CAZyme Information: PNEJI1_001731-t26_1-p1

Basic Information

• Species: Pneumocystis jirovecii
• Lineage: Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis jirovecii
• CAZyme ID: PNEJI1_001731-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
318	CAKM01000247|CGC1	36871.63	10.0076

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PjiroveciiSE8	3752	1209962	217	3535

• Gene Location: location=CAKM01000247:8193-9328(+)

Full Sequence      

MIIMKLTFWPILIFIISVLSAFSQPRISYQSELYCKVISETGEYDKVHFNTLDVPAEVFL
SVVVPAFNEKLRLSKMLQETVEFLSKFEKQQKWEILIIDDGSTDNTFEYSVEWALSKSKT
LKQGEIRICSLKKNRGKGGAVTHGMIHSRGEYIIFADADGASKFSDLRYLLKEIKKIEEN
GYGIAIGSRSHMASNNIILKRSKIRSFMMYVFHKYLWFMGIRHIKDTQCGFKLFTRKAAL
VIFSNIHVEKWIFDIEILILAEIFLIPVIEVPITWHEVSGSKLSLISDSLRMAIDLLVMR
LSYKFGLWKIKKKKIIKF

Enzyme Prediction     

No EC number prediction in PNEJI1_001731-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	61	239	2.5e-29	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
133031	DPG_synthase	9.23e-95	62	282	1	211	DPG_synthase is involved in protein N-linked glycosylation. UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.
240336	PTZ00260	5.87e-94	43	308	54	321	dolichyl-phosphate beta-glucosyltransferase; Provisional
133022	DPM_DPG-synthase_like	8.62e-53	62	261	1	185	DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
395426	Glycos_transf_2	9.65e-28	61	238	1	163	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
133062	DPM1_like	1.74e-23	62	292	1	220	DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSL67079.1|GT2	2.47e-162	3	313	666	978
NP_596707.1|GT2	8.90e-91	25	309	30	314
CAA18889.1|GT2	8.90e-91	25	309	30	314
QGN18207.1|GT2	1.38e-85	23	308	31	312
BAP73488.1|GT2	1.38e-85	23	308	31	312

PDB Hits     

PNEJI1_001731-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O60061|ALG5_SCHPO	1.58e-91	25	309	30	314	Dolichyl-phosphate beta-glucosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg5 PE=3 SV=1
sp|P40350|ALG5_YEAST	2.96e-81	25	313	37	333	Dolichyl-phosphate beta-glucosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG5 PE=1 SV=1
sp|Q54J42|ALG5_DICDI	1.28e-72	58	311	74	326	Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
sp|Q9Y673|ALG5_HUMAN	1.33e-65	60	314	67	321	Dolichyl-phosphate beta-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG5 PE=1 SV=1
sp|Q9DB25|ALG5_MOUSE	2.96e-64	60	314	67	321	Dolichyl-phosphate beta-glucosyltransferase OS=Mus musculus OX=10090 GN=Alg5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001714	0.998256	CS pos: 23-24. Pr: 0.9257

TMHMM  Annotations     

There is no transmembrane helices in PNEJI1_001731-t26_1-p1.