CAZyme Information: KAA8915962.1

Basic Information

• Species: Trichomonascus ciferrii
• Lineage: Ascomycota; Saccharomycetes; ; Trichomonascaceae; Trichomonascus; Trichomonascus ciferrii
• CAZyme ID: KAA8915962.1
• CAZy Family: GH88
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
589	SWFS01000129|CGC1	67692.54	6.2947

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=SWFS01000129:40672-42441(+)

Full Sequence      

MTSFKRCVLVGLICLGSLLTLFVVEDFFQFQIRDWGLRDVEVEVDSDGQRTLKYEWHIAR
HTLPLDGVEKKMILVNGMFPGPTIHGKVGDRVIVNVHNDLEGEETTSVHWHGIKQRGSNA
MDGAVGVTQCGIPSGDNLTYSFDLDEPGTYWWHSHVGTQRLDGMFGGLIVKGGDEHYSEI
NNSYDEEVVVILSDHYHRSGERVLQWYLSRSSGGQEPVPSNGFINGQNVYDCERFMDTEL
TCIPKVGRHAHFEFHKNKRYRVRIINASAMANFRFSIDEHEFQVIEADSIEIEPVKAHYI
PISSGQRYSAIVHTENKNRNSFFMRAEMNQECFNYKNEELDPEIKGVITYKSNTFKDLLK
SRESIPSSKKWEDIMSFDMCLDMDERTLQPLTHLDAPEPDQTVVVWTKIVQLHQNNLAPY
AYFNRTSWAPSIGAPNLHVELGLVNASMGPKSTKKWGGKQMVVDIEPENVVQLIISNGDE
SPHPFHLHGHDFWIVKIYEPPKGYIHGQWDPDEHHEYKTNNPIRRDTFTVPRFGHAVIRF
KADNPGIWAFHCHILWHLTTGMMMQFNQNHISEKIPQIMLDQCSQMRTL

Enzyme Prediction     

No EC number prediction in KAA8915962.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	68	562	1.6e-110	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.68e-84	54	579	4	536	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	7.82e-76	35	576	7	555	L-ascorbate oxidase
215324	PLN02604	2.46e-66	50	568	23	546	oxidoreductase
259953	CuRO_2_MCO_like_1	7.67e-66	188	350	1	162	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.
225043	SufI	7.21e-65	75	566	57	446	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
CCE81319.1|AA1	4.80e-196	44	589	47	607
AYO41925.1|AA1	9.41e-112	46	564	73	661
AXA49146.1|AA1	1.86e-111	46	564	73	661
AGO04566.1|AA1	1.61e-110	49	577	57	586
AOW00922.1|AA1	2.92e-110	46	566	143	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	5.37e-78	53	565	25	501	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.50e-78	53	565	26	502	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.47e-77	53	565	53	529	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
1ZPU_A	1.03e-69	51	562	2	473	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]
3V9E_A	5.85e-67	51	584	67	562	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|I1RMG9|FET3_GIBZE	2.28e-82	51	584	24	516	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|K7NCS2|FETC_EPIFE	1.28e-80	51	583	22	514	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	1.31e-79	42	589	13	517	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
sp|Q55P57|LAC1_CRYNB	3.19e-75	46	563	56	555	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	8.94e-74	46	563	56	555	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999626	0.000416

TMHMM  Annotations     

Start	End
7	24