CAZyme Information: I302_06892-t42_1-p1

Basic Information

• Species: Kwoniella bestiolae
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella bestiolae
• CAZyme ID: I302_06892-t42_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
627		69603.80	4.5534

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KbestiolaeCBS10118	9270	1296100	137	9133

• Gene Location: location=KI894023:1499035-1501909(-)

Full Sequence      

MRNLFTILSILSLAPFLILAQEIDPDTNQEVASDLDSLWGGALADISGSNSSTDPLPQRW
ARTEYQSFILSNDFEITDQPIYTINGQFPAPVIEVNTGDTVRVHVRNSLDIPQTIHWHGI
SQNGTNIMDGVPGITQCPIPPGSNFTYEFPIVEQYGTYWYHSHFANTMADGIAGAFIVHN
PNDPLKRGRDYDEERILLIQDWMWDQSTDIVAALKSREGYRGSPGAPKGDSILINNVGQT
NCSGPNYPQGAECNLPKLPEIPVIVGKKTRIRIINTGAHSMLRISIDQHELEVAEVDTDP
VLGPTIHEIPVAPAQRYSIIVDANQGQAGDKFWLRANVAVGCMDKVRQEAFAVFRYTNNN
EQYDDGDEVPDTQAWDDLAAFDSPCRDLDDQYTLTPRDPIDAFTKPLQTHALSSKFGTFL
GVKGQNITGFAFNNISFQNQIWDPMLPHVIDSGNYSVENVAQVVFDCDGYVDLILNNLDG
GIDHPYHLHGNEFQVIKRGNGNLTVEEAQAMDLSNITNPLRRDTIFIPGNAYAILRIRTD
NPGVWALHCHIGWHLAVGKLATMVVRPDDIKSFEQPEDWKGLCAGQDTDEEGPARRSLDS
PTSPAGHLQSLREVKNRVITRTGPRDV

Enzyme Prediction     

No EC number prediction in I302_06892-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	78	558	4.8e-105	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.92e-74	80	558	21	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	1.98e-69	195	357	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	6.95e-69	81	558	44	539	L-ascorbate oxidase
259971	CuRO_3_Diphenol_Ox	3.16e-67	412	565	4	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.
225043	SufI	7.35e-63	80	567	53	450	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAG50345.1|AA1	5.64e-209	37	626	16	623
AXA19842.1|AA1	5.64e-209	37	626	16	623
AXA19815.1|AA1	5.64e-209	37	626	16	623
AXA19843.1|AA1	5.64e-209	37	626	16	623
AXA19803.1|AA1	5.64e-209	37	626	16	623

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.58e-66	83	574	90	558	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	2.58e-66	83	564	90	541	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	1.34e-65	54	587	15	526	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.37e-65	54	587	16	527	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	4.69e-64	54	587	43	554	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55P57|LAC1_CRYNB	2.85e-209	37	626	16	623	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.86e-207	56	626	35	623	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	9.10e-198	52	598	31	593	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|K7NCS2|FETC_EPIFE	1.56e-71	70	594	23	525	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|W3X7K0|PFMAD_PESFW	7.26e-69	79	608	41	532	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000319	0.999653	CS pos: 20-21. Pr: 0.9801

TMHMM  Annotations     

There is no transmembrane helices in I302_06892-t42_1-p1.