Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.016G011200.4 |
Family | CBM57 |
Protein Properties | Length: 589 Molecular Weight: 65405.9 Isoelectric Point: 7.8451 |
Chromosome | Chromosome/Scaffold: 16 Start: 567108 End: 570173 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 22 | 182 | 3.7e-26 |
LYINCGGGETVVDGKVFEADSTTSNYHSAPRKNWAYSCSGDFGSKTYDSSDYIKNEECGVCDSAGTQLYNSSRLCPLSLTYYGFCLFKGYYTVKLYFAET VYQNDEDYSNLGKRVFDVYIQGKRELKDFNIKENATGTNKTWTASFTAYVGDDHLLNIHFF |
Full Sequence |
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Protein Sequence Length: 589 Download |
MSGKTKVTDF LYSLSFFTDD SLYINCGGGE TVVDGKVFEA DSTTSNYHSA PRKNWAYSCS 60 GDFGSKTYDS SDYIKNEECG VCDSAGTQLY NSSRLCPLSL TYYGFCLFKG YYTVKLYFAE 120 TVYQNDEDYS NLGKRVFDVY IQGKRELKDF NIKENATGTN KTWTASFTAY VGDDHLLNIH 180 FFWAGKGSFQ VPGFSYRTAA LSLNGPLVSG ISVTANFKVG TGLSPSQIAG ITAGSVFAPL 240 LLLAFMWKMG WLRKSELDEI TIEVQGKSFT LKQIIDATRK FSPKMEIGRG RFGIVYKAEL 300 PNEIKLAVKK ISPHSKQQGK DELQREIFNL KSLHHENLVQ LLDGYSNKGL HLLVYDYMHK 360 GSLHRALFEP NSTTKLDWRA RFDICLGIAR GLKYLHEEKR FKIVHGNIKP SNIMLDNSLT 420 AKLSDFGLAT LCDEEDPFMA IKAKGSRVYM APEYSMGKAI TVKADVYSFG VVLLEIVSGK 480 VSADYTPNQE AEFLLDKAGV LHDKGRILEL VDKKLASSYN RKQALTVLLL AMKCVNLSPT 540 LRPKMSEVVS VLEGEKRIDE ISECDTPSAN IGGLCGACSM VLEIEPIS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 2.0e-42 | 286 | 552 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 1.0e-42 | 286 | 552 | 277 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
smart00220 | S_TKc | 5.0e-43 | 286 | 480 | 197 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
pfam00069 | Pkinase | 2.0e-44 | 281 | 480 | 203 | + Protein kinase domain. | ||
cd00180 | PKc | 3.0e-51 | 287 | 476 | 193 | + 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. |
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 |
RefSeq | XP_002323147.1 | 0 | 89 | 561 | 1 | 467 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002323152.1 | 0 | 43 | 376 | 8 | 339 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002323154.1 | 0 | 110 | 588 | 308 | 787 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002323341.1 | 0 | 21 | 556 | 299 | 831 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333814.1 | 0 | 1 | 258 | 1 | 258 | predicted protein [Populus trichocarpa] |
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 | 265 | 555 | 16 | 309 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 265 | 555 | 16 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 265 | 555 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 265 | 555 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 265 | 555 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CA925701 | 238 | 220 | 457 | 0 |
CA925428 | 241 | 260 | 500 | 0 |
CA925163 | 246 | 220 | 465 | 0 |
CA925239 | 236 | 220 | 455 | 0 |
CA925482 | 233 | 268 | 500 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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