CAZyme Information: CNL06210-t26_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CNL06210-t26_1-p1
• CAZy Family: GT4
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
874		99866.54	4.7867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansJEC21	7004	214684	372	6632

• Gene Location: location=AE017352.1:715817-719039(-)

Full Sequence      

MGISPFYFWSDVPIPHHSTIAILKNMSLSHGEPTVKYRGLFINDEHPALWGWAAEKWNRD
PWEPAFQVEMYELWFEMMLRLKANYFWPAMWASKFSVDGLDITNGLPRPAIPGPNQILAN
KMGIVMGTSHHEPMSRNKPEWDVFGKGPWDWTNKDVLKDFWRYGAERAKGVETLFTMGMR
GDGDEPLTDASNELVQNITKVQQDILKEVYDTDDLEGSGVSQMWCMYKEVAGYYKNGLEV
PDDVTVLFADDNYGNIMSVLPPERQGHKAGAGIYYHVDYVGFPRDYKWINTVNPAKTWDQ
MNIARSFNTTQIWILNIGTLKPLEMPTEWFLDLAWDFDRWERNSWKRWLREWAGREFGDE
WKEEVGDIMGKYSLYASRNKAELVNSKSWSLSNYREAERVLTEWQDLTTRAGMVYDQLPK
ETQPAFFQLVYMLCAAQENLNKLHIAVARSELYAFQAKTAANVFAHEAIEAFYQDANITE
TFHSLLNRKWDHMWDQTHINYYTNLEPIRDSLPPIHLVNPFQPSRPGIPLKERDLPGQIG
YVRLTVENSLGAWPGDNVRNCERGYKCPDPTLLPMDPWGEQSRWIDIGAGGPKNVSWKME
VDVDWLTVEPRKGKTVWDGSGDERVWVSVDWDKVPASTKGERVEKEGHIEFSAADRTNVT
VSVPIIIPPSPPSSFRGHVQGDGYVVIEAVHYTRNTSEEGYAFEELEGYGRTLSGLEMFP
VTTQNFTLGKGPKLEYDFWTHGDSVDGNGKVEITVQVGPTLNFLIGEELAFGLQLDDLPP
REIHPVPIKGLGESGSDRNSGEVGSVPKDWMEVVSSEIRNVTMEVTKDDWEAGRHTVTIW
GLTTGVVVERIWVDMGGIRERGYSYLGPPESKRV

Enzyme Prediction     

EC	3.2.1.131:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	1	514	1.1e-199	0.6829268292682927

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
406396	Glyco_hydro_115	1.25e-165	31	383	1	334	Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
407695	GH115_C	7.24e-59	677	870	1	172	Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
271342	BACON	0.007	594	663	25	80	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAW46631.2|GH115	0.0	1	874	1	874
AUB23891.1|GH115	0.0	1	874	203	1076
AFR94258.2|GH115	0.0	1	874	203	1076
UOH84469.1|GH115	0.0	1	874	203	1086
ADV21474.1|GH115	0.0	1	865	203	992

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZMH_A	6.48e-161	1	873	137	935	Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
4C90_A	4.93e-102	1	552	164	694	Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
6NPS_A	8.33e-98	1	874	134	966	Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]
7PUG_A	1.39e-94	1	552	137	679	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A	6.84e-92	1	552	136	678	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]

Swiss-Prot Hits     

CNL06210-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000075	0.000000

TMHMM  Annotations     

There is no transmembrane helices in CNL06210-t26_1-p1.