CAZyme Information: QSL67079.1

Basic Information

• Species: Pneumocystis wakefieldiae
• Lineage: Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis wakefieldiae
• CAZyme ID: QSL67079.1
• CAZy Family: GT59
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
978		111869.36	8.2381

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pwakefieldiae2A	3223	N/A	41	3182

• Gene Location: location=CP054547:287416-290989(-)

Full Sequence      

MNDKDTSTILDHDPLELSNISEKPRLGHYAILKTLGEGSFGKVKLAVHSITGHKVALKII
SRKSLLNLDMSSRVDREISYLKLLRHPHIIKLYEVIATPTDIIMVIEYAGGELFDYIVSR
GKMSEDEARRFFQQIITAVEYCHRHKIVHRDLKPENLLLDDFLNVKIADFGLSNLMTDGN
FLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLVGRLPFDDEFIPTLFKKING
GIYTIPSFLSSDAKELLSQMLVVDPIQRITLQEIRESKWFNLNLPDYLHPLDKYEEKNEV
DDKIVGKLGQAMGYNKDHVYEALARSDCNEIKDAYRLVAENQMRYKDSQSPPSWDTEQIK
FPRNISSSSLSHSSTNVNTCSVSKGIYSTLLPSVGGSYTRIEDQTPFHISILPSSLHNYH
IMYMNKKISSDSSNRNIKDKKLQSNISKSVLVPMSLNTEKKKRAIRWHFGIRSRSSPLEI
MIEIYRALKDLGAEWVDIESQNINLHEKTNKFKEKNLSENNNINETILDSNKAKDPYVIK
CRLTKSFDYEKKIIVTIVIQLYHLESNNFLVDFKCGGYENVCSIISELPSNDIKSETDKI
ISGISELIKNDIIKTNSQDLNTTHYSLDTSGKNLSEKQVTSPFPFLDMASQLILQLILTN
IWSILIIAISFILFLFCVIISLLFFSKPRLSYQSELYCKVISENGEFNEVLLNTLEDPAE
VFLSVVIPAFNETLRLSKMLEEAVEFLSFELEKDQKWEIIIIDDGSTDNTYKYSVEWALS
KSKTLLKHGEIRVSRLKKNRGKGGAVTHGMIHSRGEYIIFADADGASRFSNLYNLLKEIK
KIEKNGYGIAIGSRSYTASSDIILKRSKIRNFMMHVFQKYLWFMGIRHIKDTQCGFKLFT
RRAALMIFPNMHVEKWIFDIEVLILAEIFLIPVVEVPIAWQEVSGSKLSLISDSLRMAID
LLIMRLNYKFGFWKIKKK

Enzyme Prediction     

No EC number prediction in QSL67079.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	724	903	6.4e-28	0.9647058823529412

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
270981	STKc_AMPK_alpha	8.51e-180	26	280	1	256	Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK 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.
270905	STKc_AMPK-like	8.41e-144	28	279	1	252	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.
270983	STKc_BRSK1_2	1.43e-124	27	280	1	255	Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 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.
270980	STKc_MELK	2.59e-107	26	279	2	256	Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK 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.
270973	STKc_SIK	1.34e-106	29	280	2	253	Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSL67079.1|GT2	0.0	1	978	1	978
QEU59732.1|GT2	1.67e-81	679	976	29	320
CAH01769.1|GT2	3.23e-81	679	976	29	320
NP_596707.1|GT2	1.27e-78	688	974	30	314
CAA18889.1|GT2	1.27e-78	688	974	30	314

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3H4J_A	2.46e-160	23	343	5	324	crystal structure of pombe AMPK KDAID fragment [Schizosaccharomyces pombe],3H4J_B crystal structure of pombe AMPK KDAID fragment [Schizosaccharomyces pombe]
2FH9_A	1.84e-137	20	292	1	273	Structure and dimerization of the kinase domain from yeast Snf1 [Saccharomyces cerevisiae]
3MN3_A	3.28e-137	26	292	3	269	An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1 [Saccharomyces cerevisiae]
3HYH_A	3.78e-137	18	288	4	274	Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1 [Saccharomyces cerevisiae],3HYH_B Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1 [Saccharomyces cerevisiae]
3DAE_A	5.03e-137	18	288	5	275	Crystal structure of phosphorylated SNF1 kinase domain [Saccharomyces cerevisiae],3DAE_B Crystal structure of phosphorylated SNF1 kinase domain [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94168|SNF1_CANTR	2.19e-171	19	656	42	612	Carbon catabolite-derepressing protein kinase OS=Candida tropicalis OX=5482 GN=SNF1 PE=3 SV=1
sp|P06782|SNF1_YEAST	7.58e-170	18	656	44	626	Carbon catabolite-derepressing protein kinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SNF1 PE=1 SV=1
sp|Q00372|SNF1_CANGA	5.18e-167	16	592	26	584	Carbon catabolite-derepressing protein kinase OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=SNF1 PE=3 SV=2
sp|O74536|SNF1_SCHPO	6.96e-166	23	583	28	543	SNF1-like protein kinase ssp2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ssp2 PE=1 SV=1
sp|P52497|SNF1_CANAX	1.15e-164	25	580	49	573	Carbon catabolite-derepressing protein kinase OS=Candida albicans OX=5476 GN=SNF1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000000

TMHMM  Annotations     

Start	End
662	684