CAZyme Information: KAE8541911.1

Basic Information

• Species: Cryptococcus cf. gattii
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus cf. gattii
• CAZyme ID: KAE8541911.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
598		66214.58	5.8867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccf.gattiiMF34	6321	N/A	114	6207

• Gene Location: location=CM018865:931918-934500(+)

Full Sequence      

MREVIKFFFLSCSFISLAYSQKTGTLSTSLSDRSGVPQETATIDPRVFVLSDEFLITNVP
TTREYTFNITKALASPDGYEREVIAINGMFPGPVIEANTGDTIIVHVNNGLEEGQGLHWH
GLRQKGTALMDGVPGITQASIFGQDSSFTYKFTITDQFGTYWWHSHYSNSMADGLFGPLI
VHSVDEPIQRGRDYDEDRIVFVTDWMHDDSETIINALLSPEGYRGSTGAPQGDSVLINGL
GRTNCTDTGSPSCTNPPFPEIPVPVNSRIRLRFISGSSHVFYRMSLDNHTLEVVETDGTG
VYGPMLHEVSISSGERYSALINTFDGQVGDAFWLRATSGLGCSKHGFPQVGLAIVRYTGR
GNVTTDEPQTRAWRQGQMFHVLGLTKLILLMRRPRIRRDASQTVLQSHVLNSQLGAFVDV
FGKSFQGYGFNNVTYQNQINNPLLRVVQGGGSCNSTLITNATFPDLGEVNIILNNLDANI
PHPYHLHGNEIQLLARGNGSLTLDDLPYINLNLDNPPRKDTFWMEGGSWVVMRLVTDNPG
VWALHCHIGWHLAKGKLAVVVVQPEEIEQIRWPQPWLDLCNGTDPNAFGPGRRSFLDP

Enzyme Prediction     

No EC number prediction in KAE8541911.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	79	555	1.5e-95	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.82e-77	62	571	1	529	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259971	CuRO_3_Diphenol_Ox	1.78e-75	409	562	3	158	The third cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259950	CuRO_2_Diphenol_Ox	3.13e-72	198	358	1	164	The second cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	5.91e-69	63	563	24	546	L-ascorbate oxidase
215324	PLN02604	5.07e-64	62	570	24	551	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
KGB76308.2|AA1	0.0	1	595	1	594
AFR96688.2|AA1	3.17e-310	1	594	1	592
AUB26637.1|AA1	3.17e-310	1	594	1	592
UOH83094.1|AA1	1.71e-298	1	594	1	592
BAG50325.1|AA1	6.92e-298	1	594	1	592

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	6.78e-69	57	598	20	544	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.93e-69	57	598	21	545	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.49e-67	57	598	48	572	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	3.69e-67	56	590	61	569	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	7.15e-67	56	590	61	569	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	5.62e-311	1	594	1	592	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|J9VY90|LAC1_CRYNH	1.00e-297	1	594	1	592	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	1.08e-287	1	594	1	592	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|Q12542|LAC2_AGABI	1.99e-64	48	590	7	517	Laccase-2 OS=Agaricus bisporus OX=5341 GN=lcc2 PE=1 SV=1
sp|Q01679|LAC1_PHLRA	2.77e-64	67	580	29	509	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001419	0.998573	CS pos: 20-21. Pr: 0.9510

TMHMM  Annotations     

There is no transmembrane helices in KAE8541911.1.