CAZyme Information: QRD07544.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRD07544.1
• CAZy Family: GT57
• CAZyme Description: Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:A0A7U2NRB1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553		59318.31	6.7138

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069044:957519-959488(-)

Full Sequence      

MFRLLLAAVYASLVCSKTVSYDFSIGWVTAAPDGYARPVMGVNGQWPIPTIEADMGDTIV
VTAHNNLGNETTSLHFHGMFQKGSGIYDGATAITACPIQPGDSYTYSFVANPAGTHWYHS
HDKGQYPDGLRGKMIIHDRNWENSLGIDSQIYLSMSDWYHRQMPDIIKDYMSPSNTNGDL
PSPDTILVNDTRSAPQFKFGAGKKYLIRISNIGGLACGQFHIQGYTLKVVEMDGVQIQPS
NADTIVLCAGQTIGVVVQGKTNPMGGANYIVKMTTDMLTGNIPSESARTVIGKLIYNLLG
SIIDFITDILTFNWQPASTFDDFSAKPLDGQKLLSPVDNKIELATNQTYFSGIGTRIGMG
AQPWVPAKVPSLYTALTTGSNAMDPATYGVGVEPHVVKSGQVIQIHYQNTHPYPHPMHLH
GHVFQIVAKGSGAWNGVESSLPNIPAKRDVAVVAANGYLVIRFKADNPGVWLFHCHIDLH
LVGGMAATIIEAPDLAQGILSVPAAGISNCQKGNRLYSGNCAGDQGAISASDSASKCNTV
LNSDGNNKGALIG

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	35	486	4e-93	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	1.14e-69	17	493	34	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].
274555	ascorbase	2.08e-66	18	494	1	526	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	1.67e-64	4	498	9	560	L-ascorbate oxidase
259920	CuRO_1_Fet3p	7.36e-63	19	137	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.
259966	CuRO_3_Fet3p	2.77e-60	338	493	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD07544.1|AA1_2	0.0	1	553	1	553
CAE7213185.1|AA1_2	7.85e-263	3	542	6	549
QDS68968.1|AA1_2	6.72e-158	4	526	8	519
AID53022.1|AA1	1.12e-136	122	414	1	296
AHZ65140.1|AA1_2	1.50e-133	16	524	7	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.29e-85	17	493	1	481	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]
3FPX_A	1.01e-60	22	510	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]
3PXL_A	1.40e-60	22	510	7	488	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
5LDU_A	3.79e-60	22	510	7	488	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
3V9E_A	3.85e-59	18	492	67	543	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|E9R598|FETC_ASPFU	7.62e-129	2	524	5	525	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	2.91e-127	13	524	17	528	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	6.46e-126	13	522	19	527	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	7.32e-111	16	524	20	521	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|P78591|FET3_CANAX	3.24e-98	4	522	9	529	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000359	0.999594	CS pos: 16-17. Pr: 0.9791

TMHMM  Annotations     

There is no transmembrane helices in QRD07544.1.