CAZyme Information: I317_05467-t43_1-p1

Basic Information

• Species: Kwoniella heveanensis
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella heveanensis
• CAZyme ID: I317_05467-t43_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
698		76021.62	4.6031

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KheveanensisCBS569	8002	1296119	131	7871

• Gene Location: location=KV700219:16932-20059(+)

Full Sequence      

MRIALSLAVLLASAPWPSVAQTTSAAPGASLENIFDIIRNFGRQQSSSISTSPSPTVTST
SSDPSAVPGSTESTTSPVQSGSSTVAAVEATASTIDAPPLPTNTATRDPNTFILSNDWDV
DAEPQVREFNFEIGTAAANPDGYTRQVYTINGQFPAPLIEANTGDTIVAHVKNSLPDGQT
IHWHGITQNGSNHMDGVPGVTQCPIPPGGTFTYKFEIIEQYGTYWYHSHFGNTMADGIVG
PLIIHSKDEPLKRGQDYDEERILIVTDWMHDQSADVVKALKSPEGFRGSPAAPRGDSILI
NGIGQTNCSSIHYPKDAACEPPAWSEMTLPANKKVRIRIINSAAHTLFRISLDEHEFDVV
EADTDPINAVTIRELPIAPAQRYSIIVSTDVGEPGDKYWLRLHAAIGCLDGVMDPQTAQG
IIRYAGEDGAGQNDTSEPTTQPWNDLAAMDAECRDLDELYELHPMEVIDAYETPSETRVL
SSQFGTFLGAKGQNITGFAFNNVTFQNQIYNPVLSQVEKEGNFSSPYVASIEFTTSSYAD
IVINNLDGFLSHPYHLHGNEFQLIARGDGNVTAEEVEAMGLQIANPLRRDTIFIPANTYA
VLRVKMDNPGVWAVHCHIGWHLAIGKLATIIVRPDDIRNFEQPDDWKGLCTGHPDEEGPA
RRSISLPPTTSLESRSSFSRSLKETKNSVIRRQGPRDV

Enzyme Prediction     

No EC number prediction in I317_05467-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	143	625	9.2e-108	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.42e-81	126	625	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	6.31e-78	122	625	19	539	L-ascorbate oxidase
259926	CuRO_1_Diphenol_Ox	2.25e-69	127	245	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	8.13e-69	477	632	1	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.
215324	PLN02604	2.35e-68	122	625	20	539	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UOH83094.1|AA1	2.68e-215	100	698	35	624
BAG50307.1|AA1	1.53e-214	100	698	35	624
AUB26639.1|AA1	3.06e-214	100	698	35	624
ABI58272.1|AA1	3.06e-214	100	698	35	624
AFR96690.1|AA1	3.06e-214	100	698	35	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	6.38e-78	126	650	23	522	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.54e-78	126	650	24	523	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3SQR_A	5.10e-77	113	641	54	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	5.10e-77	113	641	54	558	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.50e-76	126	650	51	550	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|J9VY90|LAC1_CRYNH	5.44e-215	100	698	35	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	2.86e-212	100	698	35	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	1.53e-209	100	665	35	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	1.67e-77	126	644	73	563	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	2.07e-77	126	653	64	575	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 SP

Other	SP_Sec_SPI	CS Position
0.000222	0.999744	CS pos: 20-21. Pr: 0.9832

TMHMM  Annotations     

There is no transmembrane helices in I317_05467-t43_1-p1.