CAZyme Information: EPE05864.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE05864.1
• CAZy Family: GH2
• CAZyme Description: Iron transport multicopper oxidase fet3 [Source:UniProtKB/TrEMBL;Acc:S3BX81]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
676		75070.68	6.0330

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148155:945328-947517(+)

Full Sequence      

MPEEVIDQSERLLGLSGPGDLNENIAGGQTKGISASHEEEQGQPLWPAPGKRSHRHQKSA
VTRLWKLWQPVFVSGITILTAIIVVTALFKLLNTSALYELEIGKSSPIYSAADDGKSHSR
DPVIFLHPKDHIYRDAMTINMSWNITKARIAPDGVYRDVVHINGQFPGPTVEARSGDVFI
IEVFNCINESVSMHWHGLHMRGASHMDGPVGVNQCAIPPGGSFIYTVPTGDQAGTFWYHA
HSELHRADGMYGGLVIHVPAEVRPDRRVDSLVHGYDNEVLLLIGDWYHFSGKHMYDIFQD
PTSNGNEPVPDSVLINGMGAYDCSNAVKSAPVDCHTTAIPWFVLDKALRYRVRVVNVGSL
TGISTTVVDATMQTIQIDGGLPIAATEANSVGVVYPAQRVDYILSWPEGRAEADAELVVS
VDGEYYVGNWQDPPDRTYRIESASSGHRTTNRVAKKSLVAHLESRDIVVFDLREARGPDL
DTELPVPDKLYMIFANVEILSHNHFIPKGYINHTMWVPQETPLLALDRTLWDSHQLVPWT
GSEPVWVELTINNIDTQGHPFHLHGFDFYVVASHEGLGGWDYYNPFAVPWKLPRGGAMNV
VDPLKRDTIYVPLYGYAVLRFRADNEGIWVLHCHILWHQASGMNMAFQVMGDEHSHSQSA
AGRSAAEYCRSISSST

Enzyme Prediction     

No EC number prediction in EPE05864.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	155	644	6e-84	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259977	CuRO_3_MCO_like_4	1.02e-60	491	649	1	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.
274556	laccase	2.41e-53	157	649	22	519	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
225043	SufI	1.98e-52	162	653	57	451	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	5.92e-51	143	647	6	521	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.
215324	PLN02604	1.88e-50	135	648	21	545	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPX44859.1|AA1	2.91e-143	122	652	76	630
QLI63946.1|AA1	1.06e-140	105	649	55	625
UPK99837.1|AA1	4.84e-140	124	649	84	600
UNI19384.1|AA1	2.64e-138	115	649	163	710
QKX62088.1|AA1	7.43e-137	126	655	97	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.27e-50	144	647	73	540	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.29e-50	144	647	73	540	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3KW7_A	4.03e-50	145	647	10	470	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]
5EHF_A	3.67e-46	145	638	10	456	Laccase from Antrodiella faginea [Antrodiella faginea]
1AOZ_A	6.78e-46	142	647	7	521	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	1.15e-64	136	647	20	493	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	5.53e-62	136	647	22	494	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	5.60e-60	136	647	20	490	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|J9VQZ4|LAC2_CRYNH	1.07e-58	121	653	43	563	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|Q55P57|LAC1_CRYNB	1.75e-57	121	642	43	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999981	0.000051

TMHMM  Annotations     

Start	End
67	89