CAZyme Information: KIS66120.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS66120.1
• CAZy Family: AA5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
710	CM003159|CGC2	78251.20	6.7884

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003159:199358-201490(+)

Full Sequence      

MRLSLVSLALLGLAANHALAFPASLGDVKRNTDHAPYFDTDKSALDPDLTLGPDMLGSDD
VDEFVRRIDQVLQSYEPDLSSFGLGPVPGFWPGHRHGDAHNHGPPHAHEDGHKDQGHQVP
GSRPINGKPPKDTCKPKPPSGVSHKCEKRDFTPQTREFDWTITYGHSAPDGFLKKRILVN
GQSPGPLIEANEGDTIVVKVRNLLDQGTSIHWHGMFQNSTPFMDGIAGFSQCPIPPRGHL
TYRFKIEGQYGSYWWHSHSKMQYTDGLYGGLIVHSKRDPYQKCRDYDDERVFLFADNYHD
FADYIVQQLLSANGYNGTAAAPSPQSGLINGAGQFNCAALAHAKGKQPGMPTRCTQLPTP
TMDVEPNKKYRFRFINTGSHAQHIISIDNHELEVIAADGTPVKPHKVHRVPIHNGQRHDV
FVDTNQGSDGDSFLLRSAMMTACFSFVDPLLDPVANLTLQYRLPGSKIAPKRPVPHDWKD
AMGSQCQDLKDSELVPAIDTSVPPNHNLGSLGIFNSQFGNLQLANGTTLGRFFVDNVTQT
NYVNKPYLEVTHAGGQINSSTVASLLIPDDVWVADIVINNEDSFLDHPFHLHATDMHIVA
RGSGSMTQAQWIALNQNAQPQNGNASALNLKNPLRRDTITVPRSSFVVVRIIPDLPGVWA
MHCHIAMHVAEGLMAAIAIHPHKIRELKFSQEVLDLCLVSRAALNEVEPA

Enzyme Prediction     

No EC number prediction in KIS66120.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	174	673	4.6e-105	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	7.04e-79	290	461	1	163	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.
274555	ascorbase	5.52e-77	155	687	1	531	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.
259926	CuRO_1_Diphenol_Ox	8.72e-74	156	274	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	1.56e-73	512	679	2	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.
177843	PLN02191	2.31e-69	156	673	24	540	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDU22960.1|AA1	0.0	1	710	1	708
CBQ70903.1|AA1	0.0	1	710	1	733
SJX65928.1|AA1	0.0	1	710	1	753
CDI56287.1|AA1	0.0	1	710	1	688
SAM64516.1|AA1	0.0	1	710	1	778

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.66e-62	153	695	18	519	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.69e-62	153	695	19	520	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	5.46e-61	153	695	46	547	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	1.53e-60	150	673	60	536	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	2.91e-60	150	673	60	536	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	1.32e-123	153	697	59	578	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	1.76e-122	153	697	59	578	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	1.50e-120	153	697	59	578	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	7.74e-71	147	697	56	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.41e-62	147	673	65	545	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000220	0.999756	CS pos: 20-21. Pr: 0.9833

TMHMM  Annotations     

There is no transmembrane helices in KIS66120.1.