Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G048500.2 |
Family | GT51 |
Protein Properties | Length: 930 Molecular Weight: 104457 Isoelectric Point: 8.6393 |
Chromosome | Chromosome/Scaffold: 10 Start: 5299130 End: 5311834 |
Description | S-locus lectin protein kinase family protein |
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 |
GT51 | 732 | 841 | 2.8e-38 |
LNEKLVKNTFLKNERTFWRKILEMVLALALERTMSKQRILSSYVCKIYWGHGINGIESASNFYFGKHPSQLSLAESAMLAGLIPAPEHRSPLRDRSSGKT FQARVLKRMV |
Full Sequence |
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Protein Sequence Length: 930 Download |
MSLAVASPHR SMIHCKTSKF RFKNPQNLFG RTLTFYSLKS PTHFNSLLCL RVHSVRPESP 60 SIQTHHPIQE LLPLLAFSLS LLCFRLLSNV LLPDFALRWQ SLVAFSREAE ARTKSYPKHL 120 WQAIVAYEDR RFFTHFGIDP VGIGRAVLSL SARGGGSTIT QQPVRYGVRF PVCQDLCSED 180 CACLGMFYEN SSGSCYVLEN DLGSVILSST VENDFLGYVK VLVGPISTDS GGDNSFSNEK 240 NEFPIAAIVL LPSIGFFLLA ALVFFWWKRR LRSKGGEIKL GHLNSGSSED MDAFYIPGLP 300 QKFDYEELEA ATDNFKTQIG SGGFGSVYRG TLPDKTVVAV KKISNPGIQG KKEFCTEIAV 360 IGNIHHVNLV KLRGFCAQGR QRFLVYEYMN RGSLDRTLFG SGAVLEWQER FDIALGTARG 420 LAYLHRGCEH KIIHCDVKPE NILLHDHFQA KISDFGLSKL LTPEQSSLFT TMRGTRGYLA 480 PEWLTNSAIS EKTDVYSFGM VLLELVSGRK NCSLKSQSHS IEDTNSGGGN SLSSSVMGLI 540 YFPLLALEMH EQGRYLELAD AKLEGRVTNK EVEKLVRVAL CCVHEEPALR PSMATVVGML 600 EGGLPLGQPR VESLNFLRFY GRRFTEASMI EEERRQSDFM LFPQANVSHS STTGSNACLS 660 YISSQQISVS SLNFVMQLYI FLWYRWDNLW LWLEYGSAVL TTFSSNSLVI FFLAYFKLVV 720 QTWPGGTSSF LLNEKLVKNT FLKNERTFWR KILEMVLALA LERTMSKQRI LSSYVCKIYW 780 GHGINGIESA SNFYFGKHPS QLSLAESAML AGLIPAPEHR SPLRDRSSGK TFQARVLKRM 840 VKSGFLDIKM ALLTVRQPLY VRLRRPEHAD ELSDASSFSE LGVGVKSNVN EEGTESTLKG 900 TWDWERESKI REVCEEMERW AIKAQLRSS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 2.0e-46 | 315 | 600 | 305 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
smart00219 | TyrKc | 4.0e-47 | 315 | 600 | 303 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00220 | S_TKc | 2.0e-48 | 318 | 509 | 194 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
pfam00069 | Pkinase | 2.0e-51 | 318 | 509 | 196 | + Protein kinase domain. | ||
cd00180 | PKc | 3.0e-52 | 319 | 505 | 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
GO:0009252 | peptidoglycan biosynthetic process |
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 | ACM89497.1 | 0 | 162 | 668 | 258 | 768 | receptor-like protein kinase like protein [Glycine max] |
DDBJ | BAB11487.1 | 0 | 157 | 668 | 337 | 833 | S-receptor kinase [Arabidopsis thaliana] |
RefSeq | XP_002284416.1 | 2e-38 | 48 | 162 | 55 | 172 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002284416.1 | 0 | 162 | 668 | 541 | 1046 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002513778.1 | 0 | 162 | 668 | 289 | 790 | s-receptor kinase, 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 | 298 | 602 | 15 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 298 | 602 | 15 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 298 | 602 | 23 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 298 | 602 | 23 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 298 | 602 | 23 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
Transmembrane Domains | ||||
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Start | End | |||
245 | 267 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DV131627 | 216 | 347 | 560 | 0 |
DN498533 | 185 | 330 | 514 | 0 |
BQ629746 | 196 | 329 | 524 | 0 |
BQ623780 | 204 | 378 | 581 | 0 |
EE172103 | 211 | 297 | 506 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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