CAZyme Information: QRC91053.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRC91053.1
• CAZy Family: AA3
• CAZyme Description: Glycoside hydrolase family 93 protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2ES79]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375	CP069023|CGC8	41082.31	5.3317

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

Full Sequence      

MLLSTLVMSLISVVSALPQQQQVQPTFSQKVIFTPPSDYTDPRVLYARSAQLADGTLLAT
WENYSPEPPKVWFPIFQSKDGGNTWSELSRVQDTQQNWGLRYQPFLYVLENDFPGYAKGT
VLLAGSSIPTDLSQTQIELYASKDSGATWEFVSHLAAGGEARPNNGLTPVWEPFLMEYKG
TLIHYYSDQRDNATHGQKMVHQTSSDLKTWGPVIDDVAYPTYTDRPGMPTVALLPNGKYI
MSYEYGGGPAIPSSYQFPVYYKIVDDPEQFGPATGISLKATDGTVPSGSPYVVWSSVGGA
NGTIIVSAHSGGDIFINKGLGEGPWVKVATPERSHYTRHLRVLADPTKLLIMGGGQLPPS
TTNKVQFSVMDISNL

Enzyme Prediction     

EC	3.2.1.-:5

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH93	42	352	9.4e-111	0.993485342019544

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
271234	Sialidase_non-viral	1.73e-04	51	250	152	329	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
271234	Sialidase_non-viral	0.005	50	149	20	125	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
271234	Sialidase_non-viral	0.009	50	161	205	305	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
350098	GH43-like	0.010	135	243	46	150	Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC91053.1|GH93	QRC91053.1|GH93	1.91e-282	1	375	1	375
CBX91309.1|GH93	CBX91309.1|GH93	9.31e-208	3	373	3	375
CAE7032166.1|GH93	CAE7032166.1|GH93	3.59e-206	1	373	1	379
AEO67494.1|GH93|3.2.1.-	AEO67494.1|GH93|3.2.1.-	2.83e-205	4	375	4	376
AEO55492.1|GH93	AEO55492.1|GH93	1.37e-193	4	375	4	378

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YDT_A	2YDT_A	3.86e-151	26	375	10	364	Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],5M1Z_A Chain A, Exo-1,5-alpha-L-arabinofuranobiosidase [Fusarium graminearum]
2W5N_A	2W5N_A	5.48e-151	26	375	10	364	Chain A, Alpha-l-arabinofuranosidase [Fusarium graminearum]
3A71_A	3A71_A	2.07e-150	32	375	11	354	High resolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum]
2YDP_A	2YDP_A	3.15e-150	26	375	10	364	Chain A, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_B Chain B, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum],2YDP_C Chain C, Exo-1,5-alpha-l-arabinofuranobiosidase [Fusarium graminearum]
2W5O_A	2W5O_A	8.44e-148	26	375	10	364	Chain A, ALPHA-L-ARABINOFURANOSIDASE [Fusarium graminearum]

Swiss-Prot Hits     

QRC91053.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000268	0.999705	CS pos: 16-17. Pr: 0.9831

TMHMM  Annotations     

There is no transmembrane helices in QRC91053.1.