CAZyme Information: HCAG_08624-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_08624-t26_1-p1
• CAZy Family: GT48
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315	CH476666|CGC2	34915.08	6.8241

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476666:174278-175380(+)

Full Sequence      

MDVGPVVAQVVCQLRKTNLVIDWHNFGYSILALKLGDGHPMVKINKSHESTFGRFSSAHF
CVSNAMARRLRDDLKIITPILVLHDRPQSCFQPFRNDEQKYAFLSSLSETAEFVGDLRAG
TCRLLVSSTSWTPDEDFSILIDALCRYSAIASTRNLSLPRLGVIITGKGPQQQMYLSRIA
KLRAQGKLENVKIKTAWLSLEEYAQLLASVSLGVCLHTSSSGVDLPMKVVDMFGAGLPVV
GWNKYEAWPELVSQGVNGLGFGSTDELVTHLVDLFGGTEEKLSLLRQGALQESERRWDDE
WDPVAGKLFGLPYNP

Enzyme Prediction     

EC	2.4.1.142:10	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT33	6	307	9.1e-111	0.7388235294117647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340843	GT33_ALG1-like	3.50e-161	6	309	110	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	9.28e-97	6	275	116	371	transferase, transferring glycosyl groups
223515	RfaB	3.52e-12	3	308	96	370	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831	GT4_PimA-like	2.09e-08	5	308	94	361	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	9.80e-05	65	261	67	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
QSS66516.1|GT33	6.77e-228	6	315	160	469
QSS73446.1|GT33	3.16e-224	6	315	161	470
QSS48656.1|GT33	7.41e-223	6	315	161	470
BCS01601.1|GT33	2.50e-137	7	311	155	458
BCS13317.1|GT33	2.50e-137	7	311	155	458

PDB Hits     

HCAG_08624-t26_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	3.00e-138	7	311	141	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	8.69e-69	7	304	137	415	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2
sp|Q6C3K2|ALG1_YARLI	4.64e-68	16	311	158	440	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALG1 PE=3 SV=1
sp|Q6BS98|ALG1_DEBHA	1.04e-60	6	309	163	467	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALG1 PE=3 SV=2
sp|Q8L7M0|TUN_ARATH	3.45e-60	15	308	125	454	UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000000

TMHMM  Annotations     

There is no transmembrane helices in HCAG_08624-t26_1-p1.