CAZyme Information: CNAG_03465-t26_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CNAG_03465-t26_1-p1
• CAZy Family: GH16
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
624	CP003827.1|CGC1	68107.15	5.6071

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansH99	8338	235443	1363	6975

• Gene Location: location=CP003827.1:1021759-1024340(+)

Full Sequence      

MRGVVKLFFLSCSLVSLVSSEETGKSPTANYDHYMPKATATIDPSVFALSNDFEITDVPT
TREYTFDITKALASPDGYEREVYVVNNMFPGPVIEANTGDTIIVHVNNHLEEGQSIHWHG
LRQLGTAFMDGVPGITQCPIPPGSSFTYQFTVSHQSGTFWWHSHYSNSMADGIWGPLIIH
SPNEPLQRGRDYDEDRIVFITDWVHDNSEVVIAALATPEGYKGSPAPPQGDAILINGRGQ
TNCTATGSSSCTYPPPPEIHVPVNCRVRLRFISATAHPMYRITIDNHPLEVVETDGTAVY
GPTVHEISIAPGERYSAIINTSEGKEGDAFWLRTSVALGCMFGGIDQVGLAVVRYTGNGM
VSTEEPQTTAWSDLAGATTPCAGLDQTYTLSPRESFSAPREFSQSHVFNSQRGAFVNVYG
NTFQGYGFNNISYQNQIFNPLLSIVQRGGSCESTLVASTTFPDLGSGNIIINNLDGVIDH
PYHLHGNEFQVIGRGTGALSLDNLTNIDFNLDNPVRKDTLWIQGGSWVVLRITTDNPGVW
ALHCHIGWHLTEGKLAVVVIQPGAIGHMEGPESWTNLCANTDPNAFGPARRSPSPSIQSS
KTSTFQYLREVKGKVVKRRGAREA

Enzyme Prediction     

No EC number prediction in CNAG_03465-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	78	553	3.3e-107	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.06e-85	61	553	1	516	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.
259950	CuRO_2_Diphenol_Ox	2.22e-84	196	356	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	4.48e-82	62	561	24	546	L-ascorbate oxidase
259971	CuRO_3_Diphenol_Ox	1.01e-74	407	560	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.
259926	CuRO_1_Diphenol_Ox	3.80e-71	62	180	1	119	The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUB26639.1|AA1	0.0	1	624	1	624
ABI58272.1|AA1	0.0	1	624	1	624
AFR96690.1|AA1	0.0	1	624	1	624
BAG50325.1|AA1	0.0	1	624	1	624
BAG50307.1|AA1	0.0	1	624	1	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.89e-77	50	590	56	571	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
2QT6_A	2.61e-77	68	582	10	491	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
3SQR_A	2.64e-77	50	590	56	571	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]
5LM8_A	2.76e-74	62	578	24	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.83e-74	62	578	25	523	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	0.0	1	624	1	624	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	0.0	1	624	1	624	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	0.0	1	594	1	594	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|A0A067XMP2|PTAK_PESFW	2.28e-74	5	578	1	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q01679|LAC1_PHLRA	2.57e-74	66	578	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
0.001395	0.998576	CS pos: 20-21. Pr: 0.7746

TMHMM  Annotations     

There is no transmembrane helices in CNAG_03465-t26_1-p1.