Species | Rhinocladiella mackenziei | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei | |||||||||||
CAZyme ID | KIX03394.1 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Chitobiosyldiphosphodolichol beta-mannosyltransferase [Source:UniProtKB/TrEMBL;Acc:A0A0D2IC55] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.142:10 | 2.4.1.-:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT33 | 31 | 442 | 5.5e-146 | 0.9929411764705882 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
340843 | GT33_ALG1-like | 0.0 | 32 | 444 | 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 | 4.07e-132 | 29 | 410 | 3 | 371 | transferase, transferring glycosyl groups |
340831 | GT4_PimA-like | 9.79e-09 | 81 | 446 | 34 | 364 | 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. |
340825 | GT4_WbuB-like | 5.34e-07 | 80 | 435 | 58 | 384 | Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase. |
340816 | Glycosyltransferase_GTB-type | 1.37e-05 | 214 | 396 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
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1.12e-171 | 10 | 447 | 13 | 459 | |
6.64e-169 | 9 | 447 | 12 | 461 | |
1.83e-168 | 9 | 447 | 12 | 462 | |
2.69e-167 | 9 | 447 | 12 | 459 | |
2.69e-167 | 9 | 447 | 12 | 459 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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1.52e-122 | 68 | 447 | 66 | 446 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01551 PE=3 SV=1 |
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1.08e-91 | 35 | 446 | 44 | 440 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALG1 PE=3 SV=1 |
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5.27e-87 | 24 | 445 | 45 | 453 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALG1 PE=3 SV=1 |
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8.04e-84 | 35 | 439 | 29 | 415 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2 |
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9.50e-82 | 27 | 445 | 51 | 468 | 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 |
Other | SP_Sec_SPI | CS Position |
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1.000026 | 0.000031 |
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