CAZyme Information: KAE8541912.1

Basic Information

• Species: Cryptococcus cf. gattii
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus cf. gattii
• CAZyme ID: KAE8541912.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
642		69850.05	6.0255

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=CM018865:935391-941189(+)

Full Sequence      

MKGASGGSGVSDNVGIWKRYSLLEVRDPALTVLLGRNVPVGPQSGIGENIGKLPTATIDP
SVFALSNDFEVSDVPTTREYTFDISKALASPDGYEREVYTVNNMFPGPVIEANTGDTIIV
HVNNHLDEGQGIHWHGMRQKNTPYMDGVPGITQCPIPPGGSYTYNFTISDQSGTYWWHSH
YSNAMADGLWGPLIVHSVHEPIQRGRDYDEDRIVFVSDWMHDDSEIIIAALATPAGYKGS
PAPPQGDAILINGRGQTNCTATNSSSCYYPSPPEIHVPVNSRVRLRFISATAHPMYRISL
DNHPLEIVETDGTAVYGPTVHEMSIAPGERYSAIINTSEGKEGDAFWLRTSVALGCMFGG
VPQVGLAVVRYTGNEMTTTAEPQSYAWSDLANATARCAGLDQTYTLSPREKESCRVSRAS
SQSHIFNSQRGAFVNHLGNTFQGYGFNNISYQNRIFNPLLSIVQRGDPYESTLVASTTFP
DMGVGAIIINNLDGPIDHPYHLHGNEFQVIGRGTGALSLDNLTNIEFNLDNPVRKDTLWI
QGGSWAALSIVTDNAGVWALHCHIGWHLTEGKLAVVVVQPNAVGQIACPESWTNLCANTD
PNAFGPARRSPSPSIQSSKTSVFQHLREVKGNVVKRRGAREA

Enzyme Prediction     

No EC number prediction in KAE8541912.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	94	571	9.9e-104	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.11e-85	77	571	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.
177843	PLN02191	6.34e-83	78	586	24	554	L-ascorbate oxidase
259950	CuRO_2_Diphenol_Ox	3.13e-82	212	372	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.
259926	CuRO_1_Diphenol_Ox	1.69e-75	78	196	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.
259971	CuRO_3_Diphenol_Ox	3.31e-67	425	578	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAG50347.1|AA1	0.0	46	641	19	614
BAG50356.1|AA1	0.0	48	642	21	615
BAG50355.1|AA1	0.0	48	642	21	615
KGB76306.2|AA1	0.0	48	641	78	670
ACB05902.1|AA1	0.0	48	641	21	613

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.76e-70	66	608	56	571	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.76e-70	66	608	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]
5EHF_A	3.90e-67	84	596	10	486	Laccase from Antrodiella faginea [Antrodiella faginea]
5LM8_A	6.69e-67	78	596	24	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.84e-67	78	596	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|Q55P57|LAC1_CRYNB	0.0	44	642	28	624	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	0.0	48	642	21	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|J9VQZ4|LAC2_CRYNH	4.81e-314	48	612	21	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|J5JH35|OPS5_BEAB2	5.63e-72	70	571	66	544	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	9.77e-72	78	596	65	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000063	0.000002

TMHMM  Annotations     

There is no transmembrane helices in KAE8541912.1.