CAZyme Information: PV10_07334-t45_2-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_07334-t45_2-p1
• CAZy Family: GT22
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
557		62423.44	5.1530

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847524:1666507-1668384(+)

Full Sequence      

MSYFWLLVHAAVIVTSCLDIFAYASPTTRFYDFNITWTVQNPDGLQTRRVISVNGQWPPP
TIEATVGDRIVVNAYNGLVDRSTSLHFHGLYQNGTTHMDGAVGVSQCAIPPGSSMVYNFT
IEQPGTYWYHSHEPGQYPDGLRAPLIVHDPQSPYKDLYTQELVLSVSDWYHQEVSEITKS
FLSVTNPTGAEPVPQSALLNDTLDLQIPVEPSTSYFLRLVNVAAFAGQYIWVEGHSLTII
ELDGVYHKPKKVEMVYLTPGQRVGAILTTKGDRSRNYAITTAMDTELFDLMPEDLKANAT
AYLVYDPERALNDSPTVDSFEPMDDFELIPADEAAVLNNPSQTIVLNVTMDNLGDGVNYA
FFNDITYRAPKVPTLYTVLSASNDLVANPTIYGTHTNTIILEPGGVIEIVLNNNDDGKHP
FHLHGHSFQVLARSEDDAGPWEGNANSTFPTAPMRRDTILLHPNGHLVLRFRSDNPGVWV
FHCHIEWHVQQGLLMTFVEVRTCRWLEYISRLDADNLLIGSPIVVPKLGCASRSFRHVQG
CEGPFCWKRRWQQQRLA

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	48	383	1.9e-142	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	1.04e-79	342	499	2	158	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	1.26e-79	28	499	1	523	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	8.09e-77	1	499	3	546	L-ascorbate oxidase
225043	SufI	1.41e-74	53	500	57	449	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].
259920	CuRO_1_Fet3p	1.62e-70	31	148	3	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
QRC92126.1|AA1_2	9.20e-215	24	543	19	537
QQX29065.1|AA1_2	1.56e-213	31	499	23	490
AEO71107.1|AA1_2	2.28e-213	24	532	30	538
AHZ65140.1|AA1_2	5.07e-213	31	499	12	478
CAE7030771.1|AA1_2	3.35e-212	31	516	27	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.22e-168	28	499	2	479	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	2.27e-70	32	499	7	472	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	1.10e-66	32	499	27	489	Chain A, Laccase [Rigidoporus microporus]
4JHU_A	3.49e-64	32	499	7	466	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5ANH_A	4.88e-64	32	499	7	466	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	8.56e-210	7	499	4	495	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	2.41e-204	24	499	20	496	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|E9R598|FETC_ASPFU	5.31e-201	25	499	19	492	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|P38993|FET3_YEAST	2.80e-167	7	499	5	500	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	4.93e-165	28	543	19	544	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000558	0.999409	CS pos: 24-25. Pr: 0.9352

TMHMM  Annotations     

Start	End
2	24