CAZyme Information: ZTRI_2.37.mRNA-p1

Basic Information

• Species: Zymoseptoria tritici
• Lineage: Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
• CAZyme ID: ZTRI_2.37.mRNA-p1
• CAZy Family: GH18
• CAZyme Description: similar to conidial pigment biosynthesis oxidase arb2 brown2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643		71609.17	6.6389

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ZtriticiIPO323	11839	336722	13	11826

• Gene Location: location=Ztri_chr_2:143780-146209(+)

Full Sequence      

MEHKYEIIVDKAANPIATTRKRGSWSLRGSVLPFITATTLLLWGAREIVQWNGVIIADCN
GSEIEASVRPVAQVVRRYNITVGVKWLNLDGGRWRPGFVCNGESPCPTLNAREGDQIELH
TTNDLPTQLSIHWSGMTHQRFGFENDGTGGLNQWAMLPRSNWTSHFDTSGHWGLNWYADH
TGAGVADGVYGTVWTAPSPSRPRPYTLIAGSPVHVRLIQEAEDDIQHMVLWNSDFRTADW
KIQKMKAKGTGLSCYKSILVNGKGRVFCKNPNYNTIDGHELDDAGCAVTPGIEPDACTPS
LADFTVIETHGKEYIMLNLINVGFEHALKWSVDNHRVWVVANDAGFIEPQLVDTVYITNG
ARVTVLLKLDQDPDDYAIRIASTSKLQNLEGYALLRYPAKRYPIYGQPMALPSIRANTKT
CLNPDSSVPHGCHEFDEYTARPFPAQIPDKTSNKTLLWTAGSQPSKYEQHVTEYYVNEKP
WQLFRAAMEPVYFTKDAASVAKPIQAGLPIGTVVDLIVQNTLNETIPLYKHGNPTFHLGS
RAFEKFEWSSIQDALEHHADININDPALAVVHDLPPLGWLAIRWRVTLTGATMFHAVKLR
YFALGMAAPMLEGIETSVRGSVSEYAKHQPHVMFEPGNDGVFG

Enzyme Prediction     

No EC number prediction in ZTRI_2.37.mRNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	95	607	1.5e-48	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	1.20e-60	226	398	1	138	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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.
274555	ascorbase	1.75e-31	101	615	26	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	5.87e-26	75	615	23	549	L-ascorbate oxidase
215324	PLN02604	1.18e-24	101	615	49	549	oxidoreductase
259919	CuRO_1_Abr2_like	2.27e-21	78	194	1	115	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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
SMQ47095.1|AA1	0.0	1	643	1	643
SMR45620.1|AA1	0.0	1	643	1	643
QKD61049.1|AA1	1.20e-213	74	643	62	639
CEI62062.1|AA1	1.28e-213	63	643	52	641
QPC70978.1|AA1	1.36e-210	63	643	52	641

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	5.17e-22	101	615	28	526	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]
3V9E_A	1.20e-18	74	612	66	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.79e-18	74	612	66	542	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]
1GW0_A	2.49e-17	78	612	38	519	Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],1GW0_B Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],2IH8_A A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH8_B A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH9_A A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],2IH9_B A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],3FU7_B Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_A Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_B Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3QPK_A Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces],3QPK_B Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces]
3DKH_A	2.49e-17	78	612	38	519	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	2.51e-79	71	636	18	584	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.47e-56	66	615	6	574	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|P17489|LAC1_EMENI	5.55e-43	90	615	37	605	Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3
sp|Q0UHZ8|ELCG_PHANO	6.64e-43	64	615	28	605	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	1.11e-40	94	615	33	591	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.990138	0.009869

TMHMM  Annotations     

There is no transmembrane helices in ZTRI_2.37.mRNA-p1.