CAZyme Information: EQL36678.1

Basic Information

• Species: Blastomyces dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces dermatitidis
• CAZyme ID: EQL36678.1
• CAZy Family: GT22
• CAZyme Description: hypothetical protein, variant 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		53775.55	8.4594

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BdermatitidisATCC26199	9560	447095	380	9180

• Gene Location: location=GL538369:724324-726176(-)

Full Sequence      

MDGTVGVTQCAINPGDSFRYDFTISDSQSGTYWYHAHSGLQRADGLYGGLVVHQPSPKAI
RGTQSRNAESDILKYKYQKEILLLVGDWYHRPADDVLKWYMRAASYGNEPVPDSLLVNGV
GRFDCARAVPARPIDCSSKTPMPHFMIDPTQSYRVRVVNTGSLAGFSLGFSQGNISLTHV
DGGLDVQHFKQSKASNSKSIGILYPGQRVDFILQHHQNARGKSSLTVELDPDCFKYPNPA
LSSAQAFPIYNANSNNIKTYSPQPLHIRSSTHINLTQVSSTAAVLSGLPPEAQQTYVIYT
KISQMSKNQNMPFGYFNQTSWRPQSDPPHPLVDLDPHHWDKNQFAISTGSKPVWIDLVVN
NLDEGPHPFHLHGHNFFILTIHSSSRGWGSYNPFSPHQQHQQYRPTSMDLARALLRDTVQ
IPPRGHAVLRFRADNPGIWLFHCHILWHLASGMAMVFDVMNGSQTGNGHGLAGGGAMEMC
RYL

Enzyme Prediction     

No EC number prediction in EQL36678.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	454	4.2e-70	0.835195530726257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259977	CuRO_3_MCO_like_4	2.16e-67	296	459	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.
274555	ascorbase	5.68e-51	2	457	71	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.
177843	PLN02191	1.89e-47	2	457	93	544	L-ascorbate oxidase
215324	PLN02604	1.59e-45	2	458	94	545	oxidoreductase
225043	SufI	6.83e-41	1	460	99	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
QSS75251.1|AA1	8.66e-311	1	483	1	483
QSS54105.1|AA1	1.52e-240	101	483	1	383
QVM10773.1|AA1	4.84e-180	64	483	2	411
BCS06095.1|AA1	9.97e-172	1	459	1	459
BCR93452.1|AA1	9.97e-172	1	459	1	459

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.70e-42	2	457	73	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]
1ZPU_A	5.24e-39	1	456	72	476	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	1.19e-33	2	457	137	540	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.98e-33	2	457	137	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]
1V10_A	1.12e-32	1	461	97	493	Chain A, Laccase [Rigidoporus microporus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	5.26e-51	1	457	94	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|K7NCS2|FETC_EPIFE	1.85e-49	1	457	92	493	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q6CII3|FET3_KLULA	8.71e-46	1	456	97	502	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|E9R598|FETC_ASPFU	1.39e-45	1	457	92	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|Q96WT3|FET3_CANGA	3.81e-43	1	480	89	521	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000001

TMHMM  Annotations     

There is no transmembrane helices in EQL36678.1.