Basic Information | |
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Species | Citrus clementina |
Cazyme ID | Ciclev10030182m |
Family | GH18 |
Protein Properties | Length: 740 Molecular Weight: 83138.3 Isoelectric Point: 7.9779 |
Chromosome | Chromosome/Scaffold: 8 Start: 20673015 End: 20677657 |
Description | lectin protein kinase family protein |
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 | 29 | 357 | 0 |
AGYWDSGGGFPVSDVNSALFTHLMCGFADVNSTSYELSLLPSDEKQFSNSTHTVKIKNPSITTLLSIGGGNDVSYSTYSSMASNPSSRKSFIDSSIKIAR LYGFQGLDLSWSQANTSWDNYNIAILFKEWRAAVDLEARNNSSQSQLILTATVSYSPFLTEATYPVDFIRQYLNWVHVFTTDYSAPTWTNFTGAHAALYD PNSDSNTEYGITEWIEEGLSADKLVLCLPFYGYAWTLVKPEDNGIGAAATGPALSEDGLVSYREIKNHIKSYGPNVHVLYNSTYVVNYCSIGKIWFGFDD VEAIRVKVAYAKEKKLRGYHVWLVSYDHD |
Full Sequence |
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Protein Sequence Length: 740 Download |
MASKIIILVL HIFIFSESLP ARAQTLIRAG YWDSGGGFPV SDVNSALFTH LMCGFADVNS 60 TSYELSLLPS DEKQFSNSTH TVKIKNPSIT TLLSIGGGND VSYSTYSSMA SNPSSRKSFI 120 DSSIKIARLY GFQGLDLSWS QANTSWDNYN IAILFKEWRA AVDLEARNNS SQSQLILTAT 180 VSYSPFLTEA TYPVDFIRQY LNWVHVFTTD YSAPTWTNFT GAHAALYDPN SDSNTEYGIT 240 EWIEEGLSAD KLVLCLPFYG YAWTLVKPED NGIGAAATGP ALSEDGLVSY REIKNHIKSY 300 GPNVHVLYNS TYVVNYCSIG KIWFGFDDVE AIRVKVAYAK EKKLRGYHVW LVSYDHDWML 360 SQAAASMVNQ RKVIDSSAEE DDKSGQNKRL LWVVVLPTTA ACILLLGFWL YYYCLMKNLK 420 LKVIDSAKSS KDGENSQVHA GDFNSNDPDL REYSLADIEV ATDRFSIENK LGEGGYGPVY 480 KGVLLDGQVI AVKKLSKTSK QGFEEFKNEV MLTAKLQHVN LIRVLGFCID REEQMLIYEY 540 MPRRSLDYFL FDPIRRFILD WKKRIHIIQG ITQGLLYLQE YSRLTIIHRD LKASNVLLDE 600 DMKPKISDFG LARIFVKDDL EANTSRIVGT HGYIPPEYVT RGIYSTKSDV YSFGVLLLQI 660 ISGRRLFVQS GQNENLSLVQ YHHHWKTSAN NRGRKFQQRG ASSTRCCASS ARPAAHAASS 720 ARCNASVHAA AARSSQRARE |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 8.0e-48 | 469 | 662 | 210 | + 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. | ||
cd02872 | GH18_chitolectin_chitotriosidase | 2.0e-64 | 36 | 350 | 332 | + This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens. | ||
pfam00704 | Glyco_hydro_18 | 2.0e-73 | 29 | 355 | 336 | + Glycosyl hydrolases family 18. | ||
smart00636 | Glyco_18 | 1.0e-78 | 29 | 355 | 344 | + Glyco_18 domain. | ||
cd02879 | GH18_plant_chitinase_class_V | 1.0e-117 | 24 | 361 | 343 | + 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:0005524 | ATP binding |
GO:0005975 | carbohydrate metabolic process |
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 |
EMBL | CBI35714.1 | 0 | 1 | 709 | 396 | 1051 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263709.1 | 0 | 21 | 709 | 20 | 685 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002263792.1 | 0 | 1 | 681 | 1 | 649 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002270006.1 | 0 | 21 | 681 | 20 | 661 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324558.1 | 0 | 1 | 686 | 1 | 666 | 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 | 3aqu_D | 0 | 24 | 365 | 2 | 340 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_C | 0 | 24 | 365 | 2 | 340 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_B | 0 | 24 | 365 | 2 | 340 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3aqu_A | 0 | 24 | 365 | 2 | 340 | A Chain A, Crystal Structure Of A Class V Chitinase From Arabidopsis Thaliana |
PDB | 3alg_A | 0 | 27 | 365 | 4 | 342 | A Chain A, Crystal Structure Of Class V Chitinase (E115q Mutant) From Nicotiana Tobaccum In Complex With Nag4 |