CAZyme Information: SPSK_09170-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_09170-t39_1-p1
• CAZy Family: GT2
• CAZyme Description: beta-1,4-mannosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
475		51989.43	9.8235

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000007:326030-327513(+)

Full Sequence      

MALGFSLIGAALLVLTAVMFLAWPRRYRGQAPTVQVLVLGDVGRSPRMQYHALSIAQRGH
VQLIGYYESDLLEELDQHPRLTKVQLAPAPVFIRRLPFVIGGPLKVVWQILNLVMTLTYF
TRPARWLLVQNPPSIPTLAVAALVCSLRGTKLLIDWHNYGWSILAGTRGAKHPFVGVSKA
YEVIFGRLGDAHLAVTAAMAAQLRKAPYNLPASAPLAVLHDRPAELFQPVEFSTSFPPAT
RGQEVARILAGASDVVVRRLLANMNTKVLVSSTSWTPDEDFQLLLDALVAYIRDVPSDSA
NGRRPPVLAVITGKGPQKAMYERKLAQLAADGHLPPDQIAVRTAFLPMKDYARLLALADL
GVCLHMSSSGVDLPMKVVDMFGAGLPVAAYSDYESFGELVRDGDNGRGFTTSGELAALLA
RLLDRRDQAAPQTTELENLRQGARKESVLRWPEEWNRVVAPIFELSEAAASKKTK

Enzyme Prediction     

EC	2.4.1.142:10	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT33	33	461	9.2e-140	0.9905882352941177

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340843	GT33_ALG1-like	2.08e-179	33	463	5	411	chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins. This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
215155	PLN02275	1.30e-126	29	414	2	362	transferase, transferring glycosyl groups
340831	GT4_PimA-like	1.61e-10	134	406	90	312	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
340816	Glycosyltransferase_GTB-type	0.001	270	409	114	235	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ55236.1|GT33	6.94e-159	33	467	38	456
AEO55016.1|GT33	4.97e-146	33	463	53	483
VBB84667.1|GT33	7.15e-145	6	470	3	452
CDP31425.1|GT33	4.44e-140	6	470	3	470
CAP65429.1|GT33	4.44e-140	6	470	3	470

PDB Hits     

SPSK_09170-t39_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AZD1|ALG1_ARTBC	1.51e-88	73	465	71	445	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01551 PE=3 SV=1
sp|O13933|ALG1_SCHPO	5.04e-83	12	464	1	421	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2
sp|Q921Q3|ALG1_MOUSE	2.77e-81	6	467	7	465	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg1 PE=1 SV=3
sp|Q6C3K2|ALG1_YARLI	4.61e-81	36	467	44	442	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALG1 PE=3 SV=1
sp|Q9BT22|ALG1_HUMAN	4.00e-75	10	462	10	460	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000067	0.000000

TMHMM  Annotations     

Start	End
2	24