CAZyme Information: RAK75757.1

Basic Information

• Species: Aspergillus fijiensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
• CAZyme ID: RAK75757.1
• CAZy Family: GH128
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
532	KZ824654|CGC2	59922.77	4.7433

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89	12336	1448319	318	12018

• Gene Location: location=KZ824654:169177-170888(+)

Full Sequence      

MLRTFLLLGLTGLVQEAFGKNVYLDWNITWVNAAPNGVERPIIGINGQWPCPQIDVHIGD
NLVVDVYNALGNQSTGIHWHGFHQNYNTFMDGVPDITQCPIKPQQRMRYVIPVNQTGTYW
YHSHQEGQYPDGIRGPIVVHDTAPLPFHYDEEITVTLSDWYNRQMPQLTEDYVYPADGPA
GLEPLPDAVLFNDAVGTKIPVKPNKTYLIHVVCMGNWAGHAFIVEDHDLTVVRADGILVE
PKLATPQYLRMTVGQRLDLLLTTKNDTSRNYAIWDGLDIDEMFIRENREMPEGYNANGTA
WLMYNEDAPFLPSPDIQIHNASLEFLDDVTLTPIDGLPLLEPVSRQIVLDFNYAQVDGVP
TYTINGNTYETPKEPTLYTALSAGSEESLDPSIYGSINQYVVEYGDIVELVINNNHNNLH
PWHLHGHDFQILQRTYPNGGAFNGYGNISAVPSRRDTLMVEPKGHAVLRFKAMNPGIWMF
HCHIEFHVETRLMAVIIEAPDHLQNLSMPADHRDICSGKPSLFAPLPPLPGF

Enzyme Prediction     

No EC number prediction in RAK75757.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	385	1.7e-117	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.40e-68	24	498	4	522	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.
225043	SufI	3.12e-65	36	500	48	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	2.72e-62	346	500	5	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.
215324	PLN02604	4.36e-58	26	487	29	535	oxidoreductase
259920	CuRO_1_Fet3p	3.21e-54	22	140	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS11789.1|AA1_2	1.61e-294	1	530	1	533
CAK42098.1|AA1_2	7.72e-287	1	530	1	547
BCR99488.1|AA1_2	1.18e-264	1	475	1	477
QQK43508.1|AA1_2	1.10e-219	14	520	13	517
QKX61289.1|AA1_2	8.65e-219	6	521	6	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.78e-109	25	516	6	500	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]
1HFU_A	3.86e-56	28	498	11	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	3.94e-56	28	498	11	468	Chain A, Laccase [Coprinopsis cinerea]
2QT6_A	3.51e-55	25	516	7	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
4JHU_A	1.75e-54	25	516	7	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WZB4|ABR1_ASPFU	2.00e-209	10	516	9	518	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
sp|E9R598|FETC_ASPFU	1.44e-146	22	524	23	519	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	9.39e-138	14	516	15	514	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	9.38e-132	6	517	12	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|W3X7K0|PFMAD_PESFW	5.31e-124	14	519	15	510	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000240	0.999739	CS pos: 19-20. Pr: 0.9771

TMHMM  Annotations     

There is no transmembrane helices in RAK75757.1.