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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna21850.1-v1.0-hybrid |
Family | CE10 |
Protein Properties | Length: 1462 Molecular Weight: 161379 Isoelectric Point: 7.5142 |
Chromosome | Chromosome/Scaffold: 2 Start: 9134212 End: 9145819 |
Description | Malectin/receptor-like protein kinase family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 959 | 1139 | 5.9e-30 |
QYDDGFDVVSFLDQNNAVLPKNADTSHVFLAGDSADGNLAHHVAVRFCRESSRLRRLKLVGLIGIQPFFGGEERTESEMRLEKDPMLSVARTDWMWKALL PAGSTRDHEVANVSVPNEDMDILGMGFLATVVFVGGEDLLQDWQRRYCEWLRKSGIEAKVVEYPRMFHGFYVFPKLPESEE |
Full Sequence |
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Protein Sequence Length: 1462 Download |
MEIEKTPPNK KYLFLSSSPS SSLTTRYMMA ILLVFVYALL CNPTIVVSEP SSTTFTPQDN 60 ILIACGAKDP PKLPDGRVFK TDAQANQYLK ANNDNKVSDE KADVPSPLFT SARIFTSEAT 120 YTFHMGRPGW HFVRLYFFPI QNSVSDLQKA TFNVMTDKYT LLHSFNFNEA AKNNTHKTLF 180 NEYLLNVTEQ QFSIKFSPEK NSAAFINAIE VVSAPDYLIG DTGNNLQPLN QFQGLSNFGY 240 QTMYRVNMGG PLVTSVNDTL GREWIPDEQF IKSKNMAKVA KVESKAIKYP QGLTPQIAPP 300 SVYSTAAEMA DEGNQKFNVT WTFPAENAYG YLIRLHFCDI VSKTLGTLFF NVYINGNVAI 360 SELDLSATVN GLAIPFYKDI VVNSSLINND GVTVQIGPSK LQNGVQDAIL NGVEVMRMSN 420 SVNSLDGEFG VDGKEANPSS GGGVHKGAVA AVGFGLMFGA FIGLGAMVYK WKKRPQDWQK 480 RNSFSSWLLP VHAGDTSFMS SKNSVGKNMY SSTMGLGRFF SFAELQEATN NFDSSKIIGV 540 GGFGNVYIGV IDDGTSVAVK RGNPQSEQGI TEFQTEIQML SKLRHRHLVS LIGYCDENEE 600 MILVYEFMSN GPFRDHLYGK DLPPLSWKQR LEICIGAARG LHYLHTGTAQ GIIHRDVKTT 660 NILLDDQFTA KVADFGLSKD APMGQNHVST AVKGSFGYLD PEYFRRQQLT DKSDVYSFGV 720 VMLEALCARP AINPALPREQ VNLADWGMQW KRKGLLEKIV DPLLIGTINP ESMKKFGEAA 780 EKCLLEHGVD RPTMGDVLWN LEYALQLQEA FTEAKGEDDS VTVNAPADAA AASLADADAA 840 ASTAAASVPH PASILEEEEA PPAEQTGFAT LSWTTWLALK QVAKINETAF RLDGPVNRHL 900 LNLVDFKASL KSANGVTSSD VVVDPTRDLW FRLFVPDVET ERVLLSSRRY LLSRRATSQY 960 DDGFDVVSFL DQNNAVLPKN ADTSHVFLAG DSADGNLAHH VAVRFCRESS RLRRLKLVGL 1020 IGIQPFFGGE ERTESEMRLE KDPMLSVART DWMWKALLPA GSTRDHEVAN VSVPNEDMDI 1080 LGMGFLATVV FVGGEDLLQD WQRRYCEWLR KSGIEAKVVE YPRMFHGFYV FPKLPESEEL 1140 VSGGISLDWT RSVQAQTESV LSCFAATELS SFLCRLVASR RKAGSGAPVK EKRTREGDCV 1200 SDWVSDSGDG GEREWYWKLP LVLVVFSMSS VSSKEVRRER FEVKEERLGS PVSFRFRPSR 1260 GLSPVWIALS PHPRRPCNFS LSRHLHGMGR VGSYVFDVWT NQPPMMSHNS PTTTKPKWTH 1320 PRPNPSPSPP PIPKPRISPP STTSPRAAPS VPSSTRSHAP EPSPSSPSLT TTSSTSPTTS 1380 SPSPNYGVSS TPPLRSTPSK TSTASAINTK GIQMSTRAGS GPWSRSRCGG LKEKREIGSV 1440 DVWRRREKFV MNGEIIPIRF L* 1500 |
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-45 | 536 | 724 | 196 | + Protein tyrosine kinase. | ||
smart00219 | TyrKc | 5.0e-47 | 535 | 730 | 204 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 5.0e-47 | 538 | 724 | 191 | + 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. | ||
cd00192 | PTKc | 2.0e-47 | 536 | 798 | 285 | + 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. | ||
smart00221 | STYKc | 2.0e-47 | 536 | 730 | 203 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
GO:0008152 | metabolic process |
GO:0016787 | hydrolase activity |
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 | 3hgk_D | 0 | 522 | 810 | 31 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_C | 0 | 522 | 810 | 31 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_B | 0 | 522 | 810 | 31 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_A | 0 | 522 | 810 | 31 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 2qkw_B | 0 | 522 | 810 | 31 | 319 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |