| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.F04180.1 |
| Family | CBM57 |
| Protein Properties | Length: 703 Molecular Weight: 77712.9 Isoelectric Point: 6.1165 |
| Chromosome | Chromosome/Scaffold: 6 Start: 50092178 End: 50097860 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 269 | 362 | 2.5e-21 |
| NSYYGLCMMKGNYKVRLHFAEIQYSNDKTFRSLGRRIFDVSIQGNQVLKDFNIAEEAGGVGKGIYRDFDNIYVNGSTLEIHLYWSGKGTTDVPD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 703 Download |
| MRNKYWNVTE TSCNDGIGLN VTTLPSGMTS IVSCDCSFIN STVCHVTKIQ LKGLDLIGIF 60 PDEFGNLTYL RVMSALGNQI SGIPKEIGNI STLEEFILED NLLEGTLEPN IGNLSRLSKF 120 ELSSNNFTGT IPESFGNLKN LRTLRISDLK GSSSNFPNLQ GMTMMQTLIL RNCLLTGSIP 180 SYIRNWTSMR TLDLSVNRLT GQVPDTMGHA LDYMFLANNS LTGAVPGWVT SQGMNCSDLS 240 YNNFNGSSPI SCQESQVNLV SSYASNGNNS YYGLCMMKGN YKVRLHFAEI QYSNDKTFRS 300 LGRRIFDVSI QGNQVLKDFN IAEEAGGVGK GIYRDFDNIY VNGSTLEIHL YWSGKGTTDV 360 PDRGVYGPLI SAIAVTPNFD VGSSGLSAGE IIGIRVALVV LLVLILLVLW LTGFFGGKEV 420 KDPEICHSLI HRTNMMPNLR PQIKVATDNF DSVNKIGEGG FGPVYKGILL DGIIIAVKQH 480 SPKSKQGNRE FLNEIGMISA LQHPNLIKLY GCCIEGNQLL LVYEYLENNS LARALFGLDE 540 QQIELDWATR KKIVLGIARG LAYLHEESGL KIVHRDIKAT NVLLDKELNA KISDFGLAKL 600 NEEEDTHIST RVAGTIGYMA PEYAMRGYLT DKADVYSFGV VALEIVSGKS NTNYRPKDEF 660 VYLLDWVKYS DFKFDENHAA KLLLDLKLSF STFCGFVWRT SE* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| smart00220 | S_TKc | 3.0e-48 | 450 | 650 | 206 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. |
| pfam00069 | Pkinase | 2.0e-49 | 455 | 649 | 200 | + Protein kinase domain. |
| smart00219 | TyrKc | 2.0e-49 | 455 | 647 | 199 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
| smart00221 | STYKc | 9.0e-50 | 455 | 647 | 199 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. |
| cd00180 | PKc | 5.0e-50 | 456 | 645 | 194 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAF78445.1 | 0 | 1 | 667 | 44 | 828 | AC018748_24 Contains a weak similarity to disease resistance protein (cf-5) gene from Lycopersicon esculentum gb |
| RefSeq | XP_002331720.1 | 0 | 28 | 667 | 46 | 795 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002332763.1 | 0.0001 | 45 | 183 | 163 | 303 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002332763.1 | 4e-30 | 46 | 251 | 140 | 325 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002332763.1 | 0 | 50 | 667 | 37 | 804 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 414 | 668 | 1 | 253 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3uim_A | 0 | 414 | 668 | 1 | 253 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 414 | 668 | 9 | 261 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 414 | 668 | 9 | 261 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 414 | 668 | 9 | 261 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
