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CAZyme Information: KAE8541470.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Cryptococcus cf. gattii | |||||||||||
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| Lineage | Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus cf. gattii | |||||||||||
| CAZyme ID | KAE8541470.1 | |||||||||||
| CAZy Family | GH79 | |||||||||||
| CAZyme Description | unspecified product | |||||||||||
| CAZyme Property |
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| Genome Property |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 1172 | 1342 | 1.9e-23 | 0.9878787878787879 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 270896 | STKc_HAL4_like | 1.17e-80 | 419 | 633 | 1 | 218 | Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| 214567 | S_TKc | 2.32e-51 | 416 | 617 | 4 | 196 | Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. |
| 270622 | PKc | 1.86e-46 | 419 | 623 | 1 | 209 | Catalytic domain of Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation 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 more than 500 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. 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. |
| 270905 | STKc_AMPK-like | 6.02e-44 | 416 | 623 | 5 | 205 | Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| 270687 | STKc_CAMK | 9.87e-41 | 416 | 606 | 5 | 190 | The catalytic domain of CAMK family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.12e-171 | 1064 | 1578 | 643 | 1141 | |
| 3.03e-171 | 1064 | 1578 | 643 | 1141 | |
| 2.37e-142 | 1067 | 1578 | 286 | 750 | |
| 2.25e-19 | 1153 | 1353 | 19 | 211 | |
| 5.98e-19 | 1143 | 1353 | 9 | 211 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5.07e-27 | 419 | 621 | 19 | 213 | Crystal Structure of Sugarcane SAPK10 (serine/threonine-protein kinase 10) [Saccharum officinarum complex],5WAX_B Crystal Structure of Sugarcane SAPK10 (serine/threonine-protein kinase 10) [Saccharum officinarum complex] |
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| 6.57e-26 | 417 | 621 | 25 | 221 | Crystal structure of SnRK2.6 [Arabidopsis thaliana],3UDB_B Crystal structure of SnRK2.6 [Arabidopsis thaliana],3UDB_C Crystal structure of SnRK2.6 [Arabidopsis thaliana],3UDB_D Crystal structure of SnRK2.6 [Arabidopsis thaliana],3UDB_E Crystal structure of SnRK2.6 [Arabidopsis thaliana],3UDB_F Crystal structure of SnRK2.6 [Arabidopsis thaliana] |
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| 4.52e-25 | 417 | 633 | 12 | 228 | Crystal Structure of the CHK1 [Homo sapiens] |
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| 4.93e-25 | 417 | 621 | 24 | 220 | Crystal structure of SnRK2.6 in complex with HAB1 [Arabidopsis thaliana] |
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| 5.37e-25 | 417 | 633 | 13 | 229 | Co-crystal structure of Checkpoint Kinase Chk1 with a pyrrolo-pyridine inhibitor [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 9.68e-90 | 405 | 653 | 294 | 536 | Serine/threonine-protein kinase oca2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=oca2 PE=1 SV=1 |
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| 3.81e-79 | 408 | 631 | 210 | 434 | Serine/threonine-protein kinase HRK1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=HRK1 PE=1 SV=1 |
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| 2.69e-73 | 409 | 631 | 434 | 654 | Nitrogen permease reactivator protein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=NPR1 PE=1 SV=2 |
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| 1.09e-69 | 408 | 631 | 297 | 523 | Probable serine/threonine-protein kinase RTK1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=RTK1 PE=1 SV=1 |
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| 1.22e-66 | 402 | 656 | 350 | 602 | Serine/threonine-protein kinase PRR2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PRR2 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.999986 | 0.000089 |