CAZyme Information: RQM14430.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM14430.1
• CAZy Family: PL3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
533		62008.61	7.2160

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000204:11164-12765(-)

Full Sequence      

MAESSGPRFLLCACVLLLTLIASLLQLLFFTLLPQIQLHIEFCNQTLASRSLLAPTPTSI
ELVPPMKLLFQSLYVSPRELALQQKEQERRRNDVTIKDQKKTIRGQKKKKKTMELEVFQA
KTLIETQALILQEQLVKKELEREKEQLRNLPAGFFLQTRGQGHEAISSKAAYCINVIAPC
DSTGLLVDFELYLNSLPSARPIYAFKGDGEQENAKNVSFDRNNVQRLDMPTSVIDIYLER
HPADKKYYPDFHPPKEKSIWMMQNVEFFDRHELDNPRVGVMIVKNRIGLKKVIEYRYRHQ
LSYSVFYTKHTSRDVYQPAVQRDWTSFLHLAGWSPFKNTRVIFQAWALHPEWPQLIIRVI
EPELCRWIEEQFGDMDSWLLQNVDYACGSVPAEEKDRLQNQIGLHLCPSETEGFGHYINE
ARSVGALILTTNIPPMNELVDEKSGVLIGEPYLWWWQTKGDLFMPLSQLTVADMERGIEQ
ILLLSIEERQRMGRRSRAKFLKDRTYFFNAMAALEESLCQDEIRIEKLQSYLY

Enzyme Prediction     

No EC number prediction in RQM14430.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340831	GT4_PimA-like	1.46e-13	327	502	195	350	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.
223515	RfaB	1.41e-08	327	503	202	360	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340838	GT4_MtfB-like	6.94e-07	327	505	195	356	glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
340816	Glycosyltransferase_GTB-type	8.25e-07	271	448	61	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.
395425	Glycos_transf_1	1.76e-06	388	497	65	156	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ29740.1|GT4	0.0	66	533	1	468
CCA20002.1|GT4	6.02e-186	5	533	10	470
AGP82611.1|GT4	2.37e-31	174	518	8	326
QNH11168.1|GT4	5.56e-31	312	521	133	325
QNH15459.1|GT4	7.62e-31	312	521	133	325

PDB Hits     

RQM14430.1 has no PDB hit.

Swiss-Prot Hits     

RQM14430.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000012	0.000000

TMHMM  Annotations     

Start	End
9	31