CAZyme Information: KAA8902223.1

Basic Information

• Species: Trichomonascus ciferrii
• Lineage: Ascomycota; Saccharomycetes; ; Trichomonascaceae; Trichomonascus; Trichomonascus ciferrii
• CAZyme ID: KAA8902223.1
• CAZy Family: GH10
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625	SWFS01000470|CGC1	70517.88	4.8621

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TciferriiCBS4856	6909	N/A	6	6903

• Gene Location: location=SWFS01000470:33083-34960(+)

Full Sequence      

MVRDEGVEYEQLPLYDMTEEGPVAKDDPLSHERIRRPWGRTTSRFLIGLIVTLVITLLGL
LIIPGPHHRSIRFGGSEKEALEQVSRTVYGRELKDWQLDTSREYHLSRDWDSDAPPTVRE
YNFTISEVIAAPNGVQKKMTVVNGQFPGPLVEANEGDRIIVHVTNEGSEPTSLHFHGMHQ
NGTNHMDGATAITQCPIQPGKSFTYDFTVKGQWGTYWYHSHYSTQYVEGFAGPFIIHSKE
EEKLMDPYDEDVVIFLSDLYHDSSFDLLDKYIAPGVENQEPIPDSGLIQGTNYFACSRLG
DDKKYNCNQQDAERAVIPVMEDKTYRFRLISAGAFSEFDFSIDDHVLTVVEADGTNTEPL
NVETVRLSNAQRYSVLVKTKSNPDNDGFWLRASMNTYCYDGENPNLDANLKAVFSYPELT
QKIIDNNGHINEAHQPQTNKSRELDGSIRCQELDPSLLVPALAIEAPPADEFITIDASFQ
IGARAISRGYFNDSTYFPTAGIPNLQKLHDAAKTSNQSILLPDTSTPAWADNQFIVTIDK
PKVIDLLINNYDDGAHPFHLHGYKMWELAHGQGYYEPEMYSTINSTNPIRRDTVQMSKLT
QPYTALILTNTLTSKIRLVPGPLRR

Enzyme Prediction     

No EC number prediction in KAA8902223.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	135	598	3.1e-102	0.8938547486033519

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259926	CuRO_1_Diphenol_Ox	8.15e-74	119	237	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.
259953	CuRO_2_MCO_like_1	4.96e-65	252	417	1	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is 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	3.88e-64	118	606	1	493	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.
259920	CuRO_1_Fet3p	2.54e-57	119	237	1	121	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259869	CuRO_1_LCC_like	3.17e-55	119	237	1	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANB14070.1|AA1	1.61e-199	87	554	90	560
AOW00922.1|AA1	2.63e-156	90	596	118	622
QNP95316.1|AA1	3.72e-156	90	596	118	622
QKX53525.1|AA1	3.07e-139	96	596	84	572
CDR40204.1|AA1	2.66e-133	8	596	5	601

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	3.48e-63	104	600	7	463	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.56e-63	104	600	8	464	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.20e-62	104	600	35	491	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3KW7_A	2.42e-60	122	594	7	431	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
1ZPU_A	3.33e-57	121	594	5	439	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	2.97e-72	104	594	47	520	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	3.02e-71	104	594	47	520	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	4.15e-68	114	594	20	456	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|J9VQZ4|LAC2_CRYNH	3.28e-66	106	596	49	522	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|E9R598|FETC_ASPFU	3.16e-65	121	594	25	452	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999997	0.000015

TMHMM  Annotations     

Start	End
45	67