CAZyme Information: PV10_03450-t45_3-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_03450-t45_3-p1
• CAZy Family: GH13|GH13
• CAZyme Description: hypothetical protein, variant 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
463		50471.96	4.2225

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=KN847521:4728056-4729607(-)

Full Sequence      

MPGLIASFLSVTNPTGAEPVPQAALMNDTQNLEIHIEPGKTYFLRIINMAAFAAQYFWID
GHTFRIIEVDGVYHEPTEAEQIYLTAAQRYGVLLTTKNETDANYAIMGSMDEDLFDQIPD
GLNPNVTSYLVYDSALPLPEPADIDEFDPFDDMLLVPTDGEELLPDPDLVVTLDVVMDNL
GNGANYAFFSGITYVKPKVPSLYTALTSGEYATNASIYGVNTHSYVLEHNEVVEIVLNNQ
DPGKHPFHLHGHAFQSILRSEEEAGDFDPESVTNGSVVLPQKPMRRDVLLVRPNGHIVMR
FRANNPGVWLFHCHIEWHVDSGLVMTFVEAPLVLQQTITIPEDHFAACAALSPPMATAGN
AAANTVDLLDLQGQNLSPAPLPSGFQAKGIVALTFSCLAGLIGVGVIAWYGMGEMTNLEK
ERQVDHVMHIQDERGIVKTESATGSVGGPDAGVGVRDTIETAR

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	4	210	2.9e-81	0.6112759643916914

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	4.31e-84	168	331	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.
259945	CuRO_2_Fet3p_like	6.25e-70	1	134	15	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.
400194	Cu-oxidase_2	1.79e-42	194	331	1	136	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
225043	SufI	5.67e-42	12	331	181	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].
259977	CuRO_3_MCO_like_4	1.46e-37	182	329	13	166	The third 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 oxidize 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 subfamily of MCOs is composed of three cupredoxin domains. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92126.1|AA1_2	3.76e-194	1	412	169	576
USW53459.1|AA1_2	5.79e-190	1	419	169	585
UDD60384.1|AA1_2	2.81e-188	1	425	168	590
BAE61606.1|AA1_2	3.93e-188	1	425	178	600
AEO71107.1|AA1_2	1.99e-186	1	411	180	587

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	8.75e-132	4	384	150	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	6.02e-32	34	329	188	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	5.44e-30	13	329	183	489	Chain A, Laccase [Rigidoporus microporus]
1HFU_A	8.56e-30	34	329	187	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	8.64e-30	34	329	187	468	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	9.34e-187	1	416	168	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	4.27e-177	4	414	171	578	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.62e-166	1	411	170	576	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	1.56e-145	4	443	171	612	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	3.21e-145	4	433	171	602	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000006

TMHMM  Annotations     

Start	End
390	412