CAZyme Information: SDRG_02595-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_02595-t26_1-p1
• CAZy Family: CBM48
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
524		56911.95	8.9460

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SdiclinaVS20	17448	1156394	89	17359

• Gene Location: location=JH767137:258946-260670(-)

Full Sequence      

MAMRLIASVVLYAAAAASAHTSLRVLWPPPNYLVATPNVPIAIAVTGPTTDGHIRLTGHK
LRTTFAMQAPGAVIGNIYLGSHHVLVEALSANFTRISAPIVLYIERIPSRVELFRDSGRS
KMALVALPAAKAARPTTRTLCFGGASSPMDGQKRLWLRLLASLRRHPTVDYSFHVFLLEP
KPVHPTDVFTAHGWNVTYVPMMVLRKDIARYDITHEKMMAALADFGQADDRTTFPSYVHS
LWASLAEAFAPCKGGVLSYPNSASDVDRVWAAVGRAVGAAGVVLELSGVMPMPHSVDLLV
GPSQYTVDHPSVSQVMRAGIRTVIPPGVDHAIFASRARSPNPCVVVGYLGRIVAEKSLGL
LARAVELLLQTNMTASCVTFRWVGDGGDAKYYKRYPITLLGSIDDEAALVHELQTWDMAV
QPGLQETFCIANLEVMAMGLPLVTFGVAGVAEYVRHMENAWVVDEISPPALASAIALLVD
DPTLRRRLGHGARRTIETRYTWAHTVAAYDEAYGRLIGHATYKP

Enzyme Prediction     

No EC number prediction in SDRG_02595-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	345	489	1.2e-20	0.925

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340831	GT4_PimA-like	4.37e-32	286	513	131	365	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	6.65e-30	140	518	4	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340842	GT4-like	1.13e-23	310	504	152	355	glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.
340837	GT4_CapM-like	2.10e-22	344	509	190	357	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
395425	Glycos_transf_1	9.16e-22	345	494	4	157	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
AIG55764.1|GT4	2.18e-126	30	505	29	503
QNO55029.1|GT4	1.64e-16	306	517	151	372
QNO55100.1|GT4	1.64e-16	306	517	151	372
ARJ66570.1|GT4	2.16e-16	295	520	177	403
SMX54185.1|GT4	1.68e-15	323	516	202	406

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3C4Q_A	4.24e-09	305	519	183	408	Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A	4.37e-09	305	519	203	428	Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P39862|CAPM_STAAU	1.45e-09	341	510	195	371	Capsular polysaccharide biosynthesis glycosyltransferase CapM OS=Staphylococcus aureus OX=1280 GN=capM PE=3 SV=1
sp|A4QB40|MSHA_CORGB	2.13e-08	305	519	183	408	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain R) OX=340322 GN=mshA PE=3 SV=1
sp|Q8NTA6|MSHA_CORGL	2.13e-08	305	519	183	408	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1
sp|A0QRG8|MGTA_MYCS2	1.01e-07	327	519	179	362	GDP-mannose-dependent alpha-mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mgtA PE=3 SV=1
sp|A5U3B9|PIMC_MYCTA	1.04e-07	324	508	172	360	GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol dimannoside mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=pimC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000420	0.999529	CS pos: 19-20. Pr: 0.9474

TMHMM  Annotations     

There is no transmembrane helices in SDRG_02595-t26_1-p1.