CAZyme Information: KGB78848.2

Basic Information

• Species: Cryptococcus gattii VGII
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGII
• CAZyme ID: KGB78848.2
• CAZy Family: GH88
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
619	CP025760|CGC6	70412.36	5.4307

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiVGIIR265	6705	294750	281	6424

• Gene Location: location=CP025760:158337-160572(+)

Full Sequence      

MSVLPPERQGHKAGAGIYYHVDYVGFPRDYKWINTVNPAKTWDQMNIARSFNTTQIWILN
IGTLKPLEMPTEWFLDLAWDFDRWERNSWKRWLREWAAREFGEEWKEEVGDIMGKYSVYA
ARNKAELVNSKSWSLSNYREAEQVLSKWHNLTTRAGQVYDQLPKENQPAFFQLVYMLCAA
QENLNKLHIAVARSTLYAFQAKTAANVFAHEAIEAFYQDANITETFHSLLNRKWDHIWDQ
THINYYTNLEPIRDSLPPIHLVNPFQPSRPGIPLRERDLPGQVAYVRLTVENSLGAWPGD
NVKNCERGYKCPDPILLPMDPWGEQSRWIDIGAGGPKNVSWKMEVDVDWLTVEPRKGKTV
WDGSGDERISVSVNWDKVPVTTKDETVKKEGHIEFSAADRTNVTVTVPIIIPPSPPSSFR
GHVEGDGYVAIEAAHYTRNTSAEGYAFEELEGYGRTLSGLEMFPVSTQNFTLGEGPKLEY
DFWAHGDSMDGKGKVEITVQVGPTLNFLVGKELAFGLQFDNLPPKEIHPVPTRGLGESGS
DRKPGEVGSVPEDWMEVVSNEIRNVTMEVTKDGWEAGKHTVTIWGMTTGVVVERIWVDMG
GIRKRGYSYLGPPESQRVF

Enzyme Prediction     

EC	3.2.1.131:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	3	260	2.1e-98	0.3715925394548063

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
407695	GH115_C	4.34e-61	421	614	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.
406396	Glyco_hydro_115	5.75e-51	4	127	210	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.-.
271342	BACON	6.66e-04	338	407	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
KGB78848.2|GH115	0.0	1	619	1	619
AAW46631.2|GH115	0.0	1	618	257	874
AUB23891.1|GH115	0.0	1	618	459	1076
AFR94258.2|GH115	0.0	1	618	459	1076
UOH84469.1|GH115	0.0	1	618	459	1086

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZMH_A	9.98e-86	7	617	379	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]
6NPS_A	3.49e-51	1	618	390	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	1.23e-34	4	278	390	666	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A	1.23e-34	4	278	389	665	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4C90_A	1.28e-33	7	296	409	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]

Swiss-Prot Hits     

KGB78848.2 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999365	0.000677

TMHMM  Annotations     

There is no transmembrane helices in KGB78848.2.