ* |
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-50 | 672 | 938 | 279 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 1.0e-51 | 672 | 938 | 276 | + 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 | 6.0e-52 | 671 | 939 | 290 | + 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 | 4.0e-52 | 672 | 938 | 274 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 8.0e-53 | 404 | 592 | 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 | AAC50043.1 | 0 | 6 | 977 | 21 | 990 | receptor-like serine/threonine kinase [Arabidopsis thaliana] |
RefSeq | NP_174268.7 | 0 | 6 | 977 | 21 | 991 | 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 | 31 | 1006 | 5 | 1008 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305711.1 | 0 | 32 | 999 | 1 | 936 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522277.1 | 0 | 42 | 1003 | 1 | 917 | 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 | 654 | 940 | 19 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 654 | 940 | 19 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 654 | 940 | 27 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 654 | 940 | 27 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 654 | 940 | 27 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |