CAZyme Information: POW12195.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW12195.1
• CAZy Family: GH7
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
537		60342.60	8.8593

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93-210	15090	N/A	0	15090

• Gene Location: location=PKSL01000033:86536-88711(-)

Full Sequence      

MLSLALALVLISTLTLFHRLHGRKSIARKESIAIVVLGDIGRSPRMMRHALSFADQQWYV
SIFAYKGSAIRSTQYLMKSIERGSNFCPPSELGPNLQPASPKSEHSTRQSARISRSDHLI
LPRVLFALVIGPLKALYLSAGLLWTLLSNSNKFSYIMVQNPPAIPTLPIVQLVRLLLGSK
LIIDWHNTAYSILALKFGSDRHPMVRLAKWTEAKFGKNATLHLFVTEAEKQALSEMWHLR
GLKKVFYDRPPKSFCRLTVPEIHSFFRQSSFNYDSVLQKMFVQSGSSLHEESLLTYEDQE
LKIIKMKSDRPALIVSSTSWTIDEDFTVLIEALAMYTRSKKKNAKGTESLPKLLCLITGK
GPLKEYYLEIISKKSKEEGWEDVGIVCQSVWFDDPEDYRKILGAADLGISLHQSSSGLDL
PMKVVDMFGCGLPVCARNFNCISELVKHGQNGLVFDSAVELSEQLEELLSGFNSEQGGNQ
LSSSTEYSPTLSGLQKGIKTVMYGIDSQSPDDKGATRSWSSWEDEWNQRVFQTFQTL

Enzyme Prediction     

EC	2.4.1.142:10	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT33	30	530	3.3e-133	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340843	GT33_ALG1-like	7.09e-146	29	530	3	407	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	5.61e-124	26	458	1	360	transferase, transferring glycosyl groups
340816	Glycosyltransferase_GTB-type	2.01e-08	288	455	85	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.
223515	RfaB	5.90e-08	107	456	41	325	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831	GT4_PimA-like	1.38e-06	163	456	90	316	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CED84249.1|GT33	1.46e-109	30	496	47	495
QRV76128.1|GT33	7.00e-103	121	527	10	400
CDR45157.1|GT33	1.11e-97	11	530	15	492
CCA73277.1|GT33	5.13e-97	31	528	45	505
QRW18978.1|GT33	6.73e-94	121	502	37	392

PDB Hits     

POW12195.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q921Q3|ALG1_MOUSE	2.92e-89	8	477	14	432	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg1 PE=1 SV=3
sp|Q5R7A2|ALG1_PONAB	1.49e-87	32	502	35	458	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Pongo abelii OX=9601 GN=ALG1 PE=2 SV=1
sp|Q9BT22|ALG1_HUMAN	5.85e-87	23	502	27	458	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG1 PE=1 SV=2
sp|Q8L7M0|TUN_ARATH	1.97e-80	28	472	3	420	UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1
sp|P90522|ALG1_DICDI	6.33e-74	32	468	4	414	Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.994113	0.005907

TMHMM  Annotations     

Start	End
4	21
125	147