Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.C00389.1 |
Family | GH18 |
Protein Properties | Length: 770 Molecular Weight: 86876.4 Isoelectric Point: 6.5109 |
Chromosome | Chromosome/Scaffold: 3 Start: 7277348 End: 7281070 |
Description | cysteine-rich RLK (RECEPTOR-like protein kinase) 34 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 31 | 355 | 0 |
YVYDGSDIRLSAIDSSLFSTLICAFAYIDSSTHQLYVNSSTEYFFHTFTDSVKFENSSITTLLSVWAGREDPSAFVSMLGESSSRRSFIESTIEKARLYG FSGVDLCGVLPSRSINMTNLSALLREWRDGVDAESRKSGKPQLLLVMAVYCQPIFNSVSYPLDSIQRNLDWVHLIAYDYHLPTRERFALPHAALFDPASQ NNTDFCITWLLTRGFPARKLVLGLPYHGYAWQLEDSSPDAIGHPAVGPAVTADGSFGYSSIKLYIRDFGYGATSVYNSTYAVNLFRKGSVWINFDDVEAI RAKVTYAKEKGLLGYNVFQINNDKN |
Full Sequence |
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Protein Sequence Length: 770 Download |
MASEGKIACF FVFFLCLRPS SEERTWVKSA YVYDGSDIRL SAIDSSLFST LICAFAYIDS 60 STHQLYVNSS TEYFFHTFTD SVKFENSSIT TLLSVWAGRE DPSAFVSMLG ESSSRRSFIE 120 STIEKARLYG FSGVDLCGVL PSRSINMTNL SALLREWRDG VDAESRKSGK PQLLLVMAVY 180 CQPIFNSVSY PLDSIQRNLD WVHLIAYDYH LPTRERFALP HAALFDPASQ NNTDFCITWL 240 LTRGFPARKL VLGLPYHGYA WQLEDSSPDA IGHPAVGPAV TADGSFGYSS IKLYIRDFGY 300 GATSVYNSTY AVNLFRKGSV WINFDDVEAI RAKVTYAKEK GLLGYNVFQI NNDKNWVLSR 360 TAQEASEDQQ HRRWFWPVLL ISIAIVLLIF GLICYLQRRT LKSKGILGVM KGFSSRLKTM 420 VCKGESLESG TPNLQTFGYV TLKAATDDFS SENKLGEGGF GPVYKGKLPK GQYIAVKRLS 480 KTSNQGLEEF KNEVMLTASL QHVNLVRLLG FCTDREELML IYEYMPNKSL DLYLFDPIRK 540 YLLDWVKCVH IIEGITQGLL YLQEYSNFTI IHRDLKASNV LLDDEMNPKI SDFGLARIFR 600 KDDIEANTNR IVGTYGYVPP EYVRKGIYST KYDIYSFGVL LLQIISGKKN SCCYGLNENL 660 NLLEYAYELW KDDKCMQFMD PSLDDSSSSC KLMRCMQVAL LCVQAKPGDR PSMLEVSSML 720 KNESSAVNSP KKPAFSINKD EDEDEDDKCL IKEAIHSVND ASISELCPR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 4.0e-46 | 452 | 720 | 277 | + 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 | 7.0e-47 | 455 | 644 | 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. | ||
pfam00704 | Glyco_hydro_18 | 5.0e-53 | 35 | 353 | 324 | + Glycosyl hydrolases family 18. | ||
smart00636 | Glyco_18 | 8.0e-58 | 35 | 353 | 337 | + Glyco_18 domain. | ||
cd02879 | GH18_plant_chitinase_class_V | 2.0e-105 | 24 | 359 | 341 | + The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004672 | protein kinase activity |
GO:0004674 | protein serine/threonine kinase activity |
GO:0005524 | ATP binding |
GO:0005975 | carbohydrate metabolic 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 |
EMBL | CBI35714.1 | 0 | 1 | 769 | 396 | 1130 | unnamed protein product [Vitis vinifera] |
EMBL | CBI35714.1 | 0 | 19 | 463 | 18 | 393 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263709.1 | 0 | 19 | 769 | 18 | 764 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002263792.1 | 0 | 1 | 769 | 1 | 753 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002270006.1 | 0 | 19 | 769 | 18 | 765 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 3aqu_D | 0 | 24 | 365 | 2 | 342 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_C | 0 | 24 | 365 | 2 | 342 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_B | 0 | 24 | 365 | 2 | 342 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_A | 0 | 24 | 365 | 2 | 342 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3alg_A | 0 | 27 | 364 | 4 | 343 | A Chain A, Crystal Structure Of Class V Chitinase (E115q Mutant) From Nicotiana Tobaccum In Complex With Nag4 |