CAZyme Information: KEF56266.1

Basic Information

• Species: Exophiala aquamarina
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
• CAZyme ID: KEF56266.1
• CAZy Family: GH154
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
636	AMGV01000006|CGC3	69437.02	4.3243

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918	13118	1182545	0	13118

• Gene Location: location=AMGV01000006:1355943-1358181(+)

Full Sequence      

MALSLSSFLTASILLLTSFVAAETRTYDFSIGWVIRNPDGQKDRPVIGINGEWPIPKIEV
NIGDRLVVNVKNDLGNQSTSLHWHGMYQNGTNHMDGVAQGTQCQIAPGASFTYNFTINQP
GTYWYHSHVGGQYPDGLRGPLIVHDPKNPYEDQFDEELILTLSDWYHEQMPPLIAKFLSV
TNPTGAEPVPQSALMNDTQGLQILIQPGKTYFLRIVNMAAFAAQYFWIDGHTFRIIEVDG
VYHEPAEASLLYITAAQRYGVLLTTRTETDVNFAIMGSMDQDLFDQIPDGLNPNVTSYLV
YDDSLPMPEAAEIAEFEPFDDMELVPTDGEELLPDPDLVVQLDVLMDNLGDGANYAFFSG
ITYVAPKVPSLYTALSAGEFATNASVYGTNTNSFVLDHHSVVEIVLNNQDPGKHPFHLHG
HAFQTILRGEEESGDFDPESVANGSVVYPTTPMRRDVILVRPNGHIVMRFRADNPGVWVF
HCHIEWHVDSGLIMTFVEAPLVLQETLTIPEDHFAACAAVSPPVPTIGNAAANTEDYLDL
TGQNMPSGPLPSGFKAKGIVALTFSIIAGLLGVAVIAWYGFGEMSQIEKDRQVSHVQHIA
ADRGVVSRSNTDASGLLAGDAANGGAASDTISSVAR

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	379	7.3e-150	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	4.01e-84	2	500	13	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].
259966	CuRO_3_Fet3p	4.12e-82	337	500	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 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.
274555	ascorbase	8.57e-78	24	499	1	524	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.
259945	CuRO_2_Fet3p_like	3.76e-76	156	303	1	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	7.31e-72	8	498	7	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92126.1|AA1_2	1.66e-279	1	580	1	575
AEO71107.1|AA1_2	1.36e-272	21	581	31	588
QOX58957.1|AA1_2	4.24e-271	21	583	22	578
USW53459.1|AA1_2	6.97e-271	16	588	15	585
UPK89259.1|AA1_2	7.38e-271	7	586	7	582

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.36e-187	23	553	1	534	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]
3KW7_A	5.34e-77	28	539	7	498	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]
1V10_A	7.73e-71	4	498	3	489	Chain A, Laccase [Rigidoporus microporus]
5LDU_A	8.81e-71	28	517	7	488	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
3FPX_A	1.23e-70	28	517	7	488	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	1.15e-262	14	585	6	577	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|K7NCS2|FETC_EPIFE	9.64e-262	5	583	7	578	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.97e-256	11	581	11	577	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|Q96WT3|FET3_CANGA	6.89e-205	13	588	5	590	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|P38993|FET3_YEAST	9.80e-200	18	584	17	586	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000318	0.999640	CS pos: 22-23. Pr: 0.9805

TMHMM  Annotations     

Start	End
559	581