CAZyme Information: PMAA_091990-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_091990-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
433	DS995902|CGC16	49696.62	6.4987

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995902:463595-464964(+)

Full Sequence      

MKITQSSSFANLQRLLTAILTSLAGRVLLVSLAVYGIVFEYCRLSYWRDPHSAFFDDRHV
YDLKYSLYREHEALQHISAYNARTQPPASTYASPNPRMCLAFVTVKRDHVNYFDASVGSL
LSGLNDRERRVFSVNVLFANTNPDVHPSWGQLWMDRLLDSVSSYNVPETDFQSLQALEES
HNWHEKGIYDYTYALDQCYLTGAPYIGIFEDDIIFADGWLVKTLRALHDIENKLKAQNWL
YLRLFYTETALSWTSDDFAYRHMGPVFLVTMLSACGALLLIRRTLPSARRHLDVATIAVI
CTITVPAFIGLVFMIGKYNITPLRGVVEMNKHGCCTQAMIFPRDQAPNLASFLRDRKGGQ
TDSLIEEYADKEALRRFALAPPQVQHVGIRSSRDNLEINTRSTWAFWFEENDPVALRREH
DEYFMEMGDMSFA

Enzyme Prediction     

No EC number prediction in PMAA_091990-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT109	25	424	6.1e-152	0.9708029197080292

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409190	PGAP4-like_fungal	0.0	24	395	1	375	uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4. This subfamily contains uncharacterized fungal proteins with similarity to animal post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. Proteins from this subfamily contain the putative catalytic site of PGAP4 and may have similar activities.
409189	PGAP4-like	6.35e-57	29	392	1	361	Post-GPI attachment to proteins factor 4 and similar proteins. This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.
409191	PGAP4	1.75e-23	26	392	4	376	Post-GPI attachment to proteins factor 4. Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.
398374	Glyco_transf_54	5.20e-05	97	242	34	186	N-Acetylglucosaminyltransferase-IV (GnT-IV) conserved region. The complex-type of oligosaccharides are synthesized through elongation by glycosyltransferases after trimming of the precursor oligosaccharides transferred to proteins in the endoplasmic reticulum. N-Acetylglucosaminyltransferases (GnTs) take part in the formation of branches in the biosynthesis of complex-type sugar chains. In vertebrates, six GnTs, designated as GnT-I to -VI, which catalyze the transfer of GlcNAc to the core mannose residues of Asn-linked sugar chains, have been identified. GnT-IV (EC:2.4.1.145) catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAc1-2Man1-3 arm of core oligosaccharide [Gn2(22)core oligosaccharide] and forms GlcNAc1-4(GlcNAc1-2)Man1-3 structure on the core oligosaccharide (Gn3(2,4,2)core oligosaccharide). In some members the conserved region occupies all but the very for N-terminal, where there is a signal sequence on all members. For other members the conserved region does not occupy the entire protein but is still to the N-terminus of the protein.
407157	HisKA_7TM	0.006	241	323	108	198	N-terminal 7TM region of histidine kinase. HisKA_7TM is an N-terminal region consisting of seven transmembrane domains found in Archaea and some bacteria. It is always found associated with histidine kinase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA19659.1|GT109	0.0	1	433	1	433
CAK46547.1|GT109	3.19e-159	24	420	25	422
BCR99311.1|GT109	2.10e-157	24	420	25	422
BCS11615.1|GT109	2.10e-157	24	420	25	422
CAP99360.1|GT109	5.47e-128	111	420	12	323

PDB Hits     

PMAA_091990-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

PMAA_091990-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000038	0.000005

TMHMM  Annotations     

Start	End
16	38
259	281
294	316