CAZyme Information: P170DRAFT_455674-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_455674-t37_1-p1
• CAZy Family: GH7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
629		71030.15	6.3542

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000004:715085-717387(-)

Full Sequence      

MERQSSRRRKPRQLQEESSCEDLHSNGKSQTAEREIRGLYSILFYPLIVCSLIVLVFLYQ
SKSSFFVLSQPHIPQLTSPGAHDPDVLRPKIELHPEDHVHRDPVTQYFEWTVTSDHLRPD
GVLKQIYLINGLFPGPTIEARTGDTLTINVTNNLQEPVSIHWHGLHIQNSMDGVPAVTQQ
PISPGSTFTYHFTIPLDQSGTFWYHAHSGVMRADGLYGGLVVHAPAPKSTVRGLMARGQS
VYEKELLILVGDWYHRPAEDVLAWFMSIESFGNEPAPDSLLINGVGAFNCSMAVPARPVN
CVQQQMDLSYLDLELDKGYRLRVVNTGSLAGFTLSFENHLFQLLEVDSINTALQEPSLAA
GILYPGQRMDILVEPSQNKNHQSSLTVHLDDECFNFPNPALTPVQRFFTSPSDENDFNSP
HDLTDISISTLDLSRIPSSQPTLSYLSQSRDLKPQVHVVYTKIQKLSINHNIPYGFFNHT
SWAPQRDPPLPLNILPKEKWDQNQFSISTTPASDTNTEPVWVDLVVNNLDEGGHPFHLHG
HHFYILRVHEASIGWGSFNPFEKIPSDSQNQHPDGYDFSRAMFRDTVYIPRRGHAVLRFR
ATNPGVWMFHCHIVWHLASGMAMLVHVEG

Enzyme Prediction     

No EC number prediction in P170DRAFT_455674-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	122	622	1.2e-95	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.01e-71	105	629	1	524	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	2.89e-65	108	629	26	547	L-ascorbate oxidase
215324	PLN02604	2.74e-61	105	621	24	540	oxidoreductase
259977	CuRO_3_MCO_like_4	1.25e-59	458	627	2	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.
225043	SufI	3.21e-59	108	628	36	449	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW37919.1|AA1	9.30e-258	42	627	24	598
QRD88142.1|AA1	4.87e-257	42	627	41	615
QMW25836.1|AA1	4.87e-257	42	627	41	615
CAK44017.1|AA1	1.02e-230	40	627	14	586
UPX44859.1|AA1	3.42e-223	87	629	74	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	7.02e-58	105	625	2	477	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]
3V9E_A	3.29e-57	104	623	66	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	8.68e-57	104	623	66	538	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]
1AOZ_A	1.42e-50	106	629	4	524	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]
3KW7_A	7.05e-49	103	624	4	469	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	4.71e-66	36	628	1	561	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	2.41e-64	36	628	1	561	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	4.46e-64	105	621	24	490	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|K7NCS2|FETC_EPIFE	1.65e-63	109	621	26	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	1.73e-61	105	622	22	487	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999965	0.000048

TMHMM  Annotations     

Start	End
38	60