Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr8g076800.1 |
Family | GH35 |
Protein Properties | Length: 395 Molecular Weight: 45450.8 Isoelectric Point: 7.2952 |
Chromosome | Chromosome/Scaffold: 8 Start: 21124963 End: 21129275 |
Description | beta galactosidase 1 |
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 |
GH35 | 60 | 182 | 1.3e-22 |
FQMQKFIEKIVDMMKAERLFESQGGPIIMSQIENECGPTEYEIGVSRYGYRTRYRSSVDHINTCNGFYCDYFYPNKDYKPKMWTEAWTGWFTEFGGPVPH RPAEDMAFSVARFIQKGGSLFTL |
Full Sequence |
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Protein Sequence Length: 395 Download |
MESSTDTKYL QESPELVSVV TKLKKEVDVW KIGFRVLDSW IVTASNGNQH MEFIIGDAKF 60 QMQKFIEKIV DMMKAERLFE SQGGPIIMSQ IENECGPTEY EIGVSRYGYR TRYRSSVDHI 120 NTCNGFYCDY FYPNKDYKPK MWTEAWTGWF TEFGGPVPHR PAEDMAFSVA RFIQKGGSLF 180 TLRKYSAQLS LTAIVCSLGT LQSIDVTFVM EHNPNAWCIG WDMNLLAAAY VGIISSGLTY 240 YVQGIVMQKK GPVFVRMTTI FSNYYQCLCF IVNVMFDVRV AICTCLSRQG VKEFLTEINV 300 ISEVEHENLV KLYGCCVERN SRILVYNYLE NNRHYIVVCV FERYENIKQI FLICLFPILP 360 FLNSILNYVA KPWPIVGSLP EMIANRPTLK WIQN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 5.0e-7 | 277 | 331 | 58 | + 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 | 3.0e-7 | 277 | 336 | 72 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 2.0e-7 | 277 | 331 | 58 | + 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. | ||
pfam01301 | Glyco_hydro_35 | 8.0e-32 | 62 | 179 | 149 | + Glycosyl hydrolases family 35. | ||
PLN03059 | PLN03059 | 8.0e-55 | 56 | 185 | 149 | + beta-galactosidase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004672 | protein kinase activity |
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 |
GenBank | ABK96254.1 | 0 | 56 | 185 | 151 | 299 | unknown [Populus trichocarpa x Populus deltoides] |
GenBank | ABN08398.1 | 0 | 59 | 187 | 149 | 296 | D-galactoside/L-rhamnose binding SUEL lectin; Galactose-binding like [Medicago truncatula] |
GenBank | ACJ85203.1 | 0 | 180 | 281 | 36 | 137 | unknown [Medicago truncatula] |
RefSeq | XP_002327432.1 | 0 | 56 | 187 | 144 | 294 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329051.1 | 0 | 2 | 185 | 81 | 283 | 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 | 0.0007 | 287 | 346 | 67 | 124 | A Chain A, The Crystal Structure Of Engineered Ospa |
PDB | 3uim_A | 0.0007 | 287 | 346 | 67 | 124 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0.0008 | 287 | 346 | 75 | 132 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0.0008 | 287 | 346 | 75 | 132 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0.0008 | 287 | 346 | 75 | 132 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |