CAZyme Information: PHYSODRAFT_484143-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_484143-t26_1-p1
• CAZy Family: GH6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
853	JH159152|CGC16	94741.48	6.6442

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159152:8889159-8891965(-)

Full Sequence      

MEAIATLVTLGLGLLYWFCWRPSASATSTNTSVTSSNANAAASSTPTRHREERYAAFVES
EVSANGIVLFVTTGDRVGPFRTLFDALRVKLHVVDLGRTAGGKHVLEALHEKFQEQVEGE
QTEFLFVRGKLVGGSKQLRGLLVEGRKDELGHECDWTHVRVDEKSDTGFMVLSPWNGFQC
VRDVRDDVDMAVKLETRPLHTVEELRNFDATTLIGCSVPIAPRSRQQRRRSKLLVCHDMK
GGYQEDRFKQGCGDFDAYRFYQWDLVDLFVYFGHALVCPPPTGWIAAGHRHGTRVLGTFL
TEGGQGTELCKELFRDVQSAELFASKLAAIAWHGGFDGWLINIENDVLVELVANIDVFLR
TLRKGMKLQNPLAQVVWYGSLSRSGKRKSFVRLDEASTDFFKNVDAFYADYGWVPDDAKF
SAAFELDRRYDVFMGIDVFGRHNMLGGGKMNCGEPLCLAWNSGVSAALFAPGWTHECCQH
EEQEDFVVVESRFWGAVRDSWKVKSPCYDALGGKNCLYSAFNIGRGVGVWAEGRRVGSGT
WSNMTELDVQTTQALHAGSTVTTATGSMKAAICHDMAFQGGSSVQLQGQLVGREKSYFKL
FDVDIEFSPRRIMELSYTTATREESVCLLVLTVCPGLDRATHYVILRSMDDSGPEAGDNR
VDPKKTLSTVAKASLEKHFYLPVSTEFFDVEAVNAEASLGITAGWCKKTYRLGGQLWDQK
HIVEIGMLCTKKLRKVPGEREDYLAYIGEVCVVGNSGKPLAKAVQRDVHSQPQSCKDATL
MSFRRNNADSVSFGVQWGFTVAGAPVRYVLAFARAENGERIFLGKSFDSSLWVESVSWAG
QSSTVVCQLHLEE

Enzyme Prediction     

EC	3.2.1.96:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	239	504	2.9e-63	0.8666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397623	Glyco_hydro_85	9.53e-95	251	526	1	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
119364	GH85_ENGase	5.10e-87	234	552	1	330	Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.
227068	COG4724	1.66e-28	250	619	94	479	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHN91514.1|GH85	2.08e-73	198	633	21	448
CAE5966838.1|GH85	1.61e-71	198	625	30	450
VDC78376.1|GH85	2.09e-71	230	631	65	454
NP_196165.3|GH85|3.2.1.96	2.17e-71	198	645	25	466
AED90876.1|GH85|3.2.1.96	2.17e-71	198	645	25	466

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FHA_A	4.37e-19	250	608	71	441	Chain A, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_C Chain C, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
3FHQ_A	4.37e-19	250	608	71	441	Chain A, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_F Chain F, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
2VTF_A	1.02e-18	250	608	76	446	X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae],2VTF_B X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|F4JZC2|ENAS1_ARATH	3.86e-72	198	645	25	466	Cytosolic endo-beta-N-acetylglucosaminidase 1 OS=Arabidopsis thaliana OX=3702 GN=ENGASE1 PE=1 SV=1
sp|Q9SRL4|ENAS2_ARATH	4.88e-69	217	544	54	373	Cytosolic endo-beta-N-acetylglucosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=ENGASE2 PE=1 SV=1
sp|P0C7A1|ENASE_CHICK	1.47e-64	216	600	105	474	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
sp|Q8BX80|ENASE_MOUSE	8.64e-62	196	617	72	491	Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
sp|Q8NFI3|ENASE_HUMAN	1.20e-60	199	617	87	499	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.884376	0.115630

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_484143-t26_1-p1.