CAZyme Information: SMR54715.1

Basic Information

• Species: Zymoseptoria tritici
• Lineage: Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
• CAZyme ID: SMR54715.1
• CAZy Family: GH31
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643		71969.62	6.4398

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ZtriticiST99CH3D1	11991	1276537	0	11991

• Gene Location: location=LT854277:2500111-2502307(-)

Full Sequence      

MSFVDMFPNQKKGEYALVEEKPPASVHKRGSKSIVTAFVVFAACAVLSIGSGFRKWYPTD
IATDWSLKASRQGQRVDYNLTLSQSWRNPDGGHWRPLFVGNSESPFATINCQEGDTLHIH
IQNDLGFPTQLHWVGVNHGSATWNDGSAGVTAYPILPRANWTSVIRTEGQWGLKWYLDHV
STPSVDGNYGTIWIRPAADRMRPYHLISSCKHEQQAMLDAEEKPAHVVMYNYQHREMPGL
LAQLQGEGYDPYCFQSVLINGKGRVHCRPAEVTALNGKSIDSHGCVYQPSGAIGYGQCEP
SNGDYEIIETENRRWMMMNFVNPGLEHPWRVSIDNHKMWIVANDGGFVQPQEVDIIQVTN
AERVTVMVKLDQEAADYPIRFHALSDLQTLQGYAILRYPHRRIGQRLGEPYPEPKQENSI
MALSGSPIGKAVLEDKSTLHPYPAQQPPEHADITLRFKATGAPDPYNPHITNCSLNGTSW
QIFRGLMHPMYLDPNQALPDAPDPAVRNLPLGSVVDIVLENDLPVALPMYKHNKALFLLG
SGEGKFGEADVAAATSTGSKSFNLKNPPLGYVHELPASGWMALRWKITEPAATMFHVFRV
RYFVLGMQVPLFEGDDYLPEVPDRVKNMPHVELDIPEHMGIFD

Enzyme Prediction     

No EC number prediction in SMR54715.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	94	607	4.2e-54	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	2.70e-63	225	399	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.
177843	PLN02191	2.45e-31	101	623	48	556	L-ascorbate oxidase
274555	ascorbase	1.46e-30	101	625	26	535	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	9.76e-23	101	622	49	555	oxidoreductase
259919	CuRO_1_Abr2_like	1.55e-22	78	195	1	117	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
SMR54715.1|AA1	0.0	1	643	1	643
SMQ51193.1|AA1	0.0	1	643	1	643
SMY24838.1|AA1	0.0	1	643	1	643
SMR53096.1|AA1	0.0	6	643	1	638
QBZ57870.1|AA1	1.88e-159	16	642	10	675

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	2.97e-22	80	613	9	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.99e-22	80	613	9	468	Chain A, Laccase [Coprinopsis cinerea]
1AOZ_A	6.87e-22	101	624	28	534	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]
3PPS_A	1.48e-21	22	613	23	560	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]
3V9E_A	2.93e-19	56	614	49	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|W3X732|PFMAY_PESFW	2.78e-100	78	643	25	592	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.42e-59	56	621	2	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	3.75e-58	46	623	12	612	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	2.07e-55	72	622	44	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|I1RF62|GIP1_GIBZE	7.77e-52	65	622	14	597	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
0.999943	0.000080

TMHMM  Annotations     

There is no transmembrane helices in SMR54715.1.