Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna23790.1-v1.0-hybrid |
Family | CBM57 |
Protein Properties | Length: 1665 Molecular Weight: 185178 Isoelectric Point: 6.632 |
Chromosome | Chromosome/Scaffold: 3 Start: 4321005 End: 4344745 |
Description | receptor-like kinase in flowers 1 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 273 | 459 | 3.9e-23 |
MHVNCGGNDLTVKEDNNAKVLYEGDGGVEGGTAKYFKNDKSMWGFSSTGDFMDVYDWRNTRYSMSMASLSLSEIYTTARISPISLTYFSYCLENGLYTIS IHFAEIKITNNGTHSLGRRFFDIYVQERLVWKDFNIVDEAGMAQKRVVKQLSNVSVTSNVLDIRLYWAGKGTTRIPEGGDYGPLISA |
Full Sequence |
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Protein Sequence Length: 1665 Download |
MGAVYWKFND DTCRIEVVGL TEAPPKGSER RIDCECHFKN NTECHVVKLM IKGYSLPGLL 60 PPELVKLPYL QEIDFAYNYL SGTIPKEWAS MKLTYLSVYV NRVSGEIPKE LGNIRTLTYL 120 SLEANQFSGT LPPELGYLVN LRSLILSSNR LTGNLPETFA GLKKLEDIRL SDNNFNGTIP 180 DWVQNWKQLK RLEMHSSGLA GPLPSNISVL TNLNDLRISD MDGPNQEFPL LRNMTGLVRL 240 DLSFNKLAGE LPFTAGVTER LKFVFWGTDS NCMHVNCGGN DLTVKEDNNA KVLYEGDGGV 300 EGGTAKYFKN DKSMWGFSST GDFMDVYDWR NTRYSMSMAS LSLSEIYTTA RISPISLTYF 360 SYCLENGLYT ISIHFAEIKI TNNGTHSLGR RFFDIYVQER LVWKDFNIVD EAGMAQKRVV 420 KQLSNVSVTS NVLDIRLYWA GKGTTRIPEG GDYGPLISAI SVVSGGDIQT GNFCLKQIKA 480 ATDDFDPANK IGEGGFGPVF KGQLPNGSLI AIKQLSSNSK QGNREFLNEM GMISCLQHPN 540 LVTLHGCCIE EDQLLLVYEY MENNSLARAL YVDALEEITR TMGAKYWKFN GGSCQIELVG 600 VTAEPPKASE SSIECECNNT VCHVVKLGLK RFSLPGKLPP QLVKLPYLRE IDLVYNYLSG 660 TIPAEWGSMQ LTSISLLVNR LSGEIPVVLG NITTLTYLNL EANQFSGVVP PELGSLINLG 720 SLILSSNYLT GNIPNTFAGL RNLTDFRIND NNFNGTIPDF IQNWKQLGRL EIHGSGLRGP 780 IPSNISLLSN LVELRISDIN GTEQDFPMLK NMTGLVRLIL RNCNISGEIP PYMWTLQNLE 840 MLDVSFNKLI GEIPTTISLE RLRFLFLTGN SLSGSIPDSI FKDGSNVDLS YNNFTWQGPE 900 QPTCQENMSE SKPELVSKLF LREQLKERSS VLEELDLSSL MVLYEASSEH FSTSSTLFHI 960 RFSILWSSFF SLFLYYLILE SYGGQATCQE NWAERKLVTD GKESDLQMGN FTLKQLQAAT 1020 NDFDYNNKIG EGGFGPVYKG QLPDGTVIAV KQLSSKSRQG NREFLNEMGM ISCLQHPNLV 1080 KLHGCCIEGG QLLLVYEYLE NNNLARALFG RDTQIKMDWP TRRKICIGIA RGLAFLHEES 1140 VLKIVHRDIK ATNVLLDVDL NPKISDFGLA KLDEEEKTHI STRVAGTIKQ TSACWPGGVD 1200 TNDMKKMKHN IIMLMILVLC LFCITLSEVE AQCSPLPVAE VEALKEIGKE LGKNWNFEED 1260 PCSKKSSWAT LVPKSDDWPS SMNNVTCSCS FPDETYHVIS IILQGQDLHG VLPTSIVKLP 1320 YLTFLDLNRN YLSGKIPIQW ASTKLEHLSL ETNRFSGTVP PELGNLVNLE TLVLSANNLT 1380 GELPMSLTKL TKLIELRISS NNFSGTIAPH FFQSWNLLQQ LEIQASGLEG PIPSTISILK 1440 NLTELRISDL TGRGSEFPPL QKMTGLKRLD LSFNRLVGSI SIPDFDFRPP LGRETKLIVG 1500 GASVLCLAVL ILGLLWWKGC LNSKTEMERA LRGLDLQTGL FTFKHIKAAT NNFDPTNKIG 1560 EGGFGPVYKI FILRRRSVRF NHRDQIDVVA GHTSSTEGKA RAKVGDSGGT KALTEMKRSL 1620 ASALRMVGRS GGRGCIRRWF WVLKCDVILL GSGHAATALF AFPI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00180 | PKc | 5.0e-13 | 491 | 566 | 78 | + 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. | ||
smart00219 | TyrKc | 2.0e-16 | 490 | 566 | 83 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 7.0e-30 | 1029 | 1188 | 163 | + 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. | ||
smart00219 | TyrKc | 1.0e-30 | 1026 | 1184 | 167 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 9.0e-51 | 272 | 460 | 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 - 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 | 1007 | 1188 | 16 | 199 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3ulz_A | 9e-18 | 469 | 570 | 16 | 118 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3uim_A | 0 | 1007 | 1188 | 16 | 199 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3uim_A | 9e-18 | 469 | 570 | 16 | 118 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |